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Database: PDB
Entry: 3E82
LinkDB: 3E82
Original site: 3E82 
HEADER    OXIDOREDUCTASE                          19-AUG-08   3E82              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE OXIDOREDUCTASE FROM KLEBSIELLA        
TITLE    2 PNEUMONIAE                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE OXIDOREDUCTASE;                                   
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH     
SOURCE   3 78578;                                                               
SOURCE   4 ORGANISM_TAXID: 272620;                                              
SOURCE   5 GENE: KPN78578_13420, KPN_01371;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)-CODON+RIL-STRATAGENE;           
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC), TOP10-INVITROGEN            
KEYWDS    NAD, GFO/IDH/MOCA FAMILY, PSI-2, NYSGXRC, 11136F, STRUCTURAL          
KEYWDS   2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER 
KEYWDS   3 FOR STRUCTURAL GENOMICS, OXIDOREDUCTASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ESWARAMOORTHY,M.B.MOHAMMAD,C.A.THOMAS,A.C.BROWN,S.K.BURLEY,         
AUTHOR   2 S.SWAMINATHAN,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS   
AUTHOR   3 (NYSGXRC)                                                            
REVDAT   3   10-FEB-21 3E82    1       AUTHOR JRNL   REMARK LINK                
REVDAT   2   24-FEB-09 3E82    1       VERSN                                    
REVDAT   1   26-AUG-08 3E82    0                                                
JRNL        AUTH   S.ESWARAMOORTHY,M.B.MOHAMMAD,C.A.THOMAS,A.C.BROWN,           
JRNL        AUTH 2 S.K.BURLEY,S.SWAMINATHAN                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE OXIDOREDUCTASE FROM          
JRNL        TITL 2 KLEBSIELLA PNEUMONIAE                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 103973                         
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 SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4166                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.2850                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 616                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10670                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 684                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.30000                                              
REMARK   3    B22 (A**2) : 4.66000                                              
REMARK   3    B33 (A**2) : -5.96000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.39000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3E82 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048992.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109371                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56000                            
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: SAD                          
REMARK 200 SOFTWARE USED: SHELX & SHARP                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BIS-TRIS, PH 5.5,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.87500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E                                  
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     MSE A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     ARG A   171                                                      
REMARK 465     VAL A   172                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     TRP A   174                                                      
REMARK 465     ARG A   175                                                      
REMARK 465     GLU A   176                                                      
REMARK 465     GLN A   177                                                      
REMARK 465     ASN A   178                                                      
REMARK 465     VAL A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     HIS A   372                                                      
REMARK 465     MSE B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     ARG B   171                                                      
REMARK 465     VAL B   172                                                      
REMARK 465     ARG B   173                                                      
REMARK 465     TRP B   174                                                      
REMARK 465     ARG B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     GLN B   177                                                      
REMARK 465     ASN B   178                                                      
REMARK 465     VAL B   179                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     HIS B   369                                                      
REMARK 465     HIS B   370                                                      
REMARK 465     HIS B   371                                                      
REMARK 465     HIS B   372                                                      
REMARK 465     MSE D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     ASN D    13                                                      
REMARK 465     ASN D    14                                                      
REMARK 465     GLN D   177                                                      
