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Database: PDB
Entry: 4LJA
LinkDB: 4LJA
Original site: 4LJA 
HEADER    CHAPERONE                               04-JUL-13   4LJA              
TITLE     CLPB NBD2 R621Q FROM T. THERMOPHILUS IN COMPLEX WITH AMPPCP AND       
TITLE    2 GUANIDINIUM CHLORIDE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHAPERONE PROTEIN CLPB;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: NUCLEOTIDE BINDING DOMAIN 2, UNP RESIDUES 520-854;         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8;                                                         
SOURCE   5 GENE: CLPB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    AAA+ PROTEIN, NUCLEOTIDE BINDING DOMAIN, MOLECULAR CHAPERONE,         
KEYWDS   2 DISAGGREGASE, CHAPERONE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.ZEYMER,T.R.M.BARENDS,N.D.WERBECK,I.SCHLICHTING,J.REINSTEIN          
REVDAT   4   08-NOV-23 4LJA    1       REMARK SEQADV LINK                       
REVDAT   3   15-NOV-17 4LJA    1       REMARK                                   
REVDAT   2   09-APR-14 4LJA    1       JRNL                                     
REVDAT   1   12-FEB-14 4LJA    0                                                
JRNL        AUTH   C.ZEYMER,T.R.M.BARENDS,N.D.WERBECK,I.SCHLICHTING,J.REINSTEIN 
JRNL        TITL   ELEMENTS IN NUCLEOTIDE SENSING AND HYDROLYSIS OF THE AAA+    
JRNL        TITL 2 DISAGGREGATION MACHINE CLPB: A STRUCTURE-BASED MECHANISTIC   
JRNL        TITL 3 DISSECTION OF A MOLECULAR MOTOR                              
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  70   582 2014              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   24531492                                                     
JRNL        DOI    10.1107/S1399004713030629                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 24325                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1256                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1797                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2550                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 77                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.30000                                              
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : -0.45000                                             
REMARK   3    B12 (A**2) : 0.15000                                              
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): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.218         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2634 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3569 ; 1.256 ; 2.000       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   320 ; 5.090 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   124 ;33.567 ;23.065       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   472 ;15.486 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;15.694 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1968 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1602 ; 0.489 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2588 ; 0.924 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1032 ; 1.613 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   980 ; 2.766 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   550        A   709                          
REMARK   3    RESIDUE RANGE :   A   741        A   755                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9822  26.5167  -9.1661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0768 T22:   0.0995                                     
REMARK   3      T33:   0.0677 T12:   0.0666                                     
REMARK   3      T13:   0.0221 T23:   0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3668 L22:   3.0169                                     
REMARK   3      L33:   2.6364 L12:  -0.3580                                     
REMARK   3      L13:  -0.0696 L23:  -0.0847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1149 S12:   0.5046 S13:   0.0054                       
REMARK   3      S21:  -0.2927 S22:  -0.2983 S23:  -0.3784                       
REMARK   3      S31:   0.0949 S32:   0.1062 S33:   0.1833                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   710        A   740                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2571  17.8513  11.7143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2955 T22:   0.1975                                     
REMARK   3      T33:   0.0640 T12:  -0.0645                                     
REMARK   3      T13:   0.0176 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.0622 L22:   5.3066                                     
REMARK   3      L33:   7.0046 L12:  -3.9353                                     
REMARK   3      L13:  -3.6150 L23:   0.7387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4709 S12:  -0.8545 S13:  -0.7934                       
REMARK   3      S21:   0.8213 S22:   0.1758 S23:   0.3551                       
REMARK   3      S31:   0.4917 S32:  -0.4396 S33:   0.2951                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   756        A   849                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.8456  40.5552 -10.5264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1109 T22:   0.1242                                     
REMARK   3      T33:   0.2874 T12:   0.0532                                     
REMARK   3      T13:  -0.0415 T23:  -0.0936                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2864 L22:   2.8926                                     
REMARK   3      L33:   4.1198 L12:  -1.0219                                     
REMARK   3      L13:   3.7308 L23:  -0.8983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3449 S12:  -0.2097 S13:   0.6165                       
REMARK   3      S21:   0.0198 S22:   0.1131 S23:   0.4526                       
REMARK   3      S31:  -0.4931 S32:  -0.2135 S33:   0.2318                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4LJA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080699.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9120                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25581                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.30                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.60                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.82100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4LJ5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL, 15% ISOPROPANOL, 10MM     
REMARK 280  MAGNESIUM CHLORIDE, 2MM AMPPCP, 100MM GUANIDINIUM CHLORIDE, PH      
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       79.66667            
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       39.83333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       59.75000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       19.91667            
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       99.58333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE FULL PROTEIN FORMS A RANGE OF OLIGOMERS, AND THIS        
REMARK 300 DOMAIN FORMS DIMERS IN SOLUTION UNDER CERTAIN CIRCUMSTANCES.         
