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Database: PDB
Entry: 5BPK
LinkDB: 5BPK
Original site: 5BPK 
HEADER    HYDROLASE                               28-MAY-15   5BPK              
TITLE     VARYING BINDING MODES OF INHIBITORS AND STRUCTURAL DIFFERENCES IN THE 
TITLE    2 BINDING POCKETS OF DIFFERENT GAMMA-GLUTAMYLTRANSPEPTIDASES           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE (GGT);                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 1-379;                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE (GGT);                        
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 380-567;                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI 26695;                      
SOURCE   3 ORGANISM_TAXID: 85962;                                               
SOURCE   4 GENE: HP_1118;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI 26695;                      
SOURCE   9 ORGANISM_TAXID: 85962;                                               
SOURCE  10 STRAIN: / 26695;                                                     
SOURCE  11 GENE: HP_1118;                                                       
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    GAMMA-GLUTAMYLTRANSPEPTIDASE, NTN-HYDROLASE, ACIVICIN, PROTEROS       
KEYWDS   2 BIOSTRUCTURES GMBH, HYDROLASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.BOLZ,N.C.BACH,H.MEYER,G.MUELLER,M.DAWIDOWSKI,G.POPOWICZ,S.A.SIEBER, 
AUTHOR   2 A.SKERRA,M.GERHARD                                                   
REVDAT   1   18-MAY-16 5BPK    0                                                
JRNL        AUTH   C.BOLZ,N.C.BACH,H.MEYER,G.MUELLER,M.DAWIDOWSKI,G.POPOWICZ,   
JRNL        AUTH 2 S.A.SIEBER,A.SKERRA,M.GERHARD                                
JRNL        TITL   VARYING BINDING MODES OF INHIBITORS AND STRUCTURAL           
JRNL        TITL 2 DIFFERENCES IN THE BINDING POCKETS OF DIFFERENT              
JRNL        TITL 3 GAMMA-GLUTAMYLTRANSPEPTIDASES                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 170766                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.145                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4718                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12465                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 363                          
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8142                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 958                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.49000                                             
REMARK   3    B22 (A**2) : 0.84000                                              
REMARK   3    B33 (A**2) : -0.33000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.53000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.072         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.065         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.043         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.592         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8609 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5946 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11576 ; 1.221 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14601 ; 0.871 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1101 ; 6.192 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   333 ;37.078 ;25.195       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1486 ;12.107 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    29 ;16.768 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1286 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9501 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1582 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5418 ; 2.289 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2223 ; 1.211 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8717 ; 3.114 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3191 ; 4.219 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2859 ; 5.766 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2): 14555 ; 2.009 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   961 ; 8.961 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2): 14423 ; 4.463 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5BPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210322.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 176874                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 2NQO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, 0.1M TRIS, VAPOR DIFFUSION,     
REMARK 280  TEMPERATURE 293K                                                    
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       56.00300            
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: 15670 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14240 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LYS A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     PHE A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ASN A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     GLU A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     ASN A   379                                                      
REMARK 465     GLY C   568                                                      
REMARK 465     THR C   569                                                      
REMARK 465     GLY C   570                                                      
REMARK 465     SER C   571                                                      
REMARK 465     LYS C   572                                                      
REMARK 465     LEU C   573                                                      
REMARK 465     ALA C   574                                                      
REMARK 465     ALA C   575                                                      
