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Database: PDB
Entry: 4D8J
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Original site: 4D8J 
HEADER    DNA BINDING PROTEIN                     10-JAN-12   4D8J              
TITLE     STRUCTURE OF E. COLI MATP-MATS COMPLEX                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MACRODOMAIN TER PROTEIN;                                   
COMPND   3 CHAIN: B, A, D, C, H, G, L, K;                                       
COMPND   4 SYNONYM: MATP;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 5'-D(*TP*TP*CP*GP*TP*GP*AP*CP*AP*TP*TP*GP*TP*CP*AP*CP*GP*AP
COMPND   8 *A)-3';                                                              
COMPND   9 CHAIN: N, F, J, P;                                                   
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: MATS STRAND 1;                                        
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: 5'-D(*TP*TP*CP*GP*TP*GP*AP*CP*AP*AP*TP*GP*TP*CP*AP*CP*GP*AP
COMPND  14 *A)-3';                                                              
COMPND  15 CHAIN: M, E, I, O;                                                   
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: MATS STRAND 2                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: MATP, YCBG, B0956, JW0939;                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 SYNTHETIC: YES;                                                      
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    MACRODOMAINS, CHROMOSOME ORGANIZATION, CHROMOSOME CONDENSATION, DNA   
KEYWDS   2 BINDING PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.DUPAIGNE,N.K.TONTHAT,O.ESPELI,T.WHITFILL,F.BOCCARD,M.A.SCHUMACHER   
REVDAT   2   30-JAN-13 4D8J    1       JRNL                                     
REVDAT   1   21-NOV-12 4D8J    0                                                
JRNL        AUTH   P.DUPAIGNE,N.K.TONTHAT,O.ESPELI,T.WHITFILL,F.BOCCARD,        
JRNL        AUTH 2 M.A.SCHUMACHER                                               
JRNL        TITL   MOLECULAR BASIS FOR A PROTEIN-MEDIATED DNA-BRIDGING          
JRNL        TITL 2 MECHANISM THAT FUNCTIONS IN CONDENSATION OF THE E. COLI      
JRNL        TITL 3 CHROMOSOME.                                                  
JRNL        REF    MOL.CELL                      V.  48   560 2012              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   23084832                                                     
JRNL        DOI    10.1016/J.MOLCEL.2012.09.009                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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) : 3.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 97.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 21487528.810                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 36461                          
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) : 0.299                           
REMARK   3   FREE R VALUE                     : 0.313                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 13.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5473                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 3.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.77                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6050                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5220                       
REMARK   3   BIN FREE R VALUE                    : 0.5080                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 13.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 937                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9812                                    
REMARK   3   NUCLEIC ACID ATOMS       : 3092                                    
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 145.40                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -35.70000                                            
REMARK   3    B22 (A**2) : -45.34000                                            
REMARK   3    B33 (A**2) : 81.04000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.82                            
REMARK   3   ESD FROM SIGMAA              (A) : 1.85                            
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) : 0.80                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.72                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.09                            
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) : 3.270 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.620 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.490 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.180 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.20                                                 
REMARK   3   BSOL        : 8.31                                                 
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 4D8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070016.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.02                               
REMARK 200  MONOCHROMATOR                  : KHOZU DOUBLE FLAT CRYSTAL SI(111)  
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36461                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 180.100                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.20000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3VEA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG 1000, 0.1 M ACETATE, PH 5.0,      