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     GLY A   516                                                      
REMARK 465     SER A   517                                                      
REMARK 465     ARG A   546                                                      
REMARK 465     GLU A   547                                                      
REMARK 465     LYS A   548                                                      
REMARK 465     LEU A   549                                                      
REMARK 465     GLY A   642                                                      
REMARK 465     TYR A   643                                                      
REMARK 465     VAL A   644                                                      
REMARK 465     GLY A   645                                                      
REMARK 465     TYR A   646                                                      
REMARK 465     GLU A   647                                                      
REMARK 465     GLU A   648                                                      
REMARK 465     ALA A   850                                                      
REMARK 465     ARG A   851                                                      
REMARK 465     VAL A   852                                                      
REMARK 465     GLU A   853                                                      
REMARK 465     ALA A   854                                                      
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     GLU A 545    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 629    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 849    O                                                   
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    ASN A 585       30.77    -94.94                                   
REMARK 500    ASP A 614      -32.39     75.58                                   
REMARK 500    LEU A 816      -56.89   -120.68                                   
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                              MG A 902  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 602   OG1                                                    
REMARK 620 2 ACP A 901   O1G 176.2                                              
REMARK 620 3 ACP A 901   O1B  81.8  98.5                                        
REMARK 620 4 HOH A1001   O    92.7  91.1  91.8                                  
REMARK 620 5 HOH A1002   O    90.4  85.8  86.4 176.2                            
REMARK 620 6 HOH A1003   O    87.7  92.0 169.5  89.0  93.4                      
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 ACP A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 903                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LJ4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LJ5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LJ6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LJ7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LJ8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LJ9   RELATED DB: PDB                                   
DBREF  4LJA A  520   854  UNP    Q9RA63   CLPB_THET8     520    854             
SEQADV 4LJA GLY A  516  UNP  Q9RA63              EXPRESSION TAG                 
SEQADV 4LJA SER A  517  UNP  Q9RA63              EXPRESSION TAG                 
SEQADV 4LJA HIS A  518  UNP  Q9RA63              EXPRESSION TAG                 
SEQADV 4LJA MET A  519  UNP  Q9RA63              EXPRESSION TAG                 
SEQADV 4LJA GLN A  621  UNP  Q9RA63    ARG   621 ENGINEERED MUTATION            
SEQRES   1 A  339  GLY SER HIS MET GLU VAL THR GLU GLU ASP ILE ALA GLU          
SEQRES   2 A  339  ILE VAL SER ARG TRP THR GLY ILE PRO VAL SER LYS LEU          
SEQRES   3 A  339  LEU GLU GLY GLU ARG GLU LYS LEU LEU ARG LEU GLU GLU          
SEQRES   4 A  339  GLU LEU HIS LYS ARG VAL VAL GLY GLN ASP GLU ALA ILE          
SEQRES   5 A  339  ARG ALA VAL ALA ASP ALA ILE ARG ARG ALA ARG ALA GLY          
SEQRES   6 A  339  LEU LYS ASP PRO ASN ARG PRO ILE GLY SER PHE LEU PHE          
SEQRES   7 A  339  LEU GLY PRO THR GLY VAL GLY LYS THR GLU LEU ALA LYS          
SEQRES   8 A  339  THR LEU ALA ALA THR LEU PHE ASP THR GLU GLU ALA MET          
SEQRES   9 A  339  ILE GLN ILE ASP MET THR GLU TYR MET GLU LYS HIS ALA          
SEQRES  10 A  339  VAL SER ARG LEU ILE GLY ALA PRO PRO GLY TYR VAL GLY          
SEQRES  11 A  339  TYR GLU GLU GLY GLY GLN LEU THR GLU ALA VAL ARG ARG          
SEQRES  12 A  339  ARG PRO TYR SER VAL ILE LEU PHE ASP GLU ILE GLU LYS          
SEQRES  13 A  339  ALA HIS PRO ASP VAL PHE ASN ILE LEU LEU GLN ILE LEU          
SEQRES  14 A  339  ASP ASP GLY ARG LEU THR ASP SER HIS GLY ARG THR VAL          
SEQRES  15 A  339  ASP PHE ARG ASN THR VAL ILE ILE LEU THR SER ASN LEU          
SEQRES  16 A  339  GLY SER PRO LEU ILE LEU GLU GLY LEU GLN LYS GLY TRP          
SEQRES  17 A  339  PRO TYR GLU ARG ILE ARG ASP GLU VAL PHE LYS VAL LEU          
SEQRES  18 A  339  GLN GLN HIS PHE ARG PRO GLU PHE LEU ASN ARG LEU ASP          
SEQRES  19 A  339  GLU ILE VAL VAL PHE ARG PRO LEU THR LYS GLU GLN ILE          
SEQRES  20 A  339  ARG GLN ILE VAL GLU ILE GLN LEU SER TYR LEU ARG ALA          
