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Database: PDB
Entry: 3CV1
LinkDB: 3CV1
Original site: 3CV1 
HEADER    TRANSFERASE                             17-APR-08   3CV1              
TITLE     ATOMIC RESOLUTION STRUCTURES OF ESCHERICHIA COLI AND BACILLIS         
TITLE    2 ANTHRACIS MALATE SYNTHASE A: COMPARISON WITH ISOFORM G AND           
TITLE    3 IMPLICATIONS FOR STRUCTURE BASED DRUG DESIGN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALATE SYNTHASE A;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MSA;                                                        
COMPND   5 EC: 2.3.3.9;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: ACEB, MAS;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBAD                                      
KEYWDS    MALATE SYNTHASE, TIM BARREL, GLYOXYLATE BYPASS, TRANSFERASE,          
KEYWDS   2 TRICARBOXYLIC ACID CYCLE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.LOHMAN                                                            
REVDAT   5   21-FEB-24 3CV1    1       REMARK LINK                              
REVDAT   4   25-OCT-17 3CV1    1       REMARK                                   
REVDAT   3   13-JUL-11 3CV1    1       VERSN                                    
REVDAT   2   24-FEB-09 3CV1    1       VERSN                                    
REVDAT   1   11-NOV-08 3CV1    0                                                
JRNL        AUTH   J.R.LOHMAN,A.C.OLSON,S.J.REMINGTON                           
JRNL        TITL   ATOMIC RESOLUTION STRUCTURES OF ESCHERICHIA COLI AND         
JRNL        TITL 2 BACILLUS ANTHRACIS MALATE SYNTHASE A: COMPARISON WITH        
JRNL        TITL 3 ISOFORM G AND IMPLICATIONS FOR STRUCTURE-BASED DRUG          
JRNL        TITL 4 DISCOVERY                                                    
JRNL        REF    PROTEIN SCI.                  V.  17  1935 2008              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   18714089                                                     
JRNL        DOI    10.1110/PS.036269.108                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 56011                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2970                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.68                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.73                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3877                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.4850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4187                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 504                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.110         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.105         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.065         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.914         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4348 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5913 ; 1.223 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   546 ; 5.525 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   211 ;31.744 ;24.171       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   731 ;12.007 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;14.279 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   648 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3358 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2173 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3009 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   376 ; 0.112 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     6 ; 0.185 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    53 ; 0.176 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.134 ; 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):  2752 ; 0.656 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4311 ; 1.014 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1829 ; 1.764 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1596 ; 2.688 ; 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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 3CV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047244.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59002                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
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) : 1.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7.5, 0.2M CALCIUM           
REMARK 280  ACETATE, 22% PEG 8K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.06200            
REMARK 290   SMTRY3   2  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 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 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     THR A     2                                                      
REMARK 465     GLU A     3                                                      
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     GLN A   4    N    CA   CB   CG   CD   OE1  NE2                   
REMARK 470     GLU A  69    CD   OE1  OE2                                       
REMARK 470     LYS A 101    NZ                                                  
REMARK 470     GLU A 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 157    CG   CD   CE   NZ                                   
REMARK 470     LYS A 337    CB   CG   CD   CE   NZ                              
