GenomeNet

Database: PDB
Entry: 2QZB
LinkDB: 2QZB
Original site: 2QZB 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   16-AUG-07   2QZB              
TITLE     CRYSTAL STRUCTURE OF THE UNCHARACTERIZED PROTEIN YFEY FROM ESCHERICHIA
TITLE    2 COLI                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN YFEY;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 28-191;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: YFEY, B2432, JW2425;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26                            
KEYWDS    STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, PROTEIN STRUCTURE       
KEYWDS   2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,    
KEYWDS   3 NYSGXRC                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.BONANNO,M.GILMORE,K.T.BAIN,B.WU,R.ROMERO,D.SMITH,S.WASSERMAN,     
AUTHOR   2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR      
AUTHOR   3 STRUCTURAL GENOMICS (NYSGXRC)                                        
REVDAT   6   03-FEB-21 2QZB    1       AUTHOR JRNL   SEQADV                     
REVDAT   5   14-NOV-18 2QZB    1       AUTHOR                                   
REVDAT   4   25-OCT-17 2QZB    1       REMARK                                   
REVDAT   3   13-JUL-11 2QZB    1       VERSN                                    
REVDAT   2   24-FEB-09 2QZB    1       VERSN                                    
REVDAT   1   28-AUG-07 2QZB    0                                                
JRNL        AUTH   J.B.BONANNO,M.GILMORE,K.T.BAIN,B.WU,R.ROMERO,D.SMITH,        
JRNL        AUTH 2 S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE UNCHARACTERIZED PROTEIN YFEY FROM   
JRNL        TITL 2 ESCHERICHIA COLI.                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18913                          
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) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 971                             
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1221                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2233                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 113                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.12000                                             
REMARK   3    B22 (A**2) : -1.12000                                             
REMARK   3    B33 (A**2) : 2.24000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
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): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.394         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.883                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2275 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3063 ; 1.543 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   287 ; 6.659 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;36.084 ;24.757       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   400 ;17.023 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;20.905 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   335 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1705 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   855 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1530 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   152 ; 0.162 ; 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):    77 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.179 ; 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):  1481 ; 1.151 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2295 ; 1.968 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   918 ; 2.824 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   767 ; 4.470 ; 4.500       
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 : 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                                                           
REMARK   4                                                                      
REMARK   4 2QZB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000044233.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97958                            
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA, SCALEPACK                   
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18942                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.450                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.23800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXCD                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 8.5, 2M AMMONIUM       
REMARK 280  SULFATE, VAPOR DIFFUSION, TEMPERATURE 294K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      210.13050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       18.79950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       18.79950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      105.06525            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       18.79950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       18.79950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      315.19575            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       18.79950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       18.79950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      105.06525            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       18.79950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       18.79950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      315.19575            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      210.13050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND PROGRAM                   
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. AUTHORS STATE THAT THE MONOMERIC ASSEMBLY                
REMARK 300 SHOWN IN REMARK 350 IS PROBABLE.                                     
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     TRP A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     TRP A    34                                                      
REMARK 465     PHE A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     ASP A   100                                                      
REMARK 465     GLN A   101                                                      
REMARK 465     ASP A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     ASP A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     ARG A   146                                                      
REMARK 465     SER B    26                                                      