REMARK 280  40% ETHYLENE GLYCOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       57.43500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       92.47500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       90.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.47500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.43500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       90.05000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, N, M, A                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, P, O, K                            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       90.05000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       92.47500            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E, C                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, J, I, G                            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       57.43500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000       92.47500            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, J, I, G                            
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 APPLY THE FOLLOWING TO CHAINS: D, F, E, C                            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       57.43500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -92.47500            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, P, O, K                            
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 APPLY THE FOLLOWING TO CHAINS: B, N, M, A                            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -90.05000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       92.47500            
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     LYS B   149                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     GLU A   150                                                      
REMARK 465     GLU D   150                                                      
REMARK 465     LYS C   149                                                      
REMARK 465     GLU C   150                                                      
REMARK 465     LYS H   149                                                      
REMARK 465     GLU H   150                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLU G   150                                                      
REMARK 465     GLU L   150                                                      
REMARK 465     LYS K   149                                                      
REMARK 465     GLU K   150                                                      
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     ILE B  99    CG1  CG2  CD1                                       
REMARK 470     ILE A  99    CG1  CG2  CD1                                       
REMARK 470     ILE D  99    CG1  CG2  CD1                                       
REMARK 470     LYS D 135    CG   CD   CE   NZ                                   
REMARK 470     LYS C  16    CG   CD   CE   NZ                                   
REMARK 470     ILE C  99    CG1  CG2  CD1                                       
REMARK 470     ILE H  99    CG1  CG2  CD1                                       
REMARK 470     THR G 118    OG1  CG2                                            
REMARK 470     ILE G 119    CG1  CG2  CD1                                       
REMARK 470     VAL L  43    CG1  CG2                                            
REMARK 470     VAL K  43    CG1  CG2                                            
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   N6    DA F     9     O4    DT E    11              1.81            
REMARK 500   O6    DG N    12     N4    DC M     8              1.89            
REMARK 500   NZ   LYS B    71     OP2   DC N     3              1.95            
REMARK 500   O6    DG F     4     N4    DC E    16              1.95            
REMARK 500   NZ   LYS H    92     OP1   DA I     9              2.00            
REMARK 500   O    LEU A     9     N    GLY A    12              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500     DG N  12   C5     DG N  12   C6     -0.091                       
REMARK 500     DA F   9   C5     DA F   9   C6     -0.105                       
REMARK 500     DC E   8   O3'    DA E   9   P      -0.076                       
REMARK 500     DT E  11   C4     DT E  11   O4     -0.058                       
REMARK 500     DA J  15   O3'    DC J  16   P      -0.123                       
REMARK 500    ASP G 125   C     ALA G 126   N       0.187                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500     DA F   9   N1  -  C6  -  N6  ANGL. DEV. =   4.0 DEGREES          
REMARK 500     DA E   9   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES          
REMARK 500     DT E  11   C1' -  O4' -  C4' ANGL. DEV. =  -6.5 DEGREES          
REMARK 500     DT E  11   C3' -  C2' -  C1' ANGL. DEV. =  -7.2 DEGREES          
REMARK 500     DT E  11   C5  -  C4  -  O4  ANGL. DEV. =  -4.4 DEGREES          
REMARK 500     DC E  16   N1  -  C1' -  C2' ANGL. DEV. =   9.0 DEGREES          
REMARK 500     DT I  11   C2' -  C3' -  O3' ANGL. DEV. = -17.3 DEGREES          
REMARK 500    ASP G 125   CA  -  C   -  N   ANGL. DEV. = -33.5 DEGREES          
REMARK 500    ASP G 125   O   -  C   -  N   ANGL. DEV. = -35.2 DEGREES          
REMARK 500    ALA G 126   C   -  N   -  CA  ANGL. DEV. = -18.8 DEGREES          
REMARK 500     DG P  12   C5' -  C4' -  O4' ANGL. DEV. =   6.6 DEGREES          
REMARK 500     DT O   5   O4' -  C1' -  N1  ANGL. DEV. =   1.9 DEGREES          
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    GLN B   4      105.36    -47.55                                   
REMARK 500    GLU B   7      -34.13    -37.70                                   
REMARK 500    ASN B   8      -70.29    -41.55                                   
REMARK 500    LYS B  20      -71.08    -54.91                                   
REMARK 500    ALA B  34      -83.90    -68.58                                   
REMARK 500    ALA B  36      -22.76    -38.44                                   