REMARK 465     ALA C   576                                                      
REMARK 465     GLN C   577                                                      
REMARK 465     LEU C   578                                                      
REMARK 465     TYR C   579                                                      
REMARK 465     THR C   580                                                      
REMARK 465     ARG C   581                                                      
REMARK 465     ALA C   582                                                      
REMARK 465     SER C   583                                                      
REMARK 465     GLN C   584                                                      
REMARK 465     PRO C   585                                                      
REMARK 465     GLU C   586                                                      
REMARK 465     LEU C   587                                                      
REMARK 465     ALA C   588                                                      
REMARK 465     PRO C   589                                                      
REMARK 465     GLU C   590                                                      
REMARK 465     ASP C   591                                                      
REMARK 465     PRO C   592                                                      
REMARK 465     GLU C   593                                                      
REMARK 465     ASP C   594                                                      
REMARK 465     LEU C   595                                                      
REMARK 465     GLU C   596                                                      
REMARK 465     HIS C   597                                                      
REMARK 465     HIS C   598                                                      
REMARK 465     HIS C   599                                                      
REMARK 465     HIS C   600                                                      
REMARK 465     HIS C   601                                                      
REMARK 465     HIS C   602                                                      
REMARK 465     HIS C   603                                                      
REMARK 465     HIS C   604                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     PHE B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     LYS B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     ILE B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     VAL B    13                                                      
REMARK 465     ILE B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     PHE B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     ASN B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     ALA B    26                                                      
REMARK 465     HIS B   375                                                      
REMARK 465     GLU B   376                                                      
REMARK 465     GLY B   377                                                      
REMARK 465     SER B   378                                                      
REMARK 465     ASN B   379                                                      
REMARK 465     GLY D   568                                                      
REMARK 465     THR D   569                                                      
REMARK 465     GLY D   570                                                      
REMARK 465     SER D   571                                                      
REMARK 465     LYS D   572                                                      
REMARK 465     LEU D   573                                                      
REMARK 465     ALA D   574                                                      
REMARK 465     ALA D   575                                                      
REMARK 465     ALA D   576                                                      
REMARK 465     GLN D   577                                                      
REMARK 465     LEU D   578                                                      
REMARK 465     TYR D   579                                                      
REMARK 465     THR D   580                                                      
REMARK 465     ARG D   581                                                      
REMARK 465     ALA D   582                                                      
REMARK 465     SER D   583                                                      
REMARK 465     GLN D   584                                                      
REMARK 465     PRO D   585                                                      
REMARK 465     GLU D   586                                                      
REMARK 465     LEU D   587                                                      
REMARK 465     ALA D   588                                                      
REMARK 465     PRO D   589                                                      
REMARK 465     GLU D   590                                                      
REMARK 465     ASP D   591                                                      
REMARK 465     PRO D   592                                                      
REMARK 465     GLU D   593                                                      
REMARK 465     ASP D   594                                                      
REMARK 465     LEU D   595                                                      
REMARK 465     GLU D   596                                                      
REMARK 465     HIS D   597                                                      
REMARK 465     HIS D   598                                                      
REMARK 465     HIS D   599                                                      
REMARK 465     HIS D   600                                                      
