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Database: PDB
Entry: 2NQO
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Original site: 2NQO 
HEADER    TRANSFERASE                             31-OCT-06   2NQO              
TITLE     CRYSTAL STRUCTURE OF HELICOBACTER PYLORI GAMMA-GLUTAMYLTRANSPEPTIDASE 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 27-379;                                           
COMPND   5 SYNONYM: GGT;                                                        
COMPND   6 EC: 2.3.2.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE;                              
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: RESIDUES 380-567;                                          
COMPND  13 SYNONYM: GGT;                                                        
COMPND  14 EC: 2.3.2.2;                                                         
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_TAXID: 210;                                                 
SOURCE   4 GENE: HP_1118;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE  12 ORGANISM_TAXID: 210;                                                 
SOURCE  13 GENE: HP_1118;                                                       
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    NTN-HYDROLASE, GLUTAMYLTRANSPEPTIDASE, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BOANCA,A.SAND,T.OKADA,H.SUZUKI,H.KUMAGAI,K.FUKUYAMA,J.J.BARYCKI     
REVDAT   5   18-OCT-17 2NQO    1       REMARK                                   
REVDAT   4   13-JUL-11 2NQO    1       VERSN                                    
REVDAT   3   24-FEB-09 2NQO    1       VERSN                                    
REVDAT   2   13-FEB-07 2NQO    1       JRNL                                     
REVDAT   1   21-NOV-06 2NQO    0                                                
JRNL        AUTH   G.BOANCA,A.SAND,T.OKADA,H.SUZUKI,H.KUMAGAI,K.FUKUYAMA,       
JRNL        AUTH 2 J.J.BARYCKI                                                  
JRNL        TITL   AUTOPROCESSING OF HELICOBACTER PYLORI                        
JRNL        TITL 2 GAMMA-GLUTAMYLTRANSPEPTIDASE LEADS TO THE FORMATION OF A     
JRNL        TITL 3 THREONINE-THREONINE CATALYTIC DYAD.                          
JRNL        REF    J.BIOL.CHEM.                  V. 282   534 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17107958                                                     
JRNL        DOI    10.1074/JBC.M607694200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 163846.344                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 72974                          
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 7385                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9371                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1024                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8089                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 590                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.41000                                             
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : 0.97000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.81000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
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) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.850                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.250 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.900 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.840 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.670 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 53.79                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2NQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000040185.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90000                            
REMARK 200  MONOCHROMATOR                  : BENT GE(111)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72974                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.5                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.04600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46600                            
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: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2DBU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM HEPES, 25% PEG MME2000, 5 MG/ML   
REMARK 280  PROTEIN, PH 7.5, 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       52.60300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 10970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 11210 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 19680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE ASYMMETRIC UNIT CONTAINS A HETEROTETRAMER WHICH                  
REMARK 400 IS FORMED FROM TWO COMPLETE POLYPEPTIDE CHAINS THAT                  
REMARK 400 UNDERGO AUTOPROCESSING (CHAIN BREAKING BETWEEN                       
REMARK 400 RESIDUES 379 AND 380). THIS CHAIN BREAKING LEADS TO                  
REMARK 400 ACTIVATION OF THE ENZYME. AUTHOR STATES, THAT                        
REMARK 400 EXCEPT BEING A TRANSFERASE, THIS ENZYME IS ALSO A                    
REMARK 400 HYDROLASE.                                                           
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     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     VAL A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     MET A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLU A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     ASN A   379                                                      
REMARK 465     GLU B   566                                                      
REMARK 465     PHE B   567                                                      
REMARK 465     MET C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     SER C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     HIS C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     SER C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     LEU C    17                                                      
REMARK 465     VAL C    18                                                      
REMARK 465     PRO C    19                                                      
REMARK 465     ARG C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     SER C    22                                                      
REMARK 465     HIS C    23                                                      
REMARK 465     MET C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     SER C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     TYR C    29                                                      
REMARK 465     PRO C    30                                                      
REMARK 465     GLU D   566                                                      
