GenomeNet

Database: PDB
Entry: 1Y23
LinkDB: 1Y23
Original site: 1Y23 
HEADER    CELL CYCLE                              19-NOV-04   1Y23              
TITLE     CRYSTAL STRUCTURE OF A MEMBER OF HIT FAMILY OF PROTEINS FROM BACILLUS 
TITLE    2 SUBTILIS                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTIDINE TRIAD PROTEIN;                                   
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 SYNONYM: HIT;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: YHAE, HIT;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834, DE3;                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET T7                                    
KEYWDS    HIT PROTEIN; PKCI-1; CELL-CYCLE REGULATION; HISTIDINE TRIAD; NYSGXRC; 
KEYWDS   2 STRUCTURAL GENOMICS; PROTEIN STRUCTURE INITIATIVE; T2097; NEW YORK   
KEYWDS   3 SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS; PSI, CELL CYCLE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.RAJASHANKAR,C.D.LIMA,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR  
AUTHOR   2 STRUCTURAL GENOMICS (NYSGXRC)                                        
REVDAT   5   03-FEB-21 1Y23    1       AUTHOR REMARK LINK                       
REVDAT   4   03-OCT-18 1Y23    1       REMARK                                   
REVDAT   3   24-FEB-09 1Y23    1       VERSN                                    
REVDAT   2   25-JAN-05 1Y23    1       AUTHOR REMARK                            
REVDAT   1   07-DEC-04 1Y23    0                                                
JRNL        AUTH   K.R.RAJASHANKAR,C.D.LIMA                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A MEMBER OF HIT FAMILY OF PROTEINS FROM 
JRNL        TITL 2 BACILLUS SUBTILIS                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 248233.080                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33077                          
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) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1644                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4817                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 270                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5561                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 287                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.35000                                              
REMARK   3    B22 (A**2) : 4.35000                                              
REMARK   3    B33 (A**2) : -8.70000                                             
REMARK   3    B12 (A**2) : 3.27000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
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) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.830                           
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) : 1.260 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.950 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.020 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.850 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 41.85                                                
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  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Y23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-NOV-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000031018.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9800                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 17.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.36300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: EXPERIMENTAL ELECTRON DENSITY MAP FROM HG SIRAS      
REMARK 200  DENSITY MODIFIED PHASES                                             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 19.5% PEG 4000, 0.5M AMMONIUM ACETATE,   
REMARK 280  0.1M SODIUM CITRATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       60.01533            