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 340    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 496    CG   CD   OE1  OE2                                  
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   O    HOH A   608     O    HOH A   972              1.88            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   830     O    HOH A   980     2755     2.15            
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    GLU A 119     -123.48   -100.86                                   
REMARK 500    SER A 207     -148.05   -108.06                                   
REMARK 500    PRO A 296     -168.19    -73.75                                   
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                              CA A   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  53   OE1                                                    
REMARK 620 2 GLN A  56   OE1  82.1                                              
REMARK 620 3 HOH A 684   O    81.0  88.8                                        
REMARK 620 4 HOH A 718   O    74.5  88.9 155.4                                  
REMARK 620 5 HOH A 814   O    80.8 162.1  83.4  91.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 534  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 250   OE1                                                    
REMARK 620 2 ASP A 278   OD2  86.5                                              
REMARK 620 3 HOH A 541   O    94.4 178.9                                        
REMARK 620 4 HOH A 657   O    80.0  86.5  94.2                                  
REMARK 620 5 HOH A 688   O    98.9  92.5  86.8 178.6                            
REMARK 620 6 HOH A 971   O   170.6  89.2  90.0  91.3  89.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 534                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 536                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1D8C   RELATED DB: PDB                                   
REMARK 900 ISOFORM                                                              
REMARK 900 RELATED ID: 3CUX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CUZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CV2   RELATED DB: PDB                                   
DBREF  3CV1 A    2   533  UNP    P08997   MASY_ECOLI       2    533             
SEQRES   1 A  532  THR GLU GLN ALA THR THR THR ASP GLU LEU ALA PHE THR          
SEQRES   2 A  532  ARG PRO TYR GLY GLU GLN GLU LYS GLN ILE LEU THR ALA          
SEQRES   3 A  532  GLU ALA VAL GLU PHE LEU THR GLU LEU VAL THR HIS PHE          
SEQRES   4 A  532  THR PRO GLN ARG ASN LYS LEU LEU ALA ALA ARG ILE GLN          
SEQRES   5 A  532  GLN GLN GLN ASP ILE ASP ASN GLY THR LEU PRO ASP PHE          
SEQRES   6 A  532  ILE SER GLU THR ALA SER ILE ARG ASP ALA ASP TRP LYS          
SEQRES   7 A  532  ILE ARG GLY ILE PRO ALA ASP LEU GLU ASP ARG ARG VAL          
SEQRES   8 A  532  GLU ILE THR GLY PRO VAL GLU ARG LYS MET VAL ILE ASN          
SEQRES   9 A  532  ALA LEU ASN ALA ASN VAL LYS VAL PHE MET ALA ASP PHE          
SEQRES  10 A  532  GLU ASP SER LEU ALA PRO ASP TRP ASN LYS VAL ILE ASP          
SEQRES  11 A  532  GLY GLN ILE ASN LEU ARG ASP ALA VAL ASN GLY THR ILE          
SEQRES  12 A  532  SER TYR THR ASN GLU ALA GLY LYS ILE TYR GLN LEU LYS          
SEQRES  13 A  532  PRO ASN PRO ALA VAL LEU ILE CYS ARG VAL ARG GLY LEU          
SEQRES  14 A  532  HIS LEU PRO GLU LYS HIS VAL THR TRP ARG GLY GLU ALA          
SEQRES  15 A  532  ILE PRO GLY SER LEU PHE ASP PHE ALA LEU TYR PHE PHE          
SEQRES  16 A  532  HIS ASN TYR GLN ALA LEU LEU ALA LYS GLY SER GLY PRO          
SEQRES  17 A  532  TYR PHE TYR LEU PRO LYS THR GLN SER TRP GLN GLU ALA          
SEQRES  18 A  532  ALA TRP TRP SER GLU VAL PHE SER TYR ALA GLU ASP ARG          
SEQRES  19 A  532  PHE ASN LEU PRO ARG GLY THR ILE LYS ALA THR LEU LEU          
SEQRES  20 A  532  ILE GLU THR LEU PRO ALA VAL PHE GLN MET ASP GLU ILE          
SEQRES  21 A  532  LEU HIS ALA LEU ARG ASP HIS ILE VAL GLY LEU ASN CYS          
SEQRES  22 A  532  GLY ARG TRP ASP TYR ILE PHE SER TYR ILE LYS THR LEU          
SEQRES  23 A  532  LYS ASN TYR PRO ASP ARG VAL LEU PRO ASP ARG GLN ALA          
SEQRES  24 A  532  VAL THR MET ASP LYS PRO PHE LEU ASN ALA TYR SER ARG          
SEQRES  25 A  532  LEU LEU ILE LYS THR CYS HIS LYS ARG GLY ALA PHE ALA          
SEQRES  26 A  532  MET GLY GLY MET ALA ALA PHE ILE PRO SER LYS ASP GLU          
SEQRES  27 A  532  GLU HIS ASN ASN GLN VAL LEU ASN LYS VAL LYS ALA ASP          
SEQRES  28 A  532  LYS SER LEU GLU ALA ASN ASN GLY HIS ASP GLY THR TRP          
SEQRES  29 A  532  ILE ALA HIS PRO GLY LEU ALA ASP THR ALA MET ALA VAL          
SEQRES  30 A  532  PHE ASN ASP ILE LEU GLY SER ARG LYS ASN GLN LEU GLU          
SEQRES  31 A  532  VAL MET ARG GLU GLN ASP ALA PRO ILE THR ALA ASP GLN          
SEQRES  32 A  532  LEU LEU ALA PRO CYS ASP GLY GLU ARG THR GLU GLU GLY          
SEQRES  33 A  532  MET ARG ALA ASN ILE ARG VAL ALA VAL GLN TYR ILE GLU          
SEQRES  34 A  532  ALA TRP ILE SER GLY ASN GLY CYS VAL PRO ILE TYR GLY          
SEQRES  35 A  532  LEU MET GLU ASP ALA ALA THR ALA GLU ILE SER ARG THR          
SEQRES  36 A  532  SER ILE TRP GLN TRP ILE HIS HIS GLN LYS THR LEU SER          
SEQRES  37 A  532  ASN GLY LYS PRO VAL THR LYS ALA LEU PHE ARG GLN MET          
SEQRES  38 A  532  LEU GLY GLU GLU MET LYS VAL ILE ALA SER GLU LEU GLY          
SEQRES  39 A  532  GLU GLU ARG PHE SER GLN GLY ARG PHE ASP ASP ALA ALA          
SEQRES  40 A  532  ARG LEU MET GLU GLN ILE THR THR SER ASP GLU LEU ILE          