REMARK 465     PHE D   567                                                      
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     TYR A  29    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS A 375    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 551    CG   CD   CE   NZ                                   
REMARK 470     LYS B 553    CG   CD   CE   NZ                                   
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      -78.61   -113.53                                   
REMARK 500    HIS A  76       58.08   -142.59                                   
REMARK 500    ALA A  79      -50.92   -137.35                                   
REMARK 500    LYS A 118       39.57    -78.55                                   
REMARK 500    GLN A 119       18.44   -156.91                                   
REMARK 500    PRO A 124      124.36    -38.28                                   
REMARK 500    LYS A 125       12.59     56.61                                   
REMARK 500    PRO A 282        9.39    -64.10                                   
REMARK 500    MET A 371       -1.86     65.95                                   
REMARK 500    GLN A 373     -132.38    -68.60                                   
REMARK 500    ASN B 400      -97.61     82.89                                   
REMARK 500    ALA B 406       -0.34     71.45                                   
REMARK 500    LYS B 426      126.55   -173.07                                   
REMARK 500    TRP B 507      -61.70     66.70                                   
REMARK 500    ASP B 542       80.21   -162.84                                   
REMARK 500    LYS C  36      -67.20   -104.17                                   
REMARK 500    ALA C  79      -48.78   -138.40                                   
REMARK 500    LYS C 125      -12.85     71.64                                   
REMARK 500    PRO C 282        6.06    -64.23                                   
REMARK 500    ASN D 400     -101.98     80.32                                   
REMARK 500    ALA D 406       -0.89     73.58                                   
REMARK 500    ASN D 446       -7.49     71.64                                   
REMARK 500    ASN D 461       40.56     92.68                                   
REMARK 500    TRP D 507      -57.16     71.56                                   
REMARK 500    ASP D 542       80.36   -167.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 259         0.08    SIDE CHAIN                              
REMARK 500    TYR C 259         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2DBU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E.COLI GAMMA-GLUTAMYLTRANSPEPTIDASE             
REMARK 900 RELATED ID: 2DBW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E.COLI GAMMA-GLUTAMYLTRANSPEPTIDASE ACYL-       
REMARK 900 ENZYME INTERMEDIATE                                                  
REMARK 900 RELATED ID: 2DBX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF E.COLI GAMMA-GLUTAMYLTRANSPEPTIDASE COMPLEXED   
REMARK 900 WITH L-GLUTAMATE                                                     
DBREF  2NQO A   27   379  UNP    O25743   O25743_HELPY    27    379             
DBREF  2NQO C   27   379  UNP    O25743   O25743_HELPY    27    379             
DBREF  2NQO B  380   567  UNP    O25743   O25743_HELPY   380    567             
DBREF  2NQO D  380   567  UNP    O25743   O25743_HELPY   380    567             
SEQADV 2NQO MET A    4  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY A    5  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A    6  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A    7  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A    8  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A    9  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A   10  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A   11  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A   12  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A   13  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A   14  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A   15  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY A   16  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO LEU A   17  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO VAL A   18  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO PRO A   19  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO ARG A   20  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY A   21  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A   22  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS A   23  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO MET A   24  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO ALA A   25  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER A   26  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO MET C    4  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY C    5  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C    6  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C    7  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C    8  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C    9  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C   10  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C   11  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C   12  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C   13  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C   14  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C   15  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY C   16  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO LEU C   17  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO VAL C   18  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO PRO C   19  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO ARG C   20  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO GLY C   21  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C   22  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO HIS C   23  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO MET C   24  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO ALA C   25  UNP  O25743              CLONING ARTIFACT               
SEQADV 2NQO SER C   26  UNP  O25743              CLONING ARTIFACT               
SEQRES   1 A  376  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  376  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA SER TYR          
SEQRES   3 A  376  PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU SER          
SEQRES   4 A  376  SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL LEU          
SEQRES   5 A  376  GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA ILE          
SEQRES   6 A  376  GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY ASN          
SEQRES   7 A  376  ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA ASN          