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      120.03067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      120.03067            
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       60.01533            
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 300 REMARK: BIOLOGICAL MOLECULE IS A DIMER. PROTOMERS A AND B TOGETHER   
REMARK 300 FORM ONE BIOLOGICAL ASSEMBLY AND SO DO PROTOMERS C AND D. THE        
REMARK 300 PARTNER PROTOMER FOR MOLECULE E IS GENERATED BY THE                  
REMARK 300 CRYSTALLOGRAPHIC TWO FOLD OPERATION X, -Y, -Z+2/3                    
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      120.03067            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     CYS A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     SER A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     CYS B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     MET C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     CYS C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     ALA C   143                                                      
REMARK 465     SER C   144                                                      
REMARK 465     SER C   145                                                      
REMARK 465     MET D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     CYS D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     SER D   144                                                      
REMARK 465     SER D   145                                                      
REMARK 465     MET E     1                                                      
REMARK 465     HIS E     2                                                      
REMARK 465     CYS E     3                                                      
REMARK 465     ALA E     4                                                      
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    HIS A 122       43.31   -140.45                                   
REMARK 500    LEU A 142       34.74    -75.61                                   
REMARK 500    ASN B   6       39.74    -91.24                                   
REMARK 500    GLN B  36       65.30     37.81                                   
REMARK 500    GLU B  80       57.30     37.42                                   
REMARK 500    HIS B 122       28.56   -151.41                                   
REMARK 500    ASP C  25     -157.57   -155.34                                   
REMARK 500    TYR C  64      -61.20    -96.72                                   
REMARK 500    GLU D  24      149.75   -175.90                                   
REMARK 500    HIS D  41      109.44    -48.19                                   
REMARK 500    TYR D  64      -67.82   -100.99                                   
REMARK 500    GLU D  80       63.02     35.72                                   
REMARK 500    ASP E  25     -159.37   -136.39                                   
REMARK 500    GLN E  36       65.58     39.93                                   
REMARK 500    TYR E  64      -69.41    -96.38                                   
REMARK 500    HIS E 122       30.10   -145.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A   7   SG                                                     
REMARK 620 2 CYS A  10   SG  109.6                                              
REMARK 620 3 HIS A  49   ND1 124.2 101.1                                        
REMARK 620 4 HIS A 100   ND1  97.6 109.5 114.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B   7   SG                                                     
REMARK 620 2 CYS B  10   SG  115.3                                              
REMARK 620 3 HIS B  49   ND1 128.2  99.4                                        
REMARK 620 4 HIS B 100   ND1 102.3 110.1 100.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B 141   O                                                      