SEQRES  41 A  532  ASP PHE LEU THR LEU PRO GLY TYR ARG LEU LEU ALA              
HET     CA  A   1       1                                                       
HET     CA  A 534       1                                                       
HET    ACT  A 535       4                                                       
HET    GOL  A 536       6                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *504(H2 O)                                                    
HELIX    1   1 GLY A   18  LEU A   25  1                                   8    
HELIX    2   2 THR A   26  ASN A   60  1                                  35    
HELIX    3   3 THR A   70  ASP A   75  1                                   6    
HELIX    4   4 PRO A   84  GLU A   88  5                                   5    
HELIX    5   5 GLU A   99  ASN A  108  1                                  10    
HELIX    6   6 ASP A  125  ASN A  141  1                                  17    
HELIX    7   7 GLY A  186  LYS A  205  1                                  20    
HELIX    8   8 SER A  218  PHE A  236  1                                  19    
HELIX    9   9 THR A  251  PHE A  256  1                                   6    
HELIX   10  10 GLN A  257  LEU A  265  1                                   9    
HELIX   11  11 ARG A  276  LEU A  287  1                                  12    
HELIX   12  12 ASP A  297  VAL A  301  5                                   5    
HELIX   13  13 LYS A  305  ARG A  322  1                                  18    
HELIX   14  14 ASP A  338  GLY A  360  1                                  23    
HELIX   15  15 HIS A  368  GLY A  370  5                                   3    
HELIX   16  16 LEU A  371  GLY A  384  1                                  14    
HELIX   17  17 THR A  401  ALA A  407  1                                   7    
HELIX   18  18 THR A  414  SER A  434  1                                  21    
HELIX   19  19 ASP A  447  HIS A  464  1                                  18    
HELIX   20  20 THR A  475  GLY A  495  1                                  21    
HELIX   21  21 GLY A  495  GLN A  501  1                                   7    
HELIX   22  22 ARG A  503  SER A  517  1                                  15    
HELIX   23  23 LEU A  524  ARG A  530  1                                   7    
SHEET    1   A 3 ALA A  12  PHE A  13  0                                        
SHEET    2   A 3 PRO A 173  TRP A 179 -1  O  THR A 178   N  ALA A  12           
SHEET    3   A 3 GLU A 182  PRO A 185 -1  O  GLU A 182   N  TRP A 179           
SHEET    1   B 9 VAL A  92  PRO A  97  0                                        
SHEET    2   B 9 VAL A 113  ASP A 117  1  O  MET A 115   N  ILE A  94           
SHEET    3   B 9 VAL A 162  ARG A 166  1  O  ARG A 166   N  ALA A 116           
SHEET    4   B 9 TYR A 210  LEU A 213  1  O  TYR A 210   N  CYS A 165           
SHEET    5   B 9 LYS A 244  LEU A 248  1  O  THR A 246   N  LEU A 213           
SHEET    6   B 9 ILE A 269  ASN A 273  1  O  GLY A 271   N  LEU A 247           
SHEET    7   B 9 PHE A 325  ALA A 331  1  O  MET A 327   N  LEU A 272           
SHEET    8   B 9 GLY A 363  ILE A 366  1  O  GLY A 363   N  GLY A 328           
SHEET    9   B 9 VAL A  92  PRO A  97  1  N  GLU A  93   O  THR A 364           
SHEET    1   C 2 SER A 145  THR A 147  0                                        
SHEET    2   C 2 ILE A 153  GLN A 155 -1  O  TYR A 154   N  TYR A 146           
SHEET    1   D 2 VAL A 439  ILE A 441  0                                        
SHEET    2   D 2 LEU A 444  GLU A 446 -1  O  LEU A 444   N  ILE A 441           
LINK        CA    CA A   1                 OE1 GLN A  53     1555   1555  2.45  
LINK        CA    CA A   1                 OE1 GLN A  56     1555   1555  2.24  
LINK        CA    CA A   1                 O   HOH A 684     1555   1555  2.34  
LINK        CA    CA A   1                 O   HOH A 718     1555   1555  2.47  
LINK        CA    CA A   1                 O   HOH A 814     1555   1555  2.44  
LINK         OE1 GLU A 250                CA    CA A 534     1555   1555  2.46  
LINK         OD2 ASP A 278                CA    CA A 534     1555   1555  2.36  
LINK        CA    CA A 534                 O   HOH A 541     1555   1555  2.31  
LINK        CA    CA A 534                 O   HOH A 657     1555   1555  2.33  
LINK        CA    CA A 534                 O   HOH A 688     1555   1555  2.50  
LINK        CA    CA A 534                 O   HOH A 971     1555   1555  2.04  
SITE     1 AC1  5 GLN A  53  GLN A  56  HOH A 684  HOH A 718                    
SITE     2 AC1  5 HOH A 814                                                     
SITE     1 AC2  6 GLU A 250  ASP A 278  HOH A 541  HOH A 657                    
SITE     2 AC2  6 HOH A 688  HOH A 971                                          
SITE     1 AC3  4 PHE A  13  TYR A  17  HOH A 870  HOH A 987                    
SITE     1 AC4  6 ILE A  73  TRP A 219  HIS A 263  ALA A 264                    
SITE     2 AC4  6 HOH A 784  HOH A 907                                          
CRYST1   52.031   74.124   71.917  90.00  97.82  90.00 P 1 21 1      2          
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      0.019219  0.000000  0.002639        0.00000                         
SCALE2      0.000000  0.013491  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014035        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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