SEQRES   8 A  376  GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA PRO          
SEQRES   9 A  376  LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN GLY          
SEQRES  10 A  376  ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU ALA          
SEQRES  11 A  376  ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA MET          
SEQRES  12 A  376  LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU ILE          
SEQRES  13 A  376  ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA ILE          
SEQRES  14 A  376  SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG GLU          
SEQRES  15 A  376  ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE PHE          
SEQRES  16 A  376  LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU PHE          
SEQRES  17 A  376  VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE LYS          
SEQRES  18 A  376  THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL ALA          
SEQRES  19 A  376  GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY ILE          
SEQRES  20 A  376  ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS TRP          
SEQRES  21 A  376  ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS ILE          
SEQRES  22 A  376  ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS LEU          
SEQRES  23 A  376  ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU SER          
SEQRES  24 A  376  ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE ALA          
SEQRES  25 A  376  ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER VAL          
SEQRES  26 A  376  TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL ASP          
SEQRES  27 A  376  LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE ASP          
SEQRES  28 A  376  THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN ILE          
SEQRES  29 A  376  LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN              
SEQRES   1 B  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 B  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 B  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 B  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 B  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 B  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 B  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 B  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 B  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 B  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 B  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 B  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 B  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 B  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 B  188  ASP PRO ARG LYS GLU PHE                                      
SEQRES   1 C  376  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  376  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA SER TYR          
SEQRES   3 C  376  PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU SER          
SEQRES   4 C  376  SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL LEU          
SEQRES   5 C  376  GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA ILE          
SEQRES   6 C  376  GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY ASN          
SEQRES   7 C  376  ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA ASN          
SEQRES   8 C  376  GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA PRO          
SEQRES   9 C  376  LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN GLY          
SEQRES  10 C  376  ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU ALA          
SEQRES  11 C  376  ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA MET          
SEQRES  12 C  376  LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU ILE          
SEQRES  13 C  376  ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA ILE          
SEQRES  14 C  376  SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG GLU          
SEQRES  15 C  376  ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE PHE          
SEQRES  16 C  376  LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU PHE          
SEQRES  17 C  376  VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE LYS          
SEQRES  18 C  376  THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL ALA          
SEQRES  19 C  376  GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY ILE          
SEQRES  20 C  376  ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS TRP          
SEQRES  21 C  376  ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS ILE          
SEQRES  22 C  376  ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS LEU          
SEQRES  23 C  376  ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU SER          
SEQRES  24 C  376  ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE ALA          
SEQRES  25 C  376  ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER VAL          
SEQRES  26 C  376  TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL ASP          
SEQRES  27 C  376  LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE ASP          
SEQRES  28 C  376  THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN ILE          
SEQRES  29 C  376  LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN              
SEQRES   1 D  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 D  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 D  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 D  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 D  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 D  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 D  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 D  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 D  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 D  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 D  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 D  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 D  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 D  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 D  188  ASP PRO ARG LYS GLU PHE                                      
FORMUL   5  HOH   *590(H2 O)                                                    
HELIX    1   1 HIS A   44  GLU A   57  1                                  14    
HELIX    2   2 ASN A   60  HIS A   76  1                                  17    
HELIX    3   3 GLY A  130  ALA A  134  5                                   5    
HELIX    4   4 GLY A  138  GLY A  151  1                                  14    
HELIX    5   5 LYS A  154  ILE A  159  1                                   6    
HELIX    6   6 ILE A  159  GLY A  169  1                                  11    
HELIX    7   7 SER A  173  ALA A  183  1                                  11    
HELIX    8   8 ALA A  183  LYS A  189  1                                   7    