REMARK 465     HIS D   601                                                      
REMARK 465     HIS D   602                                                      
REMARK 465     HIS D   603                                                      
REMARK 465     HIS D   604                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   36   CD   CE   NZ                                        
REMARK 480     LYS A   53   CE   NZ                                             
REMARK 480     LYS A  118   CD   CE   NZ                                        
REMARK 480     LYS A  154   CD   CE   NZ                                        
REMARK 480     LYS A  200   CE   NZ                                             
REMARK 480     LYS A  229   CD   CE   NZ                                        
REMARK 480     LYS A  245   CD   CE   NZ                                        
REMARK 480     LYS A  368   CD   CE   NZ                                        
REMARK 480     LYS C  463   CE   NZ                                             
REMARK 480     LYS C  529   CD   CE   NZ                                        
REMARK 480     THR C  552   OG1  CG2                                            
REMARK 480     LYS C  553   CG   CD   CE   NZ                                   
REMARK 480     GLU C  566   CD   OE1  OE2                                       
REMARK 480     LYS B  118   CG   CD   CE   NZ                                   
REMARK 480     LYS B  154   CD   CE   NZ                                        
REMARK 480     GLN B  157   CG   CD   OE1  NE2                                  
REMARK 480     LYS B  200   CD   CE   NZ                                        
REMARK 480     LYS B  218   CE   NZ                                             
REMARK 480     LYS B  265   CE   NZ                                             
REMARK 480     ASP B  359   CG   OD1  OD2                                       
REMARK 480     LYS B  368   CD   CE   NZ                                        
REMARK 480     GLN D  533   CD   OE1  NE2                                       
REMARK 480     LYS D  551   CD   CE   NZ                                        
REMARK 480     GLU D  566   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    LYS A  36      -62.01   -126.11                                   
REMARK 500    ALA A  79      -55.16   -142.68                                   
REMARK 500    LYS A 125       -3.47     74.32                                   
REMARK 500    ASN C 400     -102.49     82.92                                   
REMARK 500    ALA C 406       -0.78     69.79                                   
REMARK 500    ASN C 446       -7.09     72.32                                   
REMARK 500    TRP C 507      -58.92     75.06                                   
REMARK 500    ASP C 542       82.33   -157.52                                   
REMARK 500    LYS B  36      -60.18   -126.58                                   
REMARK 500    ALA B  79      -56.33   -143.96                                   
REMARK 500    LYS B 125       -0.97     71.84                                   
REMARK 500    ASP B 359        0.98     83.98                                   
REMARK 500    ASN D 400     -104.23     83.24                                   
REMARK 500    ALA D 406       -1.00     70.08                                   
REMARK 500    ASN D 446       -2.73     71.11                                   
REMARK 500    ASN D 462       18.92     56.19                                   
REMARK 500    PHE D 465      -51.42   -121.22                                   
REMARK 500    TRP D 507      -57.84     73.97                                   
REMARK 500    ASP D 542       80.72   -160.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 831        DISTANCE = 13.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4UD C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4UD D 701 and THR D    
REMARK 800  380                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 4UD D 701 and THR D    
REMARK 800  380                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FNM   RELATED DB: PDB                                   
REMARK 900 HELICOBACTER PYLORI GGT                                              
DBREF  5BPK A    1   379  UNP    O25743   O25743_HELPY     1    379             
DBREF  5BPK C  380   567  UNP    O25743   O25743_HELPY   380    567             
DBREF  5BPK B    1   379  UNP    O25743   O25743_HELPY     1    379             
DBREF  5BPK D  380   567  UNP    O25743   O25743_HELPY   380    567             
SEQADV 5BPK GLY C  568  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK THR C  569  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLY C  570  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK SER C  571  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LYS C  572  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU C  573  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA C  574  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA C  575  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA C  576  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLN C  577  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU C  578  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK TYR C  579  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK THR C  580  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ARG C  581  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA C  582  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK SER C  583  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLN C  584  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO C  585  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU C  586  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU C  587  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA C  588  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO C  589  