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Database: PDB
Entry: 2GPZ
LinkDB: 2GPZ
Original site: 2GPZ 
HEADER    HYDROLASE                               19-APR-06   2GPZ              
TITLE     TRANSTHYRETIN-LIKE PROTEIN FROM SALMONELLA DUBLIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSTHYRETIN-LIKE PROTEIN;                                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR     
SOURCE   3 DUBLIN;                                                              
SOURCE   4 ORGANISM_TAXID: 98360;                                               
SOURCE   5 STRAIN: SUBSP. ENTERICA SEROVAR DUBLIN;                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA BL21;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    SALMONELLA, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.BUCKLE,R.H.LAW,J.C.WHISSTOCK                                      
REVDAT   4   30-AUG-23 2GPZ    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 2GPZ    1       VERSN                                    
REVDAT   2   04-JUL-06 2GPZ    1       JRNL                                     
REVDAT   1   16-MAY-06 2GPZ    0                                                
JRNL        AUTH   S.C.HENNEBRY,R.H.LAW,S.J.RICHARDSON,A.M.BUCKLE,J.C.WHISSTOCK 
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE TRANSTHYRETIN-LIKE PROTEIN FROM 
JRNL        TITL 2 SALMONELLA DUBLIN, A PROKARYOTE 5-HYDROXYISOURATE HYDROLASE. 
JRNL        REF    J.MOL.BIOL.                   V. 359  1389 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16787778                                                     
JRNL        DOI    10.1016/J.JMB.2006.04.057                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10306                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 496                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 700                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3030                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 30                           
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1732                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 32                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.69000                                             
REMARK   3    B22 (A**2) : -0.69000                                             
REMARK   3    B33 (A**2) : 1.04000                                              
REMARK   3    B12 (A**2) : -0.35000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.465         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.282         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.236         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.260        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1786 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2426 ; 1.193 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   216 ; 6.014 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    78 ;31.307 ;23.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   278 ;16.602 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 9.216 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   258 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1360 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   750 ; 0.162 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1144 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    95 ; 0.123 ; 0.200       
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):    83 ; 0.159 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.098 ; 0.200       
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):  1130 ; 0.529 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1758 ; 0.969 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   770 ; 1.424 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   668 ; 2.084 ;10.000       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      5       A     115      1                      
REMARK   3           1     C      5       C     115      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    866 ;  NULL ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):    866 ;  0.01 ;  0.50           
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                                                           
REMARK   4                                                                      
REMARK   4 2GPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037411.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : ELLIOTT GX-13                      
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10308                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.497                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.017                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : 0.11100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.45700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1SN0                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M MAGNESIUM CHLORIDE,   
REMARK 280  0.1M SODIUM CACODYLATE, PH 6.0, EVAPORATION, RECRYSTALLIZATION,     
REMARK 280  TEMPERATURE 295K, PH 6.00                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 300 REMARK: BIOLOGICAL TETRAMER GENERATED FROM THE DIMER IN THE          
REMARK 300 ASYMMETRIC UNIT, BY -X, -Y-1, Z                                      
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, 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   BIOMT1   2 -1.000000  0.000000  0.000000       47.35250            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -82.01694            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 128  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 123  LIES ON A SPECIAL POSITION.                          
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     ASN A    33                                                      
REMARK 465     ASN C    33                                                      
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     LEU A   7    CD1  CD2                                            
REMARK 470     LYS A  30    CE   NZ                                             
REMARK 470     LYS A  31    CB   CG   CD   CE   NZ                              
REMARK 470     ASP A  32    CG   OD1  OD2                                       
REMARK 470     LYS A  56    CE   NZ                                             