REMARK 620 2 SER B 144   OG   85.8                                              
REMARK 620 3 HOH B2023   O    75.4  83.4                                        
REMARK 620 4 HOH B2035   O   100.1 154.8  74.6                                  
REMARK 620 5 HOH B2036   O    93.8  92.5 168.6 111.3                            
REMARK 620 6 ASP E 125   O   159.4  77.7  90.3  90.0  99.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C   7   SG                                                     
REMARK 620 2 CYS C  10   SG  118.7                                              
REMARK 620 3 HIS C  49   ND1 112.2 107.7                                        
REMARK 620 4 HIS C 100   ND1 109.2 111.8  94.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D   7   SG                                                     
REMARK 620 2 CYS D  10   SG  113.6                                              
REMARK 620 3 HIS D  49   ND1 115.6 100.6                                        
REMARK 620 4 HIS D 100   ND1 103.4 112.6 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E1005  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E   7   SG                                                     
REMARK 620 2 CYS E  10   SG  116.6                                              
REMARK 620 3 HIS E  49   ND1 120.5 101.7                                        
REMARK 620 4 HIS E 100   ND1 105.2 116.7  94.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 1005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T2097   RELATED DB: TARGETDB                     
DBREF  1Y23 A    1   145  UNP    O07513   HIT_BACSU        1    145             
DBREF  1Y23 B    1   145  UNP    O07513   HIT_BACSU        1    145             
DBREF  1Y23 C    1   145  UNP    O07513   HIT_BACSU        1    145             
DBREF  1Y23 D    1   145  UNP    O07513   HIT_BACSU        1    145             
DBREF  1Y23 E    1   145  UNP    O07513   HIT_BACSU        1    145             
SEQRES   1 A  145  MET HIS CYS ALA GLU ASN CYS ILE PHE CYS LYS ILE ILE          
SEQRES   2 A  145  ALA GLY ASP ILE PRO SER ALA LYS VAL TYR GLU ASP GLU          
SEQRES   3 A  145  HIS VAL LEU ALA PHE LEU ASP ILE SER GLN VAL THR LYS          
SEQRES   4 A  145  GLY HIS THR LEU VAL ILE PRO LYS THR HIS ILE GLU ASN          
SEQRES   5 A  145  VAL TYR GLU PHE THR ASP GLU LEU ALA LYS GLN TYR PHE          
SEQRES   6 A  145  HIS ALA VAL PRO LYS ILE ALA ARG ALA ILE ARG ASP GLU          
SEQRES   7 A  145  PHE GLU PRO ILE GLY LEU ASN THR LEU ASN ASN ASN GLY          
SEQRES   8 A  145  GLU LYS ALA GLY GLN SER VAL PHE HIS TYR HIS MET HIS          
SEQRES   9 A  145  ILE ILE PRO ARG TYR GLY LYS GLY ASP GLY PHE GLY ALA          
SEQRES  10 A  145  VAL TRP LYS THR HIS ALA ASP ASP TYR LYS PRO GLU ASP          
SEQRES  11 A  145  LEU GLN ASN ILE SER SER SER ILE ALA LYS ARG LEU ALA          
SEQRES  12 A  145  SER SER                                                      
SEQRES   1 B  145  MET HIS CYS ALA GLU ASN CYS ILE PHE CYS LYS ILE ILE          
SEQRES   2 B  145  ALA GLY ASP ILE PRO SER ALA LYS VAL TYR GLU ASP GLU          
SEQRES   3 B  145  HIS VAL LEU ALA PHE LEU ASP ILE SER GLN VAL THR LYS          
SEQRES   4 B  145  GLY HIS THR LEU VAL ILE PRO LYS THR HIS ILE GLU ASN          
SEQRES   5 B  145  VAL TYR GLU PHE THR ASP GLU LEU ALA LYS GLN TYR PHE          
SEQRES   6 B  145  HIS ALA VAL PRO LYS ILE ALA ARG ALA ILE ARG ASP GLU          
SEQRES   7 B  145  PHE GLU PRO ILE GLY LEU ASN THR LEU ASN ASN ASN GLY          
SEQRES   8 B  145  GLU LYS ALA GLY GLN SER VAL PHE HIS TYR HIS MET HIS          
SEQRES   9 B  145  ILE ILE PRO ARG TYR GLY LYS GLY ASP GLY PHE GLY ALA          
SEQRES  10 B  145  VAL TRP LYS THR HIS ALA ASP ASP TYR LYS PRO GLU ASP          
SEQRES  11 B  145  LEU GLN ASN ILE SER SER SER ILE ALA LYS ARG LEU ALA          
SEQRES  12 B  145  SER SER                                                      
SEQRES   1 C  145  MET HIS CYS ALA GLU ASN CYS ILE PHE CYS LYS ILE ILE          