REMARK 500    VAL B  41      -82.77    -43.83                                   
REMARK 500    LEU B  47       27.75    -70.39                                   
REMARK 500    GLU B  48      -34.90    -31.30                                   
REMARK 500    PRO B  51      -99.38    -65.60                                   
REMARK 500    VAL B  52      -15.52    -49.87                                   
REMARK 500    ASN B  55      -72.40    -55.77                                   
REMARK 500    MET B  62      149.02   -179.10                                   
REMARK 500    GLU B  85      -92.49    -44.88                                   
REMARK 500    LYS A   2      -57.39   -147.62                                   
REMARK 500    TYR A   3     -169.47    -66.65                                   
REMARK 500    TYR A  17      -72.09    -52.08                                   
REMARK 500    LEU A  47       27.21    -79.76                                   
REMARK 500    GLU A  48      -17.40    -48.10                                   
REMARK 500    ASN A  49       38.01   -145.24                                   
REMARK 500    PRO A  51      -93.98    -78.22                                   
REMARK 500    VAL A  52      -36.60    -39.90                                   
REMARK 500    ASP A  59      -75.46    -61.70                                   
REMARK 500    HIS A  61      -61.11    -91.24                                   
REMARK 500    MET A  62      158.75    -48.24                                   
REMARK 500    PRO A  64       17.26    -66.69                                   
REMARK 500    GLU A  85      -90.30    -57.33                                   
REMARK 500    HIS A  88       -6.19    -58.56                                   
REMARK 500    GLN A 102      -83.68    -38.57                                   
REMARK 500    LYS D   2      -30.38   -130.59                                   
REMARK 500    GLU D   7      -14.60    -49.05                                   
REMARK 500    ASN D   8      -68.47    -92.69                                   
REMARK 500    SER D  11       10.47    -64.00                                   
REMARK 500    ILE D  28      -70.67   -118.67                                   
REMARK 500    ILE D  32       -4.38    -58.54                                   
REMARK 500    GLU D  48      -84.37   -106.13                                   
REMARK 500    ASN D  49       43.14    -93.06                                   
REMARK 500    GLU D  50       76.57   -114.99                                   
REMARK 500    ASP D  59      -38.13    -39.62                                   
REMARK 500    LYS D  60      -98.82    -72.23                                   
REMARK 500    ASN D  68      -75.09    -57.63                                   
REMARK 500    GLU D  85      -75.54    -56.93                                   
REMARK 500    HIS D  86       92.76    -56.54                                   
REMARK 500    LYS D 129      -71.65    -45.72                                   
REMARK 500    ARG C  23       23.61    -68.35                                   
REMARK 500    ILE C  28      -79.12    -93.79                                   
REMARK 500    ALA C  34       32.75    -72.52                                   
REMARK 500    SER C  35      -77.92   -121.54                                   
REMARK 500    ALA C  36        0.31    -68.13                                   
REMARK 500    LEU C  44       20.98    -77.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     141 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  31         0.06    SIDE CHAIN                              
REMARK 500     DC E  16         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP G 125         34.14                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU D 147        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VEA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VEB   RELATED DB: PDB                                   
DBREF  4D8J B    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J A    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J D    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J C    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J H    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J G    1   149  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J L    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J K    1   150  UNP    P0A8N0   MATP_ECOLI       1    150             
DBREF  4D8J N    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J F    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J J    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J P    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J M    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J E    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J I    1    19  PDB    4D8J     4D8J             1     19             
DBREF  4D8J O    1    19  PDB    4D8J     4D8J             1     19             
SEQRES   1 B  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 B  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 B  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 B  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 B  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 B  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 B  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 B  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 B  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 B  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 B  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 B  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 N   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DT  DT  DG  DT          