REMARK 465     ASN D   178                                                      
REMARK 465     VAL D   179                                                      
REMARK 465     PRO D   180                                                      
REMARK 465     HIS D   369                                                      
REMARK 465     HIS D   370                                                      
REMARK 465     HIS D   371                                                      
REMARK 465     HIS D   372                                                      
REMARK 465     MSE E     9                                                      
REMARK 465     SER E    10                                                      
REMARK 465     LEU E    11                                                      
REMARK 465     SER E    12                                                      
REMARK 465     VAL E   170                                                      
REMARK 465     ARG E   171                                                      
REMARK 465     VAL E   172                                                      
REMARK 465     ARG E   173                                                      
REMARK 465     TRP E   174                                                      
REMARK 465     ARG E   175                                                      
REMARK 465     GLU E   176                                                      
REMARK 465     GLN E   177                                                      
REMARK 465     ASN E   178                                                      
REMARK 465     VAL E   179                                                      
REMARK 465     PRO E   180                                                      
REMARK 465     GLY E   181                                                      
REMARK 465     HIS E   369                                                      
REMARK 465     HIS E   370                                                      
REMARK 465     HIS E   371                                                      
REMARK 465     HIS E   372                                                      
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     ARG E 165    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E 167    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 169    CG   CD   OE1  OE2                                  
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    PHE A  30      -67.66   -105.34                                   
REMARK 500    ASP A 306       96.72   -164.83                                   
REMARK 500    HIS A 367       15.97    -59.60                                   
REMARK 500    PHE B  30      -74.93   -104.55                                   
REMARK 500    LEU B  58       74.38   -117.79                                   
REMARK 500    ASP B 306       95.50   -161.91                                   
REMARK 500    PHE D  30      -66.59   -102.38                                   
REMARK 500    ASP D  75       41.94    -80.86                                   
REMARK 500    ASN D  97        2.23    -68.95                                   
REMARK 500    SER D 294       -3.94    170.20                                   
REMARK 500    LEU D 295       -2.97     60.17                                   
REMARK 500    ASP D 306       92.13   -170.52                                   
REMARK 500    SER D 356      171.66    -52.65                                   
REMARK 500    ASN E  14       52.78     94.86                                   
REMARK 500    PHE E  30      -67.22   -105.86                                   
REMARK 500    ASP E  75       49.88   -104.01                                   
REMARK 500    ASP E 306       93.07   -170.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-11136F   RELATED DB: TARGETDB                    
DBREF  3E82 A   12   364  UNP    A6T882   A6T882_KLEP7    12    364             
DBREF  3E82 B   12   364  UNP    A6T882   A6T882_KLEP7    12    364             
DBREF  3E82 D   12   364  UNP    A6T882   A6T882_KLEP7    12    364             
DBREF  3E82 E   12   364  UNP    A6T882   A6T882_KLEP7    12    364             
SEQADV 3E82 MSE A    9  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 SER A   10  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 LEU A   11  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLU A  365  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLY A  366  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  367  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  368  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  369  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  370  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  371  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS A  372  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 MSE B    9  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 SER B   10  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 LEU B   11  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLU B  365  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLY B  366  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  367  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  368  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  369  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  