SEQRES   2 C  145  ALA GLY ASP ILE PRO SER ALA LYS VAL TYR GLU ASP GLU          
SEQRES   3 C  145  HIS VAL LEU ALA PHE LEU ASP ILE SER GLN VAL THR LYS          
SEQRES   4 C  145  GLY HIS THR LEU VAL ILE PRO LYS THR HIS ILE GLU ASN          
SEQRES   5 C  145  VAL TYR GLU PHE THR ASP GLU LEU ALA LYS GLN TYR PHE          
SEQRES   6 C  145  HIS ALA VAL PRO LYS ILE ALA ARG ALA ILE ARG ASP GLU          
SEQRES   7 C  145  PHE GLU PRO ILE GLY LEU ASN THR LEU ASN ASN ASN GLY          
SEQRES   8 C  145  GLU LYS ALA GLY GLN SER VAL PHE HIS TYR HIS MET HIS          
SEQRES   9 C  145  ILE ILE PRO ARG TYR GLY LYS GLY ASP GLY PHE GLY ALA          
SEQRES  10 C  145  VAL TRP LYS THR HIS ALA ASP ASP TYR LYS PRO GLU ASP          
SEQRES  11 C  145  LEU GLN ASN ILE SER SER SER ILE ALA LYS ARG LEU ALA          
SEQRES  12 C  145  SER SER                                                      
SEQRES   1 D  145  MET HIS CYS ALA GLU ASN CYS ILE PHE CYS LYS ILE ILE          
SEQRES   2 D  145  ALA GLY ASP ILE PRO SER ALA LYS VAL TYR GLU ASP GLU          
SEQRES   3 D  145  HIS VAL LEU ALA PHE LEU ASP ILE SER GLN VAL THR LYS          
SEQRES   4 D  145  GLY HIS THR LEU VAL ILE PRO LYS THR HIS ILE GLU ASN          
SEQRES   5 D  145  VAL TYR GLU PHE THR ASP GLU LEU ALA LYS GLN TYR PHE          
SEQRES   6 D  145  HIS ALA VAL PRO LYS ILE ALA ARG ALA ILE ARG ASP GLU          
SEQRES   7 D  145  PHE GLU PRO ILE GLY LEU ASN THR LEU ASN ASN ASN GLY          
SEQRES   8 D  145  GLU LYS ALA GLY GLN SER VAL PHE HIS TYR HIS MET HIS          
SEQRES   9 D  145  ILE ILE PRO ARG TYR GLY LYS GLY ASP GLY PHE GLY ALA          
SEQRES  10 D  145  VAL TRP LYS THR HIS ALA ASP ASP TYR LYS PRO GLU ASP          
SEQRES  11 D  145  LEU GLN ASN ILE SER SER SER ILE ALA LYS ARG LEU ALA          
SEQRES  12 D  145  SER SER                                                      
SEQRES   1 E  145  MET HIS CYS ALA GLU ASN CYS ILE PHE CYS LYS ILE ILE          
SEQRES   2 E  145  ALA GLY ASP ILE PRO SER ALA LYS VAL TYR GLU ASP GLU          
SEQRES   3 E  145  HIS VAL LEU ALA PHE LEU ASP ILE SER GLN VAL THR LYS          
SEQRES   4 E  145  GLY HIS THR LEU VAL ILE PRO LYS THR HIS ILE GLU ASN          
SEQRES   5 E  145  VAL TYR GLU PHE THR ASP GLU LEU ALA LYS GLN TYR PHE          
SEQRES   6 E  145  HIS ALA VAL PRO LYS ILE ALA ARG ALA ILE ARG ASP GLU          
SEQRES   7 E  145  PHE GLU PRO ILE GLY LEU ASN THR LEU ASN ASN ASN GLY          
SEQRES   8 E  145  GLU LYS ALA GLY GLN SER VAL PHE HIS TYR HIS MET HIS          
SEQRES   9 E  145  ILE ILE PRO ARG TYR GLY LYS GLY ASP GLY PHE GLY ALA          
SEQRES  10 E  145  VAL TRP LYS THR HIS ALA ASP ASP TYR LYS PRO GLU ASP          
SEQRES  11 E  145  LEU GLN ASN ILE SER SER SER ILE ALA LYS ARG LEU ALA          
SEQRES  12 E  145  SER SER                                                      
HET     ZN  A1001       1                                                       
HET     ZN  B1002       1                                                       
HET     MG  B2001       1                                                       
HET     ZN  C1003       1                                                       
HET     ZN  D1004       1                                                       
HET     ZN  E1005       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   6   ZN    5(ZN 2+)                                                     
FORMUL   8   MG    MG 2+                                                        
FORMUL  12  HOH   *287(H2 O)                                                    
HELIX    1   1 CYS A    7  ALA A   14  1                                   8    
HELIX    2   2 ASN A   52  PHE A   56  5                                   5    
HELIX    3   3 THR A   57  GLN A   63  1                                   7    
HELIX    4   4 HIS A   66  GLU A   80  1                                  15    
HELIX    5   5 GLY A   91  GLY A   95  5                                   5    
