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Database: PDB
Entry: 5OGU
LinkDB: 5OGU
Original site: 5OGU 
HEADER    DNA BINDING PROTEIN                     13-JUL-17   5OGU              
TITLE     STRUCTURE OF DNA-BINDING HU PROTEIN FROM MICOPLASMA SPIROPLASMA       
TITLE    2 MELLIFERUM                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA-BINDING PROTEIN;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPIROPLASMA MELLIFERUM KC3;                     
SOURCE   3 ORGANISM_TAXID: 570509;                                              
SOURCE   4 GENE: SPM_000560;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DNA BINDING PROTEIN                                                   
EXPDTA    SOLUTION NMR                                                          
NUMMDL    15                                                                    
AUTHOR    D.A.ALTUKHOV,A.A.TALYZINA,Y.K.AGAPOVA,A.V.VLASKINA,D.A.KORZHENEVSKIY, 
AUTHOR   2 E.V.BOCHAROV,T.V.RAKITINA,V.I.TIMOFEEV                               
REVDAT   4   14-JUN-23 5OGU    1       REMARK                                   
REVDAT   3   09-NOV-22 5OGU    1       JRNL                                     
REVDAT   2   08-MAY-19 5OGU    1       REMARK                                   
REVDAT   1   23-AUG-17 5OGU    0                                                
JRNL        AUTH   V.I.TIMOFEEV,D.A.ALTUKHOV,A.A.TALYZINA,Y.K.AGAPOVA,          
JRNL        AUTH 2 A.V.VLASKINA,D.A.KORZHENEVSKIY,S.Y.KLEYMENOV,E.V.BOCHAROV,   
JRNL        AUTH 3 T.V.RAKITINA                                                 
JRNL        TITL   STRUCTURAL PLASTICITY AND THERMAL STABILITY OF THE           
JRNL        TITL 2 HISTONE-LIKE PROTEIN FROM SPIROPLASMA MELLIFERUM ARE DUE TO  
JRNL        TITL 3 PHENYLALANINE INSERTIONS INTO THE CONSERVATIVE SCAFFOLD.     
JRNL        REF    J.BIOMOL.STRUCT.DYN.          V.  36  4392 2018              
JRNL        REFN                   ESSN 1538-0254                               
JRNL        PMID   29283021                                                     
JRNL        DOI    10.1080/07391102.2017.1417162                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : GROMACS                                              
REMARK   3   AUTHORS     : HERMAN BERENDSEN'S GROUP, DEPARTMENT OF              
REMARK   3                 BIOPHYSICAL CHEMISTRY OF GRONINGEN UNIVERSITY        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5OGU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200005707.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 6.7                                
REMARK 210  IONIC STRENGTH                 : 0.375                              
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : 5 % [U-2H] D2O, 95% H2O/5% D2O     
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 2D 1H-15N HSQC; 2D 1H-13C HSQC     
REMARK 210  SPECTROMETER FIELD STRENGTH    : 700 MHZ                            
REMARK 210  SPECTROMETER MODEL             : UNIFORM NMR SYSTEM                 
REMARK 210  SPECTROMETER MANUFACTURER      : AGILENT                            
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : TALOS+                             
REMARK 210   METHOD USED                   : MOLECULAR DYNAMICS                 
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 5000                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 15                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
REMARK 210                                   RESTRAINT VIOLATIONS               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4600 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   OE2  GLU A    43     HZ3  LYS A    51              1.52            
REMARK 500   OD1  ASP A    90     HZ3  LYS B    35              1.59            
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  1 PHE A  14   CB  -  CG  -  CD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500  1 VAL A  17   CA  -  CB  -  CG1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500  1 GLU A  43   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500  1 ILE A  46   CA  -  CB  -  CG1 ANGL. DEV. =  11.8 DEGREES          
REMARK 500  1 GLY A  48   C   -  N   -  CA  ANGL. DEV. =  16.2 DEGREES          
REMARK 500  1 ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  1 ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500  1 ASP A  90   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500  1 ASP A  90   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500  1 PHE B  29   CB  -  CG  -  CD2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  1 PHE B  49   CB  -  CG  -  CD1 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500  1 ARG B  57   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500  1 ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500  2 PHE A  29   CG  -  CD2 -  CE2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500  2 ASP A  32   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500  2 ARG A  60   NE  -  CZ  -  NH1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500  2 ARG A  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500  2 ARG A  63   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500  2 GLU B   5   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500  2 PHE B  14   CZ  -  CE2 -  CD2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500  2 ILE B  46   CA  -  CB  -  CG1 ANGL. DEV. =  12.0 DEGREES          
REMARK 500  2 ARG B  57   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  2 ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500  2 ASP B  61   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500  2 ARG B  63   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500  2 ARG B  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500  2 PHE B  81   CB  -  CG  -  CD1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  3 LYS A  82   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500  3 PHE B  31   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  3 PHE B  49   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  3 PHE B  49   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500  3 ARG B  60   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500  3 ARG B  60   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500  3 PHE B  81   CB  -  CG  -  CD1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500  4 VAL A  17   CA  -  CB  -  CG1 ANGL. DEV. =  10.8 DEGREES          
REMARK 500  4 PHE A  29   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500  4 ALA A  40   CB  -  CA  -  C   ANGL. DEV. =  -9.1 DEGREES          
REMARK 500  4 ARG A  63   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500  4 ARG A  63   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500  4 SER B  19   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES          
REMARK 500  4 PHE B  31   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500  4 GLU B  56   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500  4 ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500  4 ALA B  58   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500  4 ARG B  60   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  5 VAL A  39   CA  -  CB  -  CG1 ANGL. DEV. =   9.4 DEGREES          
REMARK 500  5 ARG A  57   NE  -  CZ  -  NH1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500  5 ARG A  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500  5 ARG A  63   NH1 -  CZ  -  NH2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500  5 ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     201 ANGLE DEVIATIONS.                             