SEQRES  21 A  339  ARG LEU ALA GLU LYS ARG ILE SER LEU GLU LEU THR GLU          
SEQRES  22 A  339  ALA ALA LYS ASP PHE LEU ALA GLU ARG GLY TYR ASP PRO          
SEQRES  23 A  339  VAL PHE GLY ALA ARG PRO LEU ARG ARG VAL ILE GLN ARG          
SEQRES  24 A  339  GLU LEU GLU THR PRO LEU ALA GLN LYS ILE LEU ALA GLY          
SEQRES  25 A  339  GLU VAL LYS GLU GLY ASP ARG VAL GLN VAL ASP VAL GLY          
SEQRES  26 A  339  PRO ALA GLY LEU VAL PHE ALA VAL PRO ALA ARG VAL GLU          
SEQRES  27 A  339  ALA                                                          
HET    ACP  A 901      31                                                       
HET     MG  A 902       1                                                       
HET    GAI  A 903       4                                                       
HETNAM     ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GAI GUANIDINE                                                        
HETSYN     ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE                 
FORMUL   2  ACP    C11 H18 N5 O12 P3                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GAI    C H5 N3                                                      
FORMUL   5  HOH   *77(H2 O)                                                     
HELIX    1   1 THR A  522  GLY A  535  1                                  14    
HELIX    2   2 PRO A  537  LEU A  542  1                                   6    
HELIX    3   3 ARG A  551  LYS A  558  1                                   8    
HELIX    4   4 GLN A  563  ALA A  579  1                                  17    
HELIX    5   5 GLY A  600  ASP A  614  1                                  15    
HELIX    6   6 THR A  615  GLU A  617  5                                   3    
HELIX    7   7 THR A  625  TYR A  627  5                                   3    
HELIX    8   8 GLU A  629  HIS A  631  5                                   3    
HELIX    9   9 ALA A  632  GLY A  638  1                                   7    
HELIX   10  10 GLY A  650  ARG A  659  1                                  10    
HELIX   11  11 GLU A  668  ALA A  672  5                                   5    
HELIX   12  12 HIS A  673  GLY A  687  1                                  15    
HELIX   13  13 GLY A  711  GLY A  722  1                                  12    
HELIX   14  14 PRO A  724  PHE A  740  1                                  17    
HELIX   15  15 ARG A  741  ASN A  746  1                                   6    
HELIX   16  16 THR A  758  LEU A  770  1                                  13    
HELIX   17  17 LEU A  770  GLU A  779  1                                  10    
HELIX   18  18 THR A  787  GLY A  798  1                                  12    
HELIX   19  19 PRO A  807  LEU A  816  1                                  10    
HELIX   20  20 LEU A  816  ALA A  826  1                                  11    
SHEET    1   A 5 MET A 619  ASP A 623  0                                        
SHEET    2   A 5 VAL A 663  ASP A 667  1  O  LEU A 665   N  ILE A 620           
SHEET    3   A 5 VAL A 703  THR A 707  1  O  VAL A 703   N  ILE A 664           
SHEET    4   A 5 GLY A 589  LEU A 594  1  N  PHE A 593   O  LEU A 706           
SHEET    5   A 5 GLU A 750  VAL A 753  1  O  VAL A 752   N  LEU A 594           
SHEET    1   B 2 ARG A 688  THR A 690  0                                        
SHEET    2   B 2 THR A 696  ASP A 698 -1  O  VAL A 697   N  LEU A 689           
SHEET    1   C 3 SER A 783  LEU A 786  0                                        
SHEET    2   C 3 ARG A 834  GLY A 840  1  O  VAL A 835   N  GLU A 785           
SHEET    3   C 3 GLY A 843  ALA A 847 -1  O  GLY A 843   N  GLY A 840           
LINK         OG1 THR A 602                MG    MG A 902     1555   1555  1.92  
LINK         O1G ACP A 901                MG    MG A 902     1555   1555  1.97  
LINK         O1B ACP A 901                MG    MG A 902     1555   1555  2.04  
LINK        MG    MG A 902                 O   HOH A1001     1555   1555  2.17  
LINK        MG    MG A 902                 O   HOH A1002     1555   1555  2.10  
LINK        MG    MG A 902                 O   HOH A1003     1555   1555  2.19  
SITE     1 AC1 20 ARG A 559  VAL A 560  VAL A 561  THR A 597                    
SITE     2 AC1 20 GLY A 598  VAL A 599  GLY A 600  LYS A 601                    
SITE     3 AC1 20 THR A 602  GLU A 603  ILE A 765  GLN A 769                    
SITE     4 AC1 20  MG A 902  GAI A 903  HOH A1001  HOH A1002                    
SITE     5 AC1 20 HOH A1003  HOH A1004  HOH A1006  HOH A1063                    
SITE     1 AC2  5 THR A 602  ACP A 901  HOH A1001  HOH A1002                    
SITE     2 AC2  5 HOH A1003                                                     
SITE     1 AC3  5 GLN A 621  ASP A 623  GLU A 668  GLU A 743                    
SITE     2 AC3  5 ACP A 901                                                     
CRYST1   74.800   74.800  119.500  90.00  90.00 120.00 P 65          6          
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      0.013369  0.007719  0.000000        0.00000                         
SCALE2      0.000000  0.015437  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008368        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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