SEQRES   2 N   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 M   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DA  DT  DG  DT          
SEQRES   2 M   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 A  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 A  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 A  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 A  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 A  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 A  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 A  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 A  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 A  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 A  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 A  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 A  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 D  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 D  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 D  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 D  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 D  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 D  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 D  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 D  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 D  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 D  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 D  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 D  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 F   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DT  DT  DG  DT          
SEQRES   2 F   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 E   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DA  DT  DG  DT          
SEQRES   2 E   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 C  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 C  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 C  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 C  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 C  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 C  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 C  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 C  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 C  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 C  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 C  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 C  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 H  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 H  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 H  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 H  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 H  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 H  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 H  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 H  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 H  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 H  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 H  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 H  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 J   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DT  DT  DG  DT          
SEQRES   2 J   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 I   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DA  DT  DG  DT          
SEQRES   2 I   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 G  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 G  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 G  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 G  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 G  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 G  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 G  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 G  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 G  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 G  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 G  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 G  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 L  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 L  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 L  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 L  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 L  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 L  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 L  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 L  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 L  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 L  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 L  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 L  150  GLN ALA LEU LEU GLY LYS GLU                                  
SEQRES   1 P   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DT  DT  DG  DT          
SEQRES   2 P   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 O   19   DT  DT  DC  DG  DT  DG  DA  DC  DA  DA  DT  DG  DT          
SEQRES   2 O   19   DC  DA  DC  DG  DA  DA                                      
SEQRES   1 K  150  MET LYS TYR GLN GLN LEU GLU ASN LEU GLU SER GLY TRP          
SEQRES   2 K  150  LYS TRP LYS TYR LEU VAL LYS LYS HIS ARG GLU GLY GLU          
SEQRES   3 K  150  LEU ILE THR ARG TYR ILE GLU ALA SER ALA ALA GLN GLU          
SEQRES   4 K  150  ALA VAL ASP VAL LEU LEU SER LEU GLU ASN GLU PRO VAL          
SEQRES   5 K  150  LEU VAL ASN GLY TRP ILE ASP LYS HIS MET ASN PRO GLU          
SEQRES   6 K  150  LEU VAL ASN ARG MET LYS GLN THR ILE ARG ALA ARG ARG          
SEQRES   7 K  150  LYS ARG HIS PHE ASN ALA GLU HIS GLN HIS THR ARG LYS          
SEQRES   8 K  150  LYS SER ILE ASP LEU GLU PHE ILE VAL TRP GLN ARG LEU          
SEQRES   9 K  150  ALA GLY LEU ALA GLN ARG ARG GLY LYS THR LEU SER GLU          