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU C  590  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ASP C  591  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO C  592  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU C  593  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ASP C  594  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU C  595  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU C  596  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  597  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  598  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  599  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  600  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  601  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  602  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  603  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS C  604  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLY D  568  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK THR D  569  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLY D  570  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK SER D  571  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LYS D  572  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU D  573  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA D  574  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA D  575  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA D  576  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLN D  577  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU D  578  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK TYR D  579  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK THR D  580  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ARG D  581  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA D  582  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK SER D  583  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLN D  584  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO D  585  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU D  586  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU D  587  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ALA D  588  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO D  589  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU D  590  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ASP D  591  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK PRO D  592  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU D  593  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK ASP D  594  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK LEU D  595  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK GLU D  596  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  597  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  598  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  599  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  600  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  601  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  602  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  603  UNP  O25743              EXPRESSION TAG                 
SEQADV 5BPK HIS D  604  UNP  O25743              EXPRESSION TAG                 
SEQRES   1 A  379  MET ARG ARG SER PHE LEU LYS THR ILE GLY LEU GLY VAL          
SEQRES   2 A  379  ILE ALA LEU PHE LEU GLY LEU LEU ASN PRO LEU SER ALA          
SEQRES   3 A  379  ALA SER TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU          
SEQRES   4 A  379  ALA LEU SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN          
SEQRES   5 A  379  LYS VAL LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA          
SEQRES   6 A  379  VAL ALA ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA          
SEQRES   7 A  379  ALA GLY ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS          
SEQRES   8 A  379  LEU ALA ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU          
SEQRES   9 A  379  LYS ALA PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP          
SEQRES  10 A  379  LYS GLN GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY          
SEQRES  11 A  379  TYR LEU ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET          
SEQRES  12 A  379  GLU ALA MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER          
SEQRES  13 A  379  GLN LEU ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY          
SEQRES  14 A  379  TYR ALA ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU          
SEQRES  15 A  379  ALA ARG GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS          
SEQRES  16 A  379  TYR PHE PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY          
SEQRES  17 A  379  ASP LEU PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN          
SEQRES  18 A  379  GLN ILE LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY          
SEQRES  19 A  379  GLN VAL ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN          
SEQRES  20 A  379  GLY GLY ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN          
SEQRES  21 A  379  VAL LYS TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY          
SEQRES  22 A  379  TYR LYS ILE ILE SER MET SER PRO PRO SER SER GLY GLY          
SEQRES  23 A  379  THR HIS LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA          
SEQRES  24 A  379  ASP LEU SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE          
SEQRES  25 A  379  HIS ILE ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP          
SEQRES  26 A  379  ARG SER VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL          
SEQRES  27 A  379  PRO VAL ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS          
SEQRES  28 A  379  ILE PHE ASP THR ILE GLN PRO ASP THR VAL THR PRO SER          
SEQRES  29 A  379  SER GLN ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY          