370  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  371  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS B  372  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 MSE D    9  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 SER D   10  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 LEU D   11  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLU D  365  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLY D  366  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  367  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  368  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  369  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  370  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  371  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS D  372  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 MSE E    9  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 SER E   10  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 LEU E   11  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLU E  365  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 GLY E  366  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  367  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  368  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  369  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  370  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  371  UNP  A6T882              EXPRESSION TAG                 
SEQADV 3E82 HIS E  372  UNP  A6T882              EXPRESSION TAG                 
SEQRES   1 A  364  MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE          
SEQRES   2 A  364  GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU          
SEQRES   3 A  364  ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA          
SEQRES   4 A  364  SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP          
SEQRES   5 A  364  VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS          
SEQRES   6 A  364  PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA          
SEQRES   7 A  364  THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY          
SEQRES   8 A  364  LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE          
SEQRES   9 A  364  GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS          
SEQRES  10 A  364  GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP          
SEQRES  11 A  364  SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY          
SEQRES  12 A  364  THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP          
SEQRES  13 A  364  ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN          
SEQRES  14 A  364  ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO          
SEQRES  15 A  364  HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO          
SEQRES  16 A  364  GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY          
SEQRES  17 A  364  ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR          
SEQRES  18 A  364  PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL          
SEQRES  19 A  364  ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS          
SEQRES  20 A  364  GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER          
SEQRES  21 A  364  GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP          
SEQRES  22 A  364  GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER          
SEQRES  23 A  364  LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN          
SEQRES  24 A  364  ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY          
SEQRES  25 A  364  GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA          
SEQRES  26 A  364  VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU          
SEQRES  27 A  364  SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU          
SEQRES  28 A  364  ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  364  MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE          
SEQRES   2 B  364  GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU          
SEQRES   3 B  364  ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA          
SEQRES   4 B  364  SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP          
SEQRES   5 B  364  VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS          
SEQRES   6 B  364  PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA          
SEQRES   7 B  364  THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY          
SEQRES   8 B  364  LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE          
SEQRES   9 B  364  GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS          
SEQRES  10 B  364  GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP          
SEQRES  11 B  364  SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY          
SEQRES  12 B  364  THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP          
SEQRES  13 B  364  ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN          
SEQRES  14 B  364  ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO          
SEQRES  15 B  364  HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO          
SEQRES  16 B  364  GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY          
SEQRES  17 B  364  ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR          