HELIX    6   6 HIS A  122  TYR A  126  5                                   5    
HELIX    7   7 LYS A  127  LEU A  142  1                                  16    
HELIX    8   8 CYS B    7  ALA B   14  1                                   8    
HELIX    9   9 ASN B   52  PHE B   56  5                                   5    
HELIX   10  10 THR B   57  GLN B   63  1                                   7    
HELIX   11  11 HIS B   66  GLU B   80  1                                  15    
HELIX   12  12 GLY B   91  GLY B   95  5                                   5    
HELIX   13  13 HIS B  122  TYR B  126  5                                   5    
HELIX   14  14 LYS B  127  LEU B  142  1                                  16    
HELIX   15  15 ALA B  143  SER B  145  5                                   3    
HELIX   16  16 CYS C    7  GLY C   15  1                                   9    
HELIX   17  17 ASN C   52  PHE C   56  5                                   5    
HELIX   18  18 THR C   57  PHE C   65  1                                   9    
HELIX   19  19 HIS C   66  GLU C   80  1                                  15    
HELIX   20  20 GLY C   91  GLY C   95  5                                   5    
HELIX   21  21 HIS C  122  TYR C  126  5                                   5    
HELIX   22  22 LYS C  127  LEU C  142  1                                  16    
HELIX   23  23 CYS D    7  GLY D   15  1                                   9    
HELIX   24  24 ASN D   52  PHE D   56  5                                   5    
HELIX   25  25 THR D   57  PHE D   65  1                                   9    
HELIX   26  26 HIS D   66  GLU D   80  1                                  15    
HELIX   27  27 GLY D   91  GLY D   95  5                                   5    
HELIX   28  28 HIS D  122  TYR D  126  5                                   5    
HELIX   29  29 LYS D  127  ARG D  141  1                                  15    
HELIX   30  30 CYS E    7  ALA E   14  1                                   8    
HELIX   31  31 ASN E   52  PHE E   56  5                                   5    
HELIX   32  32 THR E   57  PHE E   65  1                                   9    
HELIX   33  33 HIS E   66  GLU E   80  1                                  15    
HELIX   34  34 GLY E   91  GLY E   95  5                                   5    
HELIX   35  35 HIS E  122  TYR E  126  5                                   5    
HELIX   36  36 LYS E  127  ARG E  141  1                                  15    
SHEET    1   A10 LYS A  21  GLU A  24  0                                        
SHEET    2   A10 VAL A  28  LEU A  32 -1  O  ALA A  30   N  TYR A  23           
SHEET    3   A10 THR A  42  PRO A  46 -1  O  LEU A  43   N  PHE A  31           
SHEET    4   A10 MET A 103  ARG A 108 -1  O  ILE A 105   N  THR A  42           
SHEET    5   A10 GLY A  83  ASN A  90 -1  N  LEU A  87   O  HIS A 104           
SHEET    6   A10 GLY B  83  ASN B  90 -1  O  THR B  86   N  ASN A  88           
SHEET    7   A10 MET B 103  ARG B 108 -1  O  HIS B 104   N  LEU B  87           
SHEET    8   A10 THR B  42  PRO B  46 -1  N  THR B  42   O  ILE B 105           
SHEET    9   A10 VAL B  28  LEU B  32 -1  N  PHE B  31   O  LEU B  43           
SHEET   10   A10 LYS B  21  GLU B  24 -1  N  TYR B  23   O  ALA B  30           
SHEET    1   B 2 PHE A 115  TRP A 119  0                                        
SHEET    2   B 2 PHE B 115  TRP B 119 -1  O  GLY B 116   N  VAL A 118           
SHEET    1   C10 LYS C  21  GLU C  24  0                                        
SHEET    2   C10 VAL C  28  LEU C  32 -1  O  ALA C  30   N  TYR C  23           
SHEET    3   C10 THR C  42  PRO C  46 -1  O  ILE C  45   N  LEU C  29           
SHEET    4   C10 MET C 103  ARG C 108 -1  O  ILE C 105   N  THR C  42           
SHEET    5   C10 GLY C  83  ASN C  90 -1  N  LEU C  87   O  HIS C 104           
SHEET    6   C10 GLY D  83  ASN D  90 -1  O  ASN D  90   N  LEU C  84           