SEQRES  10 K  150  THR ILE VAL GLN LEU ILE GLU ASP ALA GLU ASN LYS GLU          
SEQRES  11 K  150  LYS TYR ALA ASN LYS MET SER SER LEU LYS GLN ASP LEU          
SEQRES  12 K  150  GLN ALA LEU LEU GLY LYS GLU                                  
HELIX    1   1 LEU B    6  GLY B   25  1                                  20    
HELIX    2   2 ALA B   34  ALA B   36  5                                   3    
HELIX    3   3 ALA B   37  SER B   46  1                                  10    
HELIX    4   4 GLU B   50  HIS B   61  1                                  12    
HELIX    5   5 LEU B   66  GLU B   85  1                                  20    
HELIX    6   6 GLU B   97  GLY B  112  1                                  16    
HELIX    7   7 THR B  114  LEU B  147  1                                  34    
HELIX    8   8 LEU A    6  GLU A   26  1                                  21    
HELIX    9   9 SER A   35  SER A   46  1                                  12    
HELIX   10  10 GLU A   50  HIS A   61  1                                  12    
HELIX   11  11 LEU A   66  GLU A   85  1                                  20    
HELIX   12  12 PHE A   98  GLY A  112  1                                  15    
HELIX   13  13 THR A  114  ASN A  128  1                                  15    
HELIX   14  14 ASN A  128  GLY A  148  1                                  21    
HELIX   15  15 LEU D    9  ARG D   23  1                                  15    
HELIX   16  16 SER D   35  SER D   46  1                                  12    
HELIX   17  17 GLU D   50  HIS D   61  1                                  12    
HELIX   18  18 GLU D   65  ASN D   83  1                                  19    
HELIX   19  19 PHE D   98  GLY D  112  1                                  15    
HELIX   20  20 THR D  114  ALA D  145  1                                  32    
HELIX   21  21 LEU C    9  ARG C   23  1                                  15    
HELIX   22  22 GLU C   50  ASP C   59  1                                  10    
HELIX   23  23 GLU C   65  ALA C   84  1                                  20    
HELIX   24  24 PHE C   98  GLY C  112  1                                  15    
HELIX   25  25 THR C  114  LEU C  147  1                                  34    
HELIX   26  26 GLU H    7  VAL H   19  1                                  13    
HELIX   27  27 GLU H   33  GLN H   38  1                                   6    
HELIX   28  28 GLN H   38  LEU H   47  1                                  10    
HELIX   29  29 GLU H   50  ASP H   59  1                                  10    
HELIX   30  30 GLU H   65  GLU H   85  1                                  21    
HELIX   31  31 HIS H   86  ARG H   90  5                                   5    
HELIX   32  32 PHE H   98  GLY H  112  1                                  15    
HELIX   33  33 THR H  114  ALA H  145  1                                  32    
HELIX   34  34 GLU G    7  ARG G   23  1                                  17    
HELIX   35  35 GLN G   38  SER G   46  1                                   9    
HELIX   36  36 GLU G   50  ASN G   55  5                                   6    
HELIX   37  37 GLY G   56  HIS G   61  1                                   6    
HELIX   38  38 ASN G   63  PHE G   82  1                                  20    
HELIX   39  39 GLU G   97  GLN G  109  1                                  13    
HELIX   40  40 THR G  114  LEU G  146  1                                  33    
HELIX   41  41 LEU L    6  GLY L   25  1                                  20    
HELIX   42  42 SER L   35  SER L   46  1                                  12    
HELIX   43  43 VAL L   52  ASP L   59  1                                   8    
HELIX   44  44 GLU L   65  GLU L   85  1                                  21    
HELIX   45  45 PHE L   98  ARG L  111  1                                  14    
HELIX   46  46 THR L  114  ASN L  128  1                                  15    
HELIX   47  47 ASN L  128  ASP L  142  1                                  15    
HELIX   48  48 LEU L  143  GLY L  148  5                                   6    
HELIX   49  49 LEU K    6  GLY K   25  1                                  20    
HELIX   50  50 SER K   35  VAL K   43  1                                   9    
HELIX   51  51 SER K   46  VAL K   52  5                                   7    
HELIX   52  52 LEU K   53  ASP K   59  1                                   7    
HELIX   53  53 ASN K   63  GLU K   65  5                                   3    
HELIX   54  54 LEU K   66  ALA K   84  1                                  19    
HELIX   55  55 GLU K   97  GLY K  112  1                                  16    
HELIX   56  56 THR K  114  GLU K  127  1                                  14    
HELIX   57  57 ASN K  128  MET K  136  1                                   9    
HELIX   58  58 LEU K  139  GLY K  148  1                                  10    
SHEET    1   A 2 LYS B  91  LEU B  96  0                                        
SHEET    2   A 2 LYS A  92  GLU A  97 -1  O  LEU A  96   N  LYS B  92           
SHEET    1   B 2 LYS D  91  GLU D  97  0                                        
SHEET    2   B 2 LYS C  91  GLU C  97 -1  O  LYS C  92   N  LEU D  96           
SHEET    1   C 2 LYS H  92  GLU H  97  0                                        
SHEET    2   C 2 LYS G  91  LEU G  96 -1  O  LEU G  96   N  LYS H  92           
SHEET    1   D 2 LYS L  92  GLU L  97  0                                        
SHEET    2   D 2 LYS K  91  LEU K  96 -1  O  ILE K  94   N  ILE L  94           
CRYST1  114.870  180.100  184.950  90.00  90.00  90.00 P 21 21 21   32          
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      0.008705  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005552  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005407        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system