SEQRES  18 B  364  PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL          
SEQRES  19 B  364  ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS          
SEQRES  20 B  364  GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER          
SEQRES  21 B  364  GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP          
SEQRES  22 B  364  GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER          
SEQRES  23 B  364  LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN          
SEQRES  24 B  364  ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY          
SEQRES  25 B  364  GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA          
SEQRES  26 B  364  VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU          
SEQRES  27 B  364  SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU          
SEQRES  28 B  364  ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  364  MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE          
SEQRES   2 D  364  GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU          
SEQRES   3 D  364  ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA          
SEQRES   4 D  364  SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP          
SEQRES   5 D  364  VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS          
SEQRES   6 D  364  PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA          
SEQRES   7 D  364  THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY          
SEQRES   8 D  364  LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE          
SEQRES   9 D  364  GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS          
SEQRES  10 D  364  GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP          
SEQRES  11 D  364  SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY          
SEQRES  12 D  364  THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP          
SEQRES  13 D  364  ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN          
SEQRES  14 D  364  ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO          
SEQRES  15 D  364  HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO          
SEQRES  16 D  364  GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY          
SEQRES  17 D  364  ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR          
SEQRES  18 D  364  PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL          
SEQRES  19 D  364  ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS          
SEQRES  20 D  364  GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER          
SEQRES  21 D  364  GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP          
SEQRES  22 D  364  GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER          
SEQRES  23 D  364  LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN          
SEQRES  24 D  364  ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY          
SEQRES  25 D  364  GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA          
SEQRES  26 D  364  VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU          
SEQRES  27 D  364  SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU          
SEQRES  28 D  364  ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 E  364  MSE SER LEU SER ASN ASN THR ILE ASN ILE ALA LEU ILE          
SEQRES   2 E  364  GLY TYR GLY PHE VAL GLY LYS THR PHE HIS ALA PRO LEU          
SEQRES   3 E  364  ILE ARG SER VAL PRO GLY LEU ASN LEU ALA PHE VAL ALA          
SEQRES   4 E  364  SER ARG ASP GLU GLU LYS VAL LYS ARG ASP LEU PRO ASP          
SEQRES   5 E  364  VAL THR VAL ILE ALA SER PRO GLU ALA ALA VAL GLN HIS          
SEQRES   6 E  364  PRO ASP VAL ASP LEU VAL VAL ILE ALA SER PRO ASN ALA          
SEQRES   7 E  364  THR HIS ALA PRO LEU ALA ARG LEU ALA LEU ASN ALA GLY          
SEQRES   8 E  364  LYS HIS VAL VAL VAL ASP LYS PRO PHE THR LEU ASP MSE          
SEQRES   9 E  364  GLN GLU ALA ARG GLU LEU ILE ALA LEU ALA GLU GLU LYS          
SEQRES  10 E  364  GLN ARG LEU LEU SER VAL PHE HIS ASN ARG ARG TRP ASP          
SEQRES  11 E  364  SER ASP TYR LEU GLY ILE ARG GLN VAL ILE GLU GLN GLY          
SEQRES  12 E  364  THR LEU GLY ALA VAL LYS HIS PHE GLU SER HIS PHE ASP          
SEQRES  13 E  364  ARG PHE ARG PRO GLU VAL ARG VAL ARG TRP ARG GLU GLN          
SEQRES  14 E  364  ASN VAL PRO GLY SER GLY LEU TRP PHE ASP LEU GLY PRO          
SEQRES  15 E  364  HIS LEU ILE ASP GLN ALA LEU GLN LEU PHE GLY LEU PRO          
SEQRES  16 E  364  GLN SER VAL GLN GLY ASN ILE ALA THR LEU ARG ASP GLY          
SEQRES  17 E  364  ALA GLU ILE ASN ASP TRP ALA HIS VAL VAL LEU ASN TYR          
SEQRES  18 E  364  PRO ALA HIS LYS VAL ILE LEU HIS CYS SER MSE LEU VAL          
SEQRES  19 E  364  ALA GLY GLY SER SER ARG PHE THR VAL HIS GLY ASP LYS          
SEQRES  20 E  364  GLY SER VAL ILE LYS ALA ARG ALA ASP GLN GLN GLU SER          
SEQRES  21 E  364  GLN LEU LEU ALA GLY VAL VAL PRO GLY SER ALA ASP TRP          
SEQRES  22 E  364  GLY GLN ASP ASP ASP PRO LEU VAL ILE TYR ASP ALA SER          
SEQRES  23 E  364  LEU GLN ALA HIS ALA GLN ALA THR PRO GLN GLY ASP GLN          
SEQRES  24 E  364  ARG GLN TYR TYR MSE LEU ILE ARG ASP ALA LEU LYS GLY          
SEQRES  25 E  364  GLN ILE ALA ASN PRO VAL PRO PRO VAL GLU ALA LEU ALA          
SEQRES  26 E  364  VAL MSE ALA VAL LEU GLU ALA ALA VAL ARG SER ALA GLU          
SEQRES  27 E  364  SER GLY MSE VAL GLN THR LEU ASP LEU SER ASP ASP GLU          