SHEET    7   C10 MET D 103  ARG D 108 -1  O  HIS D 104   N  LEU D  87           
SHEET    8   C10 THR D  42  PRO D  46 -1  N  THR D  42   O  ILE D 105           
SHEET    9   C10 VAL D  28  LEU D  32 -1  N  PHE D  31   O  LEU D  43           
SHEET   10   C10 LYS D  21  GLU D  24 -1  N  VAL D  22   O  ALA D  30           
SHEET    1   D 2 PHE C 115  TRP C 119  0                                        
SHEET    2   D 2 PHE D 115  TRP D 119 -1  O  VAL D 118   N  GLY C 116           
SHEET    1   E 5 LYS E  21  GLU E  24  0                                        
SHEET    2   E 5 VAL E  28  LEU E  32 -1  O  ALA E  30   N  TYR E  23           
SHEET    3   E 5 THR E  42  PRO E  46 -1  O  LEU E  43   N  PHE E  31           
SHEET    4   E 5 MET E 103  ARG E 108 -1  O  ILE E 105   N  THR E  42           
SHEET    5   E 5 GLY E  83  ASN E  88 -1  N  GLY E  83   O  ARG E 108           
LINK         SG  CYS A   7                ZN    ZN A1001     1555   1555  2.30  
LINK         SG  CYS A  10                ZN    ZN A1001     1555   1555  2.13  
LINK         ND1 HIS A  49                ZN    ZN A1001     1555   1555  1.88  
LINK         ND1 HIS A 100                ZN    ZN A1001     1555   1555  2.16  
LINK         SG  CYS B   7                ZN    ZN B1002     1555   1555  2.32  
LINK         SG  CYS B  10                ZN    ZN B1002     1555   1555  2.46  
LINK         ND1 HIS B  49                ZN    ZN B1002     1555   1555  2.17  
LINK         ND1 HIS B 100                ZN    ZN B1002     1555   1555  2.11  
LINK         O   ARG B 141                MG    MG B2001     1555   1555  2.33  
LINK         OG  SER B 144                MG    MG B2001     1555   1555  2.44  
LINK        MG    MG B2001                 O   HOH B2023     1555   1555  2.66  
LINK        MG    MG B2001                 O   HOH B2035     1555   1555  2.85  
LINK        MG    MG B2001                 O   HOH B2036     1555   1555  2.54  
LINK        MG    MG B2001                 O   ASP E 125     1555   1565  2.27  
LINK         SG  CYS C   7                ZN    ZN C1003     1555   1555  2.25  
LINK         SG  CYS C  10                ZN    ZN C1003     1555   1555  2.26  
LINK         ND1 HIS C  49                ZN    ZN C1003     1555   1555  2.06  
LINK         ND1 HIS C 100                ZN    ZN C1003     1555   1555  2.11  
LINK         SG  CYS D   7                ZN    ZN D1004     1555   1555  2.24  
LINK         SG  CYS D  10                ZN    ZN D1004     1555   1555  2.35  
LINK         ND1 HIS D  49                ZN    ZN D1004     1555   1555  2.09  
LINK         ND1 HIS D 100                ZN    ZN D1004     1555   1555  2.14  
LINK         SG  CYS E   7                ZN    ZN E1005     1555   1555  2.25  
LINK         SG  CYS E  10                ZN    ZN E1005     1555   1555  2.36  
LINK         ND1 HIS E  49                ZN    ZN E1005     1555   1555  2.03  
LINK         ND1 HIS E 100                ZN    ZN E1005     1555   1555  2.08  
SITE     1 AC1  4 CYS A   7  CYS A  10  HIS A  49  HIS A 100                    
SITE     1 AC2  4 CYS B   7  CYS B  10  HIS B  49  HIS B 100                    
SITE     1 AC3  4 CYS C   7  CYS C  10  HIS C  49  HIS C 100                    
SITE     1 AC4  4 CYS D   7  CYS D  10  HIS D  49  HIS D 100                    
SITE     1 AC5  4 CYS E   7  CYS E  10  HIS E  49  HIS E 100                    
SITE     1 AC6  6 ARG B 141  SER B 144  HOH B2023  HOH B2035                    
SITE     2 AC6  6 HOH B2036  ASP E 125                                          
CRYST1   86.444   86.444  180.046  90.00  90.00 120.00 P 31 2 1     30          
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      0.011568  0.006679  0.000000        0.00000                         
SCALE2      0.000000  0.013358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005554        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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