REMARK 465     LEU B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     TRP B    32                                                      
REMARK 465     ASN B    33                                                      
REMARK 465     TRP B    34                                                      
REMARK 465     PHE B    35                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     SER B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     ASP B    65                                                      
REMARK 465     GLY B    66                                                      
REMARK 465     ASP B    67                                                      
REMARK 465     GLN B   101                                                      
REMARK 465     ASP B   143                                                      
REMARK 465     ASP B   144                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    86     O    HOH A   248              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 134      123.77    -39.84                                   
REMARK 500    LYS B  75     -154.20   -153.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-10326A   RELATED DB: TARGETDB                    
DBREF  2QZB A   28   191  UNP    P76537   YFEY_ECOLI      28    191             
DBREF  2QZB B   28   191  UNP    P76537   YFEY_ECOLI      28    191             
SEQADV 2QZB SER A   26  UNP  P76537              EXPRESSION TAG                 
SEQADV 2QZB LEU A   27  UNP  P76537              EXPRESSION TAG                 
SEQADV 2QZB SER B   26  UNP  P76537              EXPRESSION TAG                 
SEQADV 2QZB LEU B   27  UNP  P76537              EXPRESSION TAG                 
SEQRES   1 A  166  SER LEU ALA ALA ASN PRO TRP ASN TRP PHE GLY SER SER          
SEQRES   2 A  166  THR LYS VAL SER GLU GLN GLY VAL GLY GLU LEU THR ALA          
SEQRES   3 A  166  SER THR PRO LEU GLN GLU GLN ALA ILE ALA ASP ALA LEU          
SEQRES   4 A  166  ASP GLY ASP TYR ARG LEU ARG SER GLY MET LYS THR ALA          
SEQRES   5 A  166  ASN GLY ASN VAL VAL ARG PHE PHE GLU VAL MET LYS GLY          
SEQRES   6 A  166  ASP ASN VAL ALA MET VAL ILE ASN GLY ASP GLN GLY THR          
SEQRES   7 A  166  ILE SER ARG ILE ASP VAL LEU ASP SER ASP ILE PRO ALA          
SEQRES   8 A  166  ASP THR GLY VAL LYS ILE GLY THR PRO PHE SER ASP LEU          
SEQRES   9 A  166  TYR SER LYS ALA PHE GLY ASN CYS GLN LYS ALA ASP GLY          
SEQRES  10 A  166  ASP ASP ASN ARG ALA VAL GLU CYS LYS ALA GLU GLY SER          
SEQRES  11 A  166  GLN HIS ILE SER TYR GLN PHE SER GLY GLU TRP ARG GLY          
SEQRES  12 A  166  PRO GLU GLY LEU MET PRO SER ASP ASP THR LEU LYS ASN          
SEQRES  13 A  166  TRP LYS VAL SER LYS ILE ILE TRP ARG ARG                      
SEQRES   1 B  166  SER LEU ALA ALA ASN PRO TRP ASN TRP PHE GLY SER SER          
SEQRES   2 B  166  THR LYS VAL SER GLU GLN GLY VAL GLY GLU LEU THR ALA          
SEQRES   3 B  166  SER THR PRO LEU GLN GLU GLN ALA ILE ALA ASP ALA LEU          
SEQRES   4 B  166  ASP GLY ASP TYR ARG LEU ARG SER GLY MET LYS THR ALA          
SEQRES   5 B  166  ASN GLY ASN VAL VAL ARG PHE PHE GLU VAL MET LYS GLY          
SEQRES   6 B  166  ASP ASN VAL ALA MET VAL ILE ASN GLY ASP GLN GLY THR          
SEQRES   7 B  166  ILE SER ARG ILE ASP VAL LEU ASP SER ASP ILE PRO ALA          
SEQRES   8 B  166  ASP THR GLY VAL LYS ILE GLY THR PRO PHE SER ASP LEU          
SEQRES   9 B  166  TYR SER LYS ALA PHE GLY ASN CYS GLN LYS ALA ASP GLY          
SEQRES  10 B  166  ASP ASP ASN ARG ALA VAL GLU CYS LYS ALA GLU GLY SER          
SEQRES  11 B  166  GLN HIS ILE SER TYR GLN PHE SER GLY GLU TRP ARG GLY          
SEQRES  12 B  166  PRO GLU GLY LEU MET PRO SER ASP ASP THR LEU LYS ASN          
SEQRES  13 B  166  TRP LYS VAL SER LYS ILE ILE TRP ARG ARG                      
FORMUL   3  HOH   *113(H2 O)                                                    
HELIX    1   1 GLN A   56  LEU A   64  1                                   9    
HELIX    2   2 PRO A  125  TYR A  130  1                                   6    
HELIX    3   3 SER A  175  LYS A  180  1                                   6    
HELIX    4   4 GLN B   56  LEU B   64  1                                   9    
HELIX    5   5 PRO B  125  TYR B  130  1                                   6    
HELIX    6   6 SER B  175  LYS B  180  1                                   6    
SHEET    1   A 2 VAL A  41  SER A  42  0                                        
SHEET    2   A 2 GLY A  45  VAL A  46 -1  O  GLY A  45   N  SER A  42           
SHEET    1   B 8 ARG A  69  ALA A  77  0                                        
SHEET    2   B 8 ASN A  80  LYS A  89 -1  O  VAL A  82   N  LYS A  75           
SHEET    3   B 8 ASN A  92  ASN A  98 -1  O  ASN A  92   N  LYS A  89           
SHEET    4   B 8 ARG A 106  VAL A 109 -1  O  ARG A 106   N  ASN A  98           
SHEET    5   B 8 LYS A 183  ARG A 190 -1  O  ILE A 187   N  VAL A 109           
SHEET    6   B 8 ILE A 158  SER A 163 -1  N  SER A 159   O  ILE A 188           
SHEET    7   B 8 VAL A 148  LYS A 151 -1  N  VAL A 148   O  PHE A 162           
SHEET    8   B 8 CYS A 137  GLN A 138 -1  N  GLN A 138   O  GLU A 149           
SHEET    1   C 3 VAL B  41  SER B  42  0                                        
SHEET    2   C 3 GLY B  45  VAL B  46 -1  O  GLY B  45   N  SER B  42           
SHEET    3   C 3 LEU B  49  THR B  50 -1  O  LEU B  49   N  VAL B  46           
SHEET    1   D 8 ARG B  69  ALA B  77  0                                        
SHEET    2   D 8 ASN B  80  LYS B  89 -1  O  MET B  88   N  ARG B  69           
SHEET    3   D 8 ASN B  92  GLY B  99 -1  O  ILE B  97   N  PHE B  85           
SHEET    4   D 8 ILE B 104  VAL B 109 -1  O  ARG B 106   N  ASN B  98           
SHEET    5   D 8 LYS B 183  ARG B 190 -1  O  ILE B 187   N  VAL B 109           
SHEET    6   D 8 ILE B 158  SER B 163 -1  N  SER B 159   O  ILE B 188           
SHEET    7   D 8 VAL B 148  LYS B 151 -1  N  VAL B 148   O  PHE B 162           
SHEET    8   D 8 CYS B 137  LYS B 139 -1  N  GLN B 138   O  GLU B 149           
SSBOND   1 CYS A  137    CYS A  150                          1555   1555  2.05  
SSBOND   2 CYS B  137    CYS B  150                          1555   1555  2.08  
CRYST1   37.599   37.599  420.261  90.00  90.00  90.00 P 41 21 2    16          
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      0.026596  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.026596  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002379        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system