SEQRES  28 E  364  ARG ASN THR LEU ARG GLU GLY HIS HIS HIS HIS HIS HIS          
MODRES 3E82 MSE A  112  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE A  312  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE A  335  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE A  349  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE B  112  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE B  240  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE B  312  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE B  335  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE B  349  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE D  112  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE D  240  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE D  312  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE D  335  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE D  349  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE E  112  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE E  240  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE E  312  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE E  335  MET  SELENOMETHIONINE                                   
MODRES 3E82 MSE E  349  MET  SELENOMETHIONINE                                   
HET    MSE  A 112       8                                                       
HET    MSE  A 240       8                                                       
HET    MSE  A 312       8                                                       
HET    MSE  A 335       8                                                       
HET    MSE  A 349       8                                                       
HET    MSE  B 112       8                                                       
HET    MSE  B 240       8                                                       
HET    MSE  B 312       8                                                       
HET    MSE  B 335       8                                                       
HET    MSE  B 349       8                                                       
HET    MSE  D 112       8                                                       
HET    MSE  D 240       8                                                       
HET    MSE  D 312       8                                                       
HET    MSE  D 335       8                                                       
HET    MSE  D 349       8                                                       
HET    MSE  E 112       8                                                       
HET    MSE  E 240       8                                                       
HET    MSE  E 312       8                                                       
HET    MSE  E 335       8                                                       
HET    MSE  E 349       8                                                       
HET     CL  A   1       1                                                       
HET     CL  B   2       1                                                       
HET     CL  D   3       1                                                       
HET     CL  E   4       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   9  HOH   *684(H2 O)                                                    
HELIX    1   1 GLY A   24  PHE A   30  1                                   7    
HELIX    2   2 PHE A   30  SER A   37  1                                   8    
HELIX    3   3 ASP A   50  LEU A   58  1                                   9    
HELIX    4   4 SER A   66  GLN A   72  1                                   7    
HELIX    5   5 PRO A   84  ALA A   86  5                                   3    
HELIX    6   6 THR A   87  ALA A   98  1                                  12    
HELIX    7   7 ASP A  111  LYS A  125  1                                  15    
HELIX    8   8 ASP A  138  GLY A  151  1                                  14    
HELIX    9   9 GLY A  183  GLY A  201  1                                  19    
HELIX   10  10 GLN A  265  GLY A  273  1                                   9    
HELIX   11  11 GLN A  307  LYS A  319  1                                  13    
HELIX   12  12 PRO A  327  GLY A  348  1                                  22    
HELIX   13  13 SER A  356  HIS A  367  1                                  12    
HELIX   14  14 GLY B   24  PHE B   30  1                                   7    
HELIX   15  15 PHE B   30  SER B   37  1                                   8    
HELIX   16  16 ASP B   50  LEU B   58  1                                   9    
HELIX   17  17 SER B   66  HIS B   73  1                                   8    
HELIX   18  18 PRO B   84  ALA B   86  5                                   3    
HELIX   19  19 THR B   87  ALA B   98  1                                  12    
HELIX   20  20 ASP B  111  LYS B  125  1                                  15    
HELIX   21  21 ASP B  138  GLY B  151  1                                  14    
HELIX   22  22 GLY B  183  GLY B  201  1                                  19    
HELIX   23  23 GLN B  265  ALA B  272  1                                   8    
HELIX   24  24 GLN B  307  LYS B  319  1                                  13    
HELIX   25  25 PRO B  327  GLY B  348  1                                  22    
HELIX   26  26 SER B  356  GLU B  365  1                                  10    