SEQRES  30 A  379  SER ASN                                                      
SEQRES   1 C  225  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 C  225  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 C  225  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 C  225  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 C  225  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 C  225  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 C  225  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 C  225  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 C  225  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 C  225  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 C  225  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 C  225  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 C  225  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 C  225  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 C  225  ASP PRO ARG LYS GLU PHE GLY THR GLY SER LYS LEU ALA          
SEQRES  16 C  225  ALA ALA GLN LEU TYR THR ARG ALA SER GLN PRO GLU LEU          
SEQRES  17 C  225  ALA PRO GLU ASP PRO GLU ASP LEU GLU HIS HIS HIS HIS          
SEQRES  18 C  225  HIS HIS HIS HIS                                              
SEQRES   1 B  379  MET ARG ARG SER PHE LEU LYS THR ILE GLY LEU GLY VAL          
SEQRES   2 B  379  ILE ALA LEU PHE LEU GLY LEU LEU ASN PRO LEU SER ALA          
SEQRES   3 B  379  ALA SER TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU          
SEQRES   4 B  379  ALA LEU SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN          
SEQRES   5 B  379  LYS VAL LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA          
SEQRES   6 B  379  VAL ALA ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA          
SEQRES   7 B  379  ALA GLY ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS          
SEQRES   8 B  379  LEU ALA ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU          
SEQRES   9 B  379  LYS ALA PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP          
SEQRES  10 B  379  LYS GLN GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY          
SEQRES  11 B  379  TYR LEU ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET          
SEQRES  12 B  379  GLU ALA MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER          
SEQRES  13 B  379  GLN LEU ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY          
SEQRES  14 B  379  TYR ALA ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU          
SEQRES  15 B  379  ALA ARG GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS          
SEQRES  16 B  379  TYR PHE PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY          
SEQRES  17 B  379  ASP LEU PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN          
SEQRES  18 B  379  GLN ILE LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY          
SEQRES  19 B  379  GLN VAL ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN          
SEQRES  20 B  379  GLY GLY ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN          
SEQRES  21 B  379  VAL LYS TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY          
SEQRES  22 B  379  TYR LYS ILE ILE SER MET SER PRO PRO SER SER GLY GLY          
SEQRES  23 B  379  THR HIS LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA          
SEQRES  24 B  379  ASP LEU SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE          
SEQRES  25 B  379  HIS ILE ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP          
SEQRES  26 B  379  ARG SER VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL          
SEQRES  27 B  379  PRO VAL ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS          
SEQRES  28 B  379  ILE PHE ASP THR ILE GLN PRO ASP THR VAL THR PRO SER          
SEQRES  29 B  379  SER GLN ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY          
SEQRES  30 B  379  SER ASN                                                      
SEQRES   1 D  225  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 D  225  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 D  225  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 D  225  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 D  225  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 D  225  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 D  225  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 D  225  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 D  225  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 D  225  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 D  225  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 D  225  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 D  225  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 D  225  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 D  225  ASP PRO ARG LYS GLU PHE GLY THR GLY SER LYS LEU ALA          
SEQRES  16 D  225  ALA ALA GLN LEU TYR THR ARG ALA SER GLN PRO GLU LEU          
SEQRES  17 D  225  ALA PRO GLU ASP PRO GLU ASP LEU GLU HIS HIS HIS HIS          
SEQRES  18 D  225  HIS HIS HIS HIS                                              
HET    EDO  A 401       4                                                       
HET    EDO  A 402       4                                                       
HET    EDO  A 403       4                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HET    EDO  A 408       4                                                       
HET    EDO  A 409       4                                                       
HET    EDO  A 410       4                                                       
HET    4UD  C 701      10                                                       
HET    EDO  C 702       4                                                       
HET    EDO  C 703       4                                                       
HET    EDO  C 704       4                                                       