HELIX    9   9 TYR A  190  PHE A  197  1                                   8    
HELIX   10  10 GLN A  213  GLY A  227  1                                  15    
HELIX   11  11 ALA A  228  GLN A  233  1                                   6    
HELIX   12  12 GLN A  233  ASN A  247  1                                  15    
HELIX   13  13 THR A  252  TYR A  259  1                                   8    
HELIX   14  14 SER A  284  GLU A  297  1                                  14    
HELIX   15  15 ASN A  298  ALA A  299  5                                   2    
HELIX   16  16 ASP A  300  LEU A  304  5                                   5    
HELIX   17  17 ALA A  308  MET A  330  1                                  23    
HELIX   18  18 PRO A  339  ILE A  344  1                                   6    
HELIX   19  19 ASN A  345  ASP A  354  1                                  10    
HELIX   20  20 PRO A  363  ILE A  367  5                                   5    
HELIX   21  21 LYS A  368  GLN A  373  5                                   6    
HELIX   22  22 ASN B  418  PHE B  423  5                                   6    
HELIX   23  23 GLY B  472  SER B  474  5                                   3    
HELIX   24  24 ARG B  475  ASP B  489  1                                  15    
HELIX   25  25 ASN B  493  ALA B  500  1                                   8    
HELIX   26  26 PRO B  520  GLY B  531  1                                  12    
HELIX   27  27 HIS C   44  GLU C   57  1                                  14    
HELIX   28  28 ASN C   60  HIS C   76  1                                  17    
HELIX   29  29 GLY C  130  ALA C  134  5                                   5    
HELIX   30  30 GLY C  138  GLY C  151  1                                  14    
HELIX   31  31 LYS C  154  ILE C  159  1                                   6    
HELIX   32  32 ILE C  159  GLY C  169  1                                  11    
HELIX   33  33 SER C  173  ALA C  183  1                                  11    
HELIX   34  34 ALA C  183  LYS C  189  1                                   7    
HELIX   35  35 TYR C  190  PHE C  198  1                                   9    
HELIX   36  36 GLN C  213  GLY C  227  1                                  15    
HELIX   37  37 ALA C  228  GLN C  233  1                                   6    
HELIX   38  38 GLN C  233  ASN C  247  1                                  15    
HELIX   39  39 THR C  252  TYR C  259  1                                   8    
HELIX   40  40 SER C  284  GLU C  297  1                                  14    
HELIX   41  41 ASN C  298  ALA C  299  5                                   2    
HELIX   42  42 ASP C  300  LEU C  304  5                                   5    
HELIX   43  43 ALA C  308  MET C  330  1                                  23    
HELIX   44  44 PRO C  339  ILE C  344  1                                   6    
HELIX   45  45 ASN C  345  ILE C  356  1                                  12    
HELIX   46  46 PRO C  363  ILE C  367  5                                   5    
HELIX   47  47 LYS C  368  GLN C  373  5                                   6    
HELIX   48  48 ASN D  418  PHE D  423  5                                   6    
HELIX   49  49 GLY D  472  SER D  474  5                                   3    
HELIX   50  50 ARG D  475  ASP D  489  1                                  15    
HELIX   51  51 ASN D  493  ALA D  500  1                                   8    
HELIX   52  52 PRO D  520  GLY D  531  1                                  12    
SHEET    1   A 7 ILE A  32  ASN A  34  0                                        
SHEET    2   A 7 SER B 555  SER B 560 -1  O  PHE B 557   N  ASN A  34           
SHEET    3   A 7 ALA B 545  PRO B 550 -1  N  GLN B 547   O  TYR B 558           
SHEET    4   A 7 LYS B 463  VAL B 468 -1  N  VAL B 467   O  ILE B 546           
SHEET    5   A 7 THR B 456  LYS B 460 -1  N  THR B 456   O  VAL B 468           
SHEET    6   A 7 TYR A 274  SER A 278 -1  N  LYS A 275   O  LEU B 459           
SHEET    7   A 7 VAL A 267  TYR A 271 -1  N  GLY A 269   O  ILE A 276           
SHEET    1   B 6 GLY A  38  LEU A  41  0                                        
SHEET    2   B 6 THR B 381  ASP B 387 -1  O  SER B 384   N  LEU A  41           
SHEET    3   B 6 ALA B 392  THR B 398 -1  O  VAL B 395   N  TYR B 383           
SHEET    4   B 6 GLY A  85  HIS A  91 -1  N  GLY A  85   O  THR B 398           
SHEET    5   B 6 ASN A  97  PHE A 102 -1  O  LEU A 100   N  ALA A  88           
SHEET    6   B 6 LYS A 262  ARG A 264 -1  O  ARG A 264   N  ALA A  99           
SHEET    1   C 2 TYR A 170  ALA A 171  0                                        
SHEET    2   C 2 LEU A 210  PHE A 211 -1  O  PHE A 211   N  TYR A 170           
SHEET    1   D 2 LEU B 512  ILE B 514  0                                        
SHEET    2   D 2 ILE B 534  THR B 536  1  O  VAL B 535   N  ILE B 514           
SHEET    1   E 7 ILE C  32  ASN C  34  0                                        
SHEET    2   E 7 GLY D 554  SER D 560 -1  O  PHE D 557   N  ASN C  34           
SHEET    3   E 7 ALA D 545  LYS D 551 -1  N  GLN D 547   O  TYR D 558           
SHEET    4   E 7 VAL D 464  VAL D 468 -1  N  VAL D 467   O  ILE D 546           
SHEET    5   E 7 THR D 456  LEU D 459 -1  N  VAL D 458   O  PHE D 465           
SHEET    6   E 7 TYR C 274  SER C 278 -1  N  ILE C 277   O  ILE D 457           
SHEET    7   E 7 VAL C 267  TYR C 271 -1  N  GLY C 269   O  ILE C 276           
SHEET    1   F 6 GLY C  38  LEU C  41  0                                        
SHEET    2   F 6 THR D 381  ASP D 387 -1  O  SER D 384   N  LEU C  41           
SHEET    3   F 6 ALA D 392  THR D 398 -1  O  VAL D 393   N  VAL D 385           
SHEET    4   F 6 GLY C  85  HIS C  91 -1  N  GLY C  85   O  THR D 398           
SHEET    5   F 6 ASN C  97  PHE C 102 -1  O  VAL C  98   N  ILE C  90           
SHEET    6   F 6 LYS C 262  ARG C 264 -1  O  ARG C 264   N  ALA C  99           
SHEET    1   G 2 TYR C 170  ALA C 171  0                                        
SHEET    2   G 2 LEU C 210  PHE C 211 -1  O  PHE C 211   N  TYR C 170           
SHEET    1   H 2 LEU D 512  ILE D 514  0                                        
SHEET    2   H 2 ILE D 534  THR D 536  1  O  VAL D 535   N  ILE D 514           
CISPEP   1 PRO A  281    PRO A  282          0         0.59                     
CISPEP   2 LEU B  508    PRO B  509          0        -0.11                     
CISPEP   3 PRO C  281    PRO C  282          0         0.69                     
CISPEP   4 LEU D  508    PRO D  509          0        -0.08                     
CRYST1   54.354  105.206   91.060  90.00  91.99  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      0.018398  0.000000  0.000639        0.00000                         
SCALE2      0.000000  0.009505  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010988        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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