HELIX   27  27 GLY D   24  PHE D   30  1                                   7    
HELIX   28  28 PHE D   30  SER D   37  1                                   8    
HELIX   29  29 ASP D   50  LEU D   58  1                                   9    
HELIX   30  30 SER D   66  GLN D   72  1                                   7    
HELIX   31  31 PRO D   84  ALA D   86  5                                   3    
HELIX   32  32 THR D   87  ASN D   97  1                                  11    
HELIX   33  33 ASP D  111  LYS D  125  1                                  15    
HELIX   34  34 ASP D  138  GLN D  150  1                                  13    
HELIX   35  35 GLY D  183  GLY D  201  1                                  19    
HELIX   36  36 GLN D  265  ALA D  272  1                                   8    
HELIX   37  37 GLN D  307  LYS D  319  1                                  13    
HELIX   38  38 PRO D  327  GLY D  348  1                                  22    
HELIX   39  39 SER D  356  HIS D  367  1                                  12    
HELIX   40  40 GLY E   24  PHE E   30  1                                   7    
HELIX   41  41 PHE E   30  SER E   37  1                                   8    
HELIX   42  42 ASP E   50  ARG E   56  1                                   7    
HELIX   43  43 SER E   66  GLN E   72  1                                   7    
HELIX   44  44 PRO E   84  ALA E   86  5                                   3    
HELIX   45  45 THR E   87  ALA E   98  1                                  12    
HELIX   46  46 ASP E  111  LYS E  125  1                                  15    
HELIX   47  47 HIS E  133  TRP E  137  5                                   5    
HELIX   48  48 ASP E  138  GLN E  150  1                                  13    
HELIX   49  49 GLY E  183  GLY E  201  1                                  19    
HELIX   50  50 GLN E  265  GLY E  273  1                                   9    
HELIX   51  51 GLN E  307  LYS E  319  1                                  13    
HELIX   52  52 PRO E  327  GLY E  348  1                                  22    
HELIX   53  53 SER E  356  HIS E  368  1                                  13    
SHEET    1   A 6 THR A  62  ILE A  64  0                                        
SHEET    2   A 6 LEU A  41  ALA A  47  1  N  ALA A  44   O  THR A  62           
SHEET    3   A 6 ILE A  16  ILE A  21  1  N  ILE A  16   O  ASN A  42           
SHEET    4   A 6 LEU A  78  ILE A  81  1  O  VAL A  80   N  ILE A  21           
SHEET    5   A 6 HIS A 101  VAL A 104  1  O  HIS A 101   N  VAL A  79           
SHEET    6   A 6 LEU A 129  VAL A 131  1  O  SER A 130   N  VAL A 104           
SHEET    1   B 8 SER A 205  ALA A 211  0                                        
SHEET    2   B 8 TRP A 222  ASN A 228 -1  O  TRP A 222   N  ALA A 211           
SHEET    3   B 8 LYS A 233  SER A 239 -1  O  LEU A 236   N  VAL A 225           
SHEET    4   B 8 VAL A 156  ASP A 164  1  N  PHE A 159   O  ILE A 235           
SHEET    5   B 8 PHE A 249  GLY A 253 -1  O  HIS A 252   N  HIS A 158           
SHEET    6   B 8 GLY A 256  LYS A 260 -1  O  VAL A 258   N  VAL A 251           
SHEET    7   B 8 LEU A 288  ASP A 292 -1  O  TYR A 291   N  SER A 257           
SHEET    8   B 8 ALA A 297  GLN A 300 -1  O  HIS A 298   N  ILE A 290           
SHEET    1   C 6 THR B  62  ILE B  64  0                                        
SHEET    2   C 6 LEU B  41  ALA B  47  1  N  ALA B  44   O  THR B  62           
SHEET    3   C 6 ILE B  16  ILE B  21  1  N  ILE B  18   O  ASN B  42           
SHEET    4   C 6 LEU B  78  ILE B  81  1  O  VAL B  80   N  ILE B  21           
SHEET    5   C 6 HIS B 101  VAL B 104  1  O  HIS B 101   N  VAL B  79           
SHEET    6   C 6 LEU B 129  VAL B 131  1  O  SER B 130   N  VAL B 104           
SHEET    1   D 8 SER B 205  ALA B 211  0                                        
SHEET    2   D 8 TRP B 222  ASN B 228 -1  O  TRP B 222   N  ALA B 211           
SHEET    3   D 8 LYS B 233  SER B 239 -1  O  LEU B 236   N  VAL B 225           
SHEET    4   D 8 VAL B 156  ASP B 164  1  N  PHE B 159   O  ILE B 235           
SHEET    5   D 8 PHE B 249  GLY B 253 -1  O  HIS B 252   N  HIS B 158           
SHEET    6   D 8 GLY B 256  LYS B 260 -1  O  GLY B 256   N  GLY B 253           
SHEET    7   D 8 LEU B 288  ASP B 292 -1  O  TYR B 291   N  SER B 257           
SHEET    8   D 8 ALA B 297  GLN B 300 -1  O  HIS B 298   N  ILE B 290           
SHEET    1   E 5 LEU D  41  ALA D  47  0                                        
SHEET    2   E 5 ILE D  16  ILE D  21  1  N  LEU D  20   O  ALA D  47           
SHEET    3   E 5 LEU D  78  ILE D  81  1  O  VAL D  80   N  ILE D  21           
SHEET    4   E 5 HIS D 101  VAL D 104  1  O  VAL D 103   N  ILE D  81           
SHEET    5   E 5 LEU D 129  VAL D 131  1  O  SER D 130   N  VAL D 104           
SHEET    1   F 8 SER D 205  ALA D 211  0                                        
SHEET    2   F 8 TRP D 222  TYR D 229 -1  O  TRP D 222   N  ALA D 211           
SHEET    3   F 8 HIS D 232  SER D 239 -1  O  LEU D 236   N  VAL D 225           
SHEET    4   F 8 VAL D 156  ASP D 164  1  N  PHE D 159   O  ILE D 235           
SHEET    5   F 8 PHE D 249  GLY D 253 -1  O  THR D 250   N  GLU D 160           
SHEET    6   F 8 SER D 257  LYS D 260 -1  O  LYS D 260   N  PHE D 249           
SHEET    7   F 8 LEU D 288  TYR D 291 -1  O  TYR D 291   N  SER D 257           