HET    EDO  C 705       4                                                       
HET    EDO  C 706       4                                                       
HET    EDO  C 707       4                                                       
HET    EDO  C 708       4                                                       
HET    EDO  C 709       4                                                       
HET    EDO  C 710       4                                                       
HET    EDO  C 711       4                                                       
HET    EDO  B 401       4                                                       
HET    EDO  B 402       4                                                       
HET    EDO  B 403       4                                                       
HET    EDO  B 404       4                                                       
HET    EDO  B 405       4                                                       
HET    EDO  B 406       4                                                       
HET    EDO  B 407       4                                                       
HET    EDO  B 408       4                                                       
HET    EDO  B 409       4                                                       
HET    EDO  B 410       4                                                       
HET    EDO  B 411       4                                                       
HET    EDO  B 412       4                                                       
HET    EDO  B 413       4                                                       
HET    4UD  D 701      10                                                       
HET    EDO  D 702       4                                                       
HET    EDO  D 703       4                                                       
HET    EDO  D 704       4                                                       
HET    EDO  D 705       4                                                       
HET    EDO  D 706       4                                                       
HET    EDO  D 707       4                                                       
HET    EDO  D 708       4                                                       
HET    EDO  D 709       4                                                       
HET    EDO  D 710       4                                                       
HET    EDO  D 711       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     4UD (2S)-AMINO[(5S)-4,5-DIHYDRO-1,2-OXAZOL-5-YL]ACETIC ACID          
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    43(C2 H6 O2)                                                 
FORMUL  15  4UD    2(C5 H8 N2 O3)                                               
FORMUL  50  HOH   *958(H2 O)                                                    
HELIX    1 AA1 HIS A   44  GLU A   57  1                                  14    
HELIX    2 AA2 ASN A   60  HIS A   76  1                                  17    
HELIX    3 AA3 GLY A  130  ALA A  134  5                                   5    
HELIX    4 AA4 GLY A  138  GLY A  151  1                                  14    
HELIX    5 AA5 LYS A  154  GLY A  169  1                                  16    
HELIX    6 AA6 SER A  173  LEU A  188  1                                  16    
HELIX    7 AA7 TYR A  190  PHE A  197  1                                   8    
HELIX    8 AA8 GLN A  213  GLY A  227  1                                  15    
HELIX    9 AA9 ALA A  228  GLN A  233  1                                   6    
HELIX   10 AB1 GLN A  233  ASN A  247  1                                  15    
HELIX   11 AB2 THR A  252  SER A  258  1                                   7    
HELIX   12 AB3 SER A  284  GLU A  297  1                                  14    
HELIX   13 AB4 ASN A  298  ALA A  299  5                                   2    
HELIX   14 AB5 ASP A  300  LEU A  304  5                                   5    
HELIX   15 AB6 ALA A  308  MET A  330  1                                  23    
HELIX   16 AB7 PRO A  339  ILE A  344  1                                   6    
HELIX   17 AB8 ASN A  345  THR A  355  1                                  11    
HELIX   18 AB9 PRO A  363  ILE A  367  5                                   5    
HELIX   19 AC1 LYS A  368  GLN A  373  5                                   6    
HELIX   20 AC2 ASN C  418  PHE C  423  5                                   6    
HELIX   21 AC3 GLY C  472  SER C  474  5                                   3    
HELIX   22 AC4 ARG C  475  ASP C  489  1                                  15    
HELIX   23 AC5 ASN C  493  ALA C  500  1                                   8    
HELIX   24 AC6 PRO C  520  GLY C  531  1                                  12    
HELIX   25 AC7 ASP C  562  PHE C  567  5                                   6    
HELIX   26 AC8 HIS B   44  GLU B   57  1                                  14    
HELIX   27 AC9 ASN B   60  HIS B   76  1                                  17    
HELIX   28 AD1 GLY B  138  GLY B  151  1                                  14    
HELIX   29 AD2 LYS B  154  GLY B  169  1                                  16    
HELIX   30 AD3 SER B  173  LEU B  188  1                                  16    
HELIX   31 AD4 TYR B  190  PHE B  197  1                                   8    
HELIX   32 AD5 GLN B  213  GLY B  227  1                                  15    
HELIX   33 AD6 ALA B  228  GLN B  233  1                                   6    
HELIX   34 AD7 GLN B  233  ASN B  247  1                                  15    
HELIX   35 AD8 THR B  252  SER B  258  1                                   7    
HELIX   36 AD9 SER B  284  GLU B  297  1                                  14    
HELIX   37 AE1 ASN B  298  ALA B  299  5                                   2    
HELIX   38 AE2 ASP B  300  LEU B  304  5                                   5    