REMARK 470     GLN A  71    CG   CD   NE2                                       
REMARK 470     GLU A  74    CD   OE2                                            
REMARK 470     ASP A  79    OD1  OD2                                            
REMARK 470     LYS A  93    NZ                                                  
REMARK 470     LEU C   7    CD1  CD2                                            
REMARK 470     LYS C  30    CE   NZ                                             
REMARK 470     LYS C  31    CB   CG   CD   CE   NZ                              
REMARK 470     ASP C  32    CG   OD1  OD2                                       
REMARK 470     LYS C  56    CE   NZ                                             
REMARK 470     GLN C  71    CG   CD   NE2                                       
REMARK 470     GLU C  74    CD   OE2                                            
REMARK 470     ASP C  79    OD1  OD2                                            
REMARK 470     LYS C  93    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    TRP A  53       73.51     53.58                                   
REMARK 500    GLU A  55       99.64    -56.90                                   
REMARK 500    TRP C  53       74.52     53.18                                   
REMARK 500    GLU C  55       99.67    -57.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 116                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 116                 
DBREF  2GPZ A    6   115  GB     66947663 CAI99863        27    136             
DBREF  2GPZ C    6   115  GB     66947663 CAI99863        27    136             
SEQADV 2GPZ MET A    5  GB   66947663            INITIATING METHIONINE          
SEQADV 2GPZ MET C    5  GB   66947663            INITIATING METHIONINE          
SEQRES   1 A  111  MET ILE LEU SER VAL HIS ILE LEU ASP GLN GLN THR GLY          
SEQRES   2 A  111  LYS PRO ALA PRO GLY VAL GLU VAL VAL LEU GLU GLN LYS          
SEQRES   3 A  111  LYS ASP ASN GLY TRP THR GLN LEU ASN THR GLY HIS THR          
SEQRES   4 A  111  ASP GLN ASP GLY ARG ILE LYS ALA LEU TRP PRO GLU LYS          
SEQRES   5 A  111  ALA ALA ALA PRO GLY ASP TYR ARG VAL ILE PHE LYS THR          
SEQRES   6 A  111  GLY GLN TYR PHE GLU SER LYS LYS LEU ASP THR PHE PHE          
SEQRES   7 A  111  PRO GLU ILE PRO VAL GLU PHE HIS ILE SER LYS THR ASN          
SEQRES   8 A  111  GLU HIS TYR HIS VAL PRO LEU LEU LEU SER GLN TYR GLY          
SEQRES   9 A  111  TYR SER THR TYR ARG GLY SER                                  
SEQRES   1 C  111  MET ILE LEU SER VAL HIS ILE LEU ASP GLN GLN THR GLY          
SEQRES   2 C  111  LYS PRO ALA PRO GLY VAL GLU VAL VAL LEU GLU GLN LYS          
SEQRES   3 C  111  LYS ASP ASN GLY TRP THR GLN LEU ASN THR GLY HIS THR          
SEQRES   4 C  111  ASP GLN ASP GLY ARG ILE LYS ALA LEU TRP PRO GLU LYS          
SEQRES   5 C  111  ALA ALA ALA PRO GLY ASP TYR ARG VAL ILE PHE LYS THR          
SEQRES   6 C  111  GLY GLN TYR PHE GLU SER LYS LYS LEU ASP THR PHE PHE          
SEQRES   7 C  111  PRO GLU ILE PRO VAL GLU PHE HIS ILE SER LYS THR ASN          
SEQRES   8 C  111  GLU HIS TYR HIS VAL PRO LEU LEU LEU SER GLN TYR GLY          
SEQRES   9 C  111  TYR SER THR TYR ARG GLY SER                                  
HET    SO4  A 116       5                                                       
HET    SO4  C 116       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *32(H2 O)                                                     
HELIX    1   1 LYS A   68  LYS A   76  1                                   9    
HELIX    2   2 LYS C   68  LYS C   76  1                                   9    
SHEET    1   A 3 LYS A  18  PRO A  19  0                                        
SHEET    2   A 3 ILE A   6  ASP A  13 -1  N  ASP A  13   O  LYS A  18           
SHEET    3   A 3 HIS A  97  HIS A  99  1  O  TYR A  98   N  ILE A   6           
SHEET    1   B 4 ARG A  48  ILE A  49  0                                        
SHEET    2   B 4 ILE A   6  ASP A  13 -1  N  VAL A   9   O  ILE A  49           
SHEET    3   B 4 LEU A 102  SER A 105  1  O  LEU A 102   N  LEU A  12           
SHEET    4   B 4 GLY A 108  THR A 111 -1  O  SER A 110   N  LEU A 103           
SHEET    1   C 4 TRP A  35  HIS A  42  0                                        
SHEET    2   C 4 GLU A  24  LYS A  30 -1  N  VAL A  25   O  GLY A  41           
SHEET    3   C 4 GLY A  61  PHE A  67 -1  O  ARG A  64   N  GLU A  28           
SHEET    4   C 4 ILE A  85  ILE A  91 -1  O  PHE A  89   N  TYR A  63           
SHEET    1   D 3 LYS C  18  PRO C  19  0                                        
SHEET    2   D 3 ILE C   6  ASP C  13 -1  N  ASP C  13   O  LYS C  18           
SHEET    3   D 3 HIS C  97  HIS C  99  1  O  TYR C  98   N  ILE C   6           
SHEET    1   E 4 ARG C  48  ILE C  49  0                                        
SHEET    2   E 4 ILE C   6  ASP C  13 -1  N  VAL C   9   O  ILE C  49           
SHEET    3   E 4 LEU C 102  SER C 105  1  O  LEU C 102   N  LEU C  12           
SHEET    4   E 4 GLY C 108  THR C 111 -1  O  SER C 110   N  LEU C 103           
SHEET    1   F 4 TRP C  35  HIS C  42  0                                        
SHEET    2   F 4 GLU C  24  LYS C  30 -1  N  VAL C  25   O  GLY C  41           
SHEET    3   F 4 GLY C  61  PHE C  67 -1  O  ARG C  64   N  GLU C  28           
SHEET    4   F 4 ILE C  85  ILE C  91 -1  O  PHE C  89   N  TYR C  63           
CISPEP   1 LEU A   52    TRP A   53          0         6.79                     
CISPEP   2 GLY A  114    SER A  115          0         4.90                     
CISPEP   3 LEU C   52    TRP C   53          0         7.07                     
CISPEP   4 GLY C  114    SER C  115          0         4.60                     
SITE     1 AC1  5 ASP C  44  GLN C  45  ASP C  46  LYS C  50                    
SITE     2 AC1  5 HIS C  97                                                     
SITE     1 AC2  5 ASP A  44  GLN A  45  ASP A  46  LYS A  50                    
SITE     2 AC2  5 HIS A  97                                                     
CRYST1   94.705   94.705   57.381  90.00  90.00 120.00 P 6          12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010559  0.006096  0.000000        0.00000                         
SCALE2      0.000000  0.012193  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017427        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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