SHEET    8   F 8 ALA D 297  GLN D 300 -1  O  GLN D 300   N  LEU D 288           
SHEET    1   G 6 THR E  62  ILE E  64  0                                        
SHEET    2   G 6 LEU E  41  ALA E  47  1  N  VAL E  46   O  THR E  62           
SHEET    3   G 6 ILE E  16  ILE E  21  1  N  ILE E  18   O  ASN E  42           
SHEET    4   G 6 LEU E  78  ILE E  81  1  O  VAL E  80   N  ILE E  21           
SHEET    5   G 6 HIS E 101  VAL E 104  1  O  VAL E 103   N  VAL E  79           
SHEET    6   G 6 LEU E 129  VAL E 131  1  O  SER E 130   N  VAL E 104           
SHEET    1   H 8 SER E 205  ALA E 211  0                                        
SHEET    2   H 8 TRP E 222  ASN E 228 -1  O  VAL E 226   N  GLN E 207           
SHEET    3   H 8 LYS E 233  SER E 239 -1  O  LEU E 236   N  VAL E 225           
SHEET    4   H 8 VAL E 156  ASP E 164  1  N  PHE E 159   O  ILE E 235           
SHEET    5   H 8 PHE E 249  GLY E 253 -1  O  HIS E 252   N  HIS E 158           
SHEET    6   H 8 SER E 257  LYS E 260 -1  O  VAL E 258   N  VAL E 251           
SHEET    7   H 8 LEU E 288  TYR E 291 -1  O  VAL E 289   N  ILE E 259           
SHEET    8   H 8 ALA E 297  GLN E 300 -1  O  GLN E 300   N  LEU E 288           
LINK         C   ASP A 111                 N   MSE A 112     1555   1555  1.33  
LINK         C   MSE A 112                 N   GLN A 113     1555   1555  1.33  
LINK         C   SER A 239                 N   MSE A 240     1555   1555  1.33  
LINK         C   MSE A 240                 N   LEU A 241     1555   1555  1.33  
LINK         C   TYR A 311                 N   MSE A 312     1555   1555  1.33  
LINK         C   MSE A 312                 N   LEU A 313     1555   1555  1.33  
LINK         C   VAL A 334                 N   MSE A 335     1555   1555  1.33  
LINK         C   MSE A 335                 N   ALA A 336     1555   1555  1.33  
LINK         C   GLY A 348                 N   MSE A 349     1555   1555  1.33  
LINK         C   MSE A 349                 N   VAL A 350     1555   1555  1.33  
LINK         C   ASP B 111                 N   MSE B 112     1555   1555  1.33  
LINK         C   MSE B 112                 N   GLN B 113     1555   1555  1.33  
LINK         C   SER B 239                 N   MSE B 240     1555   1555  1.33  
LINK         C   MSE B 240                 N   LEU B 241     1555   1555  1.33  
LINK         C   TYR B 311                 N   MSE B 312     1555   1555  1.33  
LINK         C   MSE B 312                 N   LEU B 313     1555   1555  1.33  
LINK         C   VAL B 334                 N   MSE B 335     1555   1555  1.33  
LINK         C   MSE B 335                 N   ALA B 336     1555   1555  1.33  
LINK         C   GLY B 348                 N   MSE B 349     1555   1555  1.33  
LINK         C   MSE B 349                 N   VAL B 350     1555   1555  1.34  
LINK         C   ASP D 111                 N   MSE D 112     1555   1555  1.33  
LINK         C   MSE D 112                 N   GLN D 113     1555   1555  1.33  
LINK         C   SER D 239                 N   MSE D 240     1555   1555  1.33  
LINK         C   MSE D 240                 N   LEU D 241     1555   1555  1.33  
LINK         C   TYR D 311                 N   MSE D 312     1555   1555  1.33  
LINK         C   MSE D 312                 N   LEU D 313     1555   1555  1.33  
LINK         C   VAL D 334                 N   MSE D 335     1555   1555  1.33  
LINK         C   MSE D 335                 N   ALA D 336     1555   1555  1.33  
LINK         C   GLY D 348                 N   MSE D 349     1555   1555  1.33  
LINK         C   MSE D 349                 N   VAL D 350     1555   1555  1.33  
LINK         C   ASP E 111                 N   MSE E 112     1555   1555  1.33  
LINK         C   MSE E 112                 N   GLN E 113     1555   1555  1.33  
LINK         C   SER E 239                 N   MSE E 240     1555   1555  1.33  
LINK         C   MSE E 240                 N   LEU E 241     1555   1555  1.33  
LINK         C   TYR E 311                 N   MSE E 312     1555   1555  1.33  
LINK         C   MSE E 312                 N   LEU E 313     1555   1555  1.33  
LINK         C   VAL E 334                 N   MSE E 335     1555   1555  1.33  
LINK         C   MSE E 335                 N   ALA E 336     1555   1555  1.33  
LINK         C   GLY E 348                 N   MSE E 349     1555   1555  1.33  
LINK         C   MSE E 349                 N   VAL E 350     1555   1555  1.33  
CISPEP   1 LYS A  106    PRO A  107          0        -0.40                     
CISPEP   2 LYS B  106    PRO B  107          0        -0.93                     
CISPEP   3 LYS D  106    PRO D  107          0        -0.30                     
CISPEP   4 LYS E  106    PRO E  107          0        -0.09                     
SITE     1 AC1  3 LYS A 106  HIS A 133  HIS A 191                               
SITE     1 AC2  4 LYS B 106  HIS B 133  HIS B 191  HOH B 425                    
SITE     1 AC3  4 LYS D 106  HIS D 133  HIS D 191  HOH D 392                    
SITE     1 AC4  4 LYS E 106  HIS E 133  HIS E 191  HOH E 427                    
CRYST1   52.910   79.750  209.144  90.00  94.00  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018900  0.000000  0.001322        0.00000                         
SCALE2      0.000000  0.012539  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004793        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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