HELIX   39 AE3 ALA B  308  MET B  330  1                                  23    
HELIX   40 AE4 PRO B  339  ILE B  344  1                                   6    
HELIX   41 AE5 ASN B  345  THR B  355  1                                  11    
HELIX   42 AE6 PRO B  363  ILE B  367  5                                   5    
HELIX   43 AE7 LYS B  368  GLN B  373  5                                   6    
HELIX   44 AE8 ASN D  418  PHE D  423  5                                   6    
HELIX   45 AE9 GLY D  472  SER D  474  5                                   3    
HELIX   46 AF1 ARG D  475  ASP D  489  1                                  15    
HELIX   47 AF2 ASN D  493  ALA D  500  1                                   8    
HELIX   48 AF3 PRO D  520  MET D  530  1                                  11    
HELIX   49 AF4 ASP D  562  PHE D  567  5                                   6    
SHEET    1 AA1 7 ILE A  32  ASN A  34  0                                        
SHEET    2 AA1 7 SER C 555  SER C 560 -1  O  PHE C 557   N  ASN A  34           
SHEET    3 AA1 7 ALA C 545  PRO C 550 -1  N  GLN C 547   O  TYR C 558           
SHEET    4 AA1 7 LYS C 463  VAL C 468 -1  N  VAL C 467   O  ILE C 546           
SHEET    5 AA1 7 THR C 456  LYS C 460 -1  N  THR C 456   O  VAL C 468           
SHEET    6 AA1 7 TYR A 274  SER A 278 -1  N  LYS A 275   O  LEU C 459           
SHEET    7 AA1 7 VAL A 267  TYR A 271 -1  N  VAL A 267   O  SER A 278           
SHEET    1 AA2 6 GLY A  38  LEU A  41  0                                        
SHEET    2 AA2 6 THR C 381  ASP C 387 -1  O  SER C 384   N  LEU A  41           
SHEET    3 AA2 6 ALA C 392  THR C 398 -1  O  VAL C 395   N  TYR C 383           
SHEET    4 AA2 6 GLY A  85  HIS A  91 -1  N  HIS A  91   O  ALA C 392           
SHEET    5 AA2 6 ASN A  97  PHE A 102 -1  O  LEU A 100   N  ALA A  88           
SHEET    6 AA2 6 LYS A 262  ARG A 264 -1  O  ARG A 264   N  ALA A  99           
SHEET    1 AA3 2 TYR A 170  ALA A 171  0                                        
SHEET    2 AA3 2 LEU A 210  PHE A 211 -1  O  PHE A 211   N  TYR A 170           
SHEET    1 AA4 2 PHE A 198  LYS A 199  0                                        
SHEET    2 AA4 2 LEU A 203  ASP A 204 -1  O  LEU A 203   N  LYS A 199           
SHEET    1 AA5 2 LEU C 512  ILE C 514  0                                        
SHEET    2 AA5 2 ILE C 534  THR C 536  1  O  VAL C 535   N  ILE C 514           
SHEET    1 AA6 7 ILE B  32  ASN B  34  0                                        
SHEET    2 AA6 7 SER D 555  SER D 560 -1  O  PHE D 557   N  ASN B  34           
SHEET    3 AA6 7 ALA D 545  PRO D 550 -1  N  GLN D 547   O  TYR D 558           
SHEET    4 AA6 7 LYS D 463  VAL D 468 -1  N  VAL D 467   O  ILE D 546           
SHEET    5 AA6 7 THR D 456  LYS D 460 -1  N  THR D 456   O  VAL D 468           
SHEET    6 AA6 7 TYR B 274  SER B 278 -1  N  ILE B 277   O  ILE D 457           
SHEET    7 AA6 7 VAL B 267  TYR B 271 -1  N  GLY B 269   O  ILE B 276           
SHEET    1 AA7 6 GLY B  38  LEU B  41  0                                        
SHEET    2 AA7 6 THR D 381  ASP D 387 -1  O  SER D 384   N  LEU B  41           
SHEET    3 AA7 6 ALA D 392  THR D 398 -1  O  VAL D 395   N  TYR D 383           
SHEET    4 AA7 6 GLY B  85  HIS B  91 -1  N  GLY B  85   O  THR D 398           
SHEET    5 AA7 6 ASN B  97  PHE B 102 -1  O  LEU B 100   N  ALA B  88           
SHEET    6 AA7 6 LYS B 262  ARG B 264 -1  O  ARG B 264   N  ALA B  99           
SHEET    1 AA8 2 TYR B 170  ALA B 171  0                                        
SHEET    2 AA8 2 LEU B 210  PHE B 211 -1  O  PHE B 211   N  TYR B 170           
SHEET    1 AA9 2 LEU D 512  ILE D 514  0                                        
SHEET    2 AA9 2 ILE D 534  THR D 536  1  O  VAL D 535   N  ILE D 514           
LINK         OG1ATHR C 380                 C3  4UD C 701     1555   1555  1.33  
LINK         OG1BTHR C 380                 C3  4UD C 701     1555   1555  1.39  
LINK         OG1ATHR D 380                 C3  4UD D 701     1555   1555  1.39  
LINK         OG1BTHR D 380                 C3  4UD D 701     1555   1555  1.34  
CISPEP   1 PRO A  281    PRO A  282          0        18.00                     
CISPEP   2 LEU C  508    PRO C  509          0        -2.82                     
CISPEP   3 PRO B  281    PRO B  282          0        18.33                     
CISPEP   4 LEU D  508    PRO D  509          0        -1.16                     
SITE     1 AC1  2 TYR A  29  HOH D 815                                          
SITE     1 AC2  5 HIS A  76  HOH A 534  HOH A 611  LYS C 565                    
SITE     2 AC2  5 HOH C 809                                                     
SITE     1 AC3  7 LEU A 180  ARG A 184  PHE A 197  PHE A 198                    
SITE     2 AC3  7 ASP A 204  TYR A 205  HOH A 647                               
SITE     1 AC4  8 SER A  28  TYR A  29  SER B  28  TYR B  29                    
SITE     2 AC4  8 SER C 499  HOH C 802  SER D 499  HOH D 801                    
SITE     1 AC5  3 ASP A 341  ASN A 345  HOH A 694                               
SITE     1 AC6  5 ARG A 272  GLY A 273  TYR A 274  LYS C 460                    
SITE     2 AC6  5 ASN C 461                                                     
SITE     1 AC7  2 GLU A 297  HOH A 744                                          
SITE     1 AC8  5 ASN A  94  LEU A 188  LYS A 189  SER A 191                    
SITE     2 AC8  5 LYS A 194                                                     
SITE     1 AC9  4 ALA A 145  LYS A 148  LYS A 149  TRP A 263                    
SITE     1 AD1  4 ASN A 260  HOH A 621  LYS B 253  ALA B 257                    
SITE     1 AD2 14 ARG A 103  THR C 380  THR C 398  ASN C 400                    
SITE     2 AD2 14 GLU C 419  ASP C 422  TYR C 433  SER C 451                    
SITE     3 AD2 14 SER C 452  MET C 453  GLY C 472  GLY C 473                    
SITE     4 AD2 14 ILE C 476  HOH C 835                                          
SITE     1 AD3  9 HIS A  91  ALA A  93  HOH A 511  GLY C 390                    
SITE     2 AD3  9 ASN C 462  LYS C 463  VAL C 464  EDO C 707                    
SITE     3 AD3  9 HOH C 816                                                     
SITE     1 AD4 10 ARG A 326  ASP C 422  PHE C 423  SER C 424                    
SITE     2 AD4 10 ASN C 429  ASN C 431  LEU C 435  ASN C 441                    
SITE     3 AD4 10 HOH C 849  HOH C 868                                          
SITE     1 AD5  8 PRO C 501  ARG C 502  PHE C 503  ILE C 514                    
SITE     2 AD5  8 GLU C 515  GLY C 518  HOH C 807  HOH C 875                    
SITE     1 AD6  7 PRO A  30  TYR B  29  SER C 495  SER C 560                    
SITE     2 AD6  7 THR C 561  HOH C 802  HOH C 837                               
SITE     1 AD7  7 ALA A  93  LYS A 194  HIS A 202  ASN C 391                    
SITE     2 AD7  7 EDO C 711  HOH C 820  HOH C 867                               
SITE     1 AD8  6 ASP C 387  GLY C 390  SER C 555  EDO C 702                    
SITE     2 AD8  6 HOH C 839  HOH C 861                                          
SITE     1 AD9  6 MET A 296  ASN A 311  SER C 485  TYR C 490                    
SITE     2 AD9  6 HOH C 823  HOH C 836                                          
SITE     1 AE1  5 LYS C 516  PRO C 538  VAL C 539  HOH C 862                    
SITE     2 AE1  5 HOH C 883                                                     
SITE     1 AE2  6 ASP C 522  ASP C 525  ASN C 526  HOH C 817                    
SITE     2 AE2  6 HOH C 841  ASN D 526                                          
SITE     1 AE3  7 THR A 152  GLY A 201  HIS A 202  TRP C 389                    
SITE     2 AE3  7 EDO C 706  HOH C 804  HOH C 820                               
SITE     1 AE4  3 GLU B 167  LYS B 214  HOH B 565                               
SITE     1 AE5  6 THR B 152  GLY B 201  HIS B 202  HOH B 574                    
SITE     2 AE5  6 HOH B 711  TRP D 389                                          
SITE     1 AE6  6 LYS B 194  HIS B 202  HOH B 711  TRP D 389                    
SITE     2 AE6  6 ASN D 391  HOH D 879                                          
SITE     1 AE7  6 SER B  42  SER B  43  HIS B  44  PRO B  45                    
SITE     2 AE7  6 SER B  48  LYS D 565                                          
SITE     1 AE8  6 ASN B  94  LEU B 188  LYS B 189  SER B 191                    
SITE     2 AE8  6 LYS B 194  HOH B 778                                          
SITE     1 AE9  4 LYS B 199  ASP B 204  GLN B 206  EDO B 412                    
SITE     1 AF1  5 PHE B 353  ILE B 356  GLN B 357  PRO B 358                    
SITE     2 AF1  5 HOH B 616                                                     
SITE     1 AF2  4 LYS B 262  ASP B 334  GLU C 444  HOH C 944                    
SITE     1 AF3  4 LYS B 109  GLU B 241  LYS B 245  HOH B 682                    
SITE     1 AF4  4 LYS B  33  ASN B  34  GLN B  52  HOH B 519                    
SITE     1 AF5  4 LEU B 203  ASP B 204  EDO B 407  ARG D 388                    
SITE     1 AF6  6 LEU B 180  ARG B 184  PHE B 197  PHE B 198                    
SITE     2 AF6  6 ASP B 204  TYR B 205                                          
SITE     1 AF7  8 ALA A  27  HOH A 597  ALA B  27  SER C 499                    
SITE     2 AF7  8 SER D 499  HOH D 806  HOH D 854  HOH D 864                    
SITE     1 AF8  3 ASP D 510  GLU D 511  GLN D 533                               
SITE     1 AF9  5 LEU A 304  ALA D 521  ASP D 525  HOH D 880                    
SITE     2 AF9  5 HOH D 917                                                     
SITE     1 AG1  8 PRO D 501  ARG D 502  PHE D 503  ILE D 514                    
SITE     2 AG1  8 GLU D 515  GLY D 518  HOH D 814  HOH D 856                    
SITE     1 AG2  8 TYR A  29  PRO B  30  ILE B  32  SER D 495                    
SITE     2 AG2  8 SER D 560  THR D 561  HOH D 801  HOH D 815                    
SITE     1 AG3  5 ASN B 311  SER D 485  TYR D 490  HOH D 807                    
SITE     2 AG3  5 HOH D 846                                                     
SITE     1 AG4 10 ARG B 326  ASP D 422  PHE D 423  ASN D 429                    
SITE     2 AG4 10 ASN D 431  LEU D 435  ASN D 441  HOH D 850                    
SITE     3 AG4 10 HOH D 862  HOH D 911                                          
SITE     1 AG5  9 ASP D 387  ARG D 388  TRP D 389  GLY D 390                    
SITE     2 AG5  9 SER D 555  PHE D 557  HOH D 852  HOH D 873                    
SITE     3 AG5  9 HOH D 897                                                     
SITE     1 AG6  5 ASN C 526  HOH C 841  ASP D 522  ASP D 525                    
SITE     2 AG6  5 HOH D 818                                                     
SITE     1 AG7  2 ARG D 475  ARG D 513                                          
SITE     1 AG8 20 ALA B  79  ARG B 103  THR D 381  TYR D 397                    
SITE     2 AG8 20 THR D 398  ASN D 400  GLU D 419  ASP D 422                    
SITE     3 AG8 20 TYR D 433  SER D 451  SER D 452  MET D 453                    
SITE     4 AG8 20 PRO D 471  GLY D 472  GLY D 473  ILE D 476                    
SITE     5 AG8 20 HOH D 855  HOH D 857  HOH D 860  HOH D 914                    
SITE     1 AG9 20 ALA B  79  ARG B 103  THR D 381  TYR D 397                    
SITE     2 AG9 20 THR D 398  ASN D 400  GLU D 419  ASP D 422                    
SITE     3 AG9 20 TYR D 433  SER D 451  SER D 452  MET D 453                    
SITE     4 AG9 20 PRO D 471  GLY D 472  GLY D 473  ILE D 476                    
SITE     5 AG9 20 HOH D 855  HOH D 857  HOH D 860  HOH D 914                    
CRYST1   53.777  112.006   91.854  90.00  90.79  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018595  0.000000  0.000257        0.00000                         
SCALE2      0.000000  0.008928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010888        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system