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  1 PHE A  14       61.70   -113.68                                   
REMARK 500  1 LYS A  88     -107.20   -120.86                                   
REMARK 500  1 THR B  67      -33.93   -138.12                                   
REMARK 500  1 LYS B  72       37.83   -145.53                                   
REMARK 500  1 LYS B  88      -91.33   -136.86                                   
REMARK 500  2 ASP A  16        1.90    -68.08                                   
REMARK 500  2 VAL A  17      -35.71   -146.44                                   
REMARK 500  2 LYS A  20      -70.93    -29.60                                   
REMARK 500  2 ALA A  47      102.95    -34.21                                   
REMARK 500  2 THR A  67      -53.96   -137.64                                   
REMARK 500  2 LYS A  72       34.97   -154.25                                   
REMARK 500  2 LYS A  88     -109.72   -133.81                                   
REMARK 500  2 ASN A  92       89.07    -69.46                                   
REMARK 500  2 LYS B  72       47.52   -143.19                                   
REMARK 500  2 LYS B  82      101.15   -161.42                                   
REMARK 500  2 ALA B  83      156.20    -42.66                                   
REMARK 500  2 LYS B  88      -65.22   -146.02                                   
REMARK 500  3 VAL A  17      -42.19   -139.68                                   
REMARK 500  3 PHE A  29       -9.79    -48.41                                   
REMARK 500  3 VAL A  30      -70.01    -76.65                                   
REMARK 500  3 LYS A  72       58.08   -140.85                                   
REMARK 500  3 LYS A  88     -107.72   -135.63                                   
REMARK 500  3 PHE B  14       57.65   -140.30                                   
REMARK 500  3 VAL B  17      -69.69   -128.54                                   
REMARK 500  3 LYS B  20      -49.39    -29.76                                   
REMARK 500  3 LYS B  72       56.07   -144.86                                   
REMARK 500  3 SER B  78     -146.86   -136.88                                   
REMARK 500  3 LYS B  88      -84.60   -156.48                                   
REMARK 500  4 ALA A  47      100.36    -59.89                                   
REMARK 500  4 THR A  67      -70.01   -131.32                                   
REMARK 500  4 LYS A  88     -110.72   -125.26                                   
REMARK 500  4 VAL B  17      -62.67   -128.39                                   
REMARK 500  4 ALA B  47      108.46    -50.00                                   
REMARK 500  4 LYS B  72       51.35   -156.71                                   
REMARK 500  4 LYS B  88      -71.41   -141.56                                   
REMARK 500  5 VAL A  17      -61.68   -105.40                                   
REMARK 500  5 ALA A  47      100.13    -56.04                                   
REMARK 500  5 THR A  67      -40.24   -137.65                                   
REMARK 500  5 LYS A  72       83.68   -158.29                                   
REMARK 500  5 LYS A  88      -78.53   -141.70                                   
REMARK 500  5 THR B  15      -39.55    -39.37                                   
REMARK 500  5 VAL B  17       -8.03   -142.54                                   
REMARK 500  5 THR B  67      -52.85   -120.09                                   
REMARK 500  5 LYS B  72       64.42   -156.30                                   
REMARK 500  5 ALA B  75       98.68    -59.22                                   
REMARK 500  5 LYS B  88      -80.60   -140.60                                   
REMARK 500  6 PHE A  14       33.70   -141.59                                   
REMARK 500  6 ALA A  47       99.06    -44.87                                   
REMARK 500  6 LYS A  72       51.84   -151.94                                   
REMARK 500  6 LYS A  85      -48.66    -24.81                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     128 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS A    0     MET A    1          6       149.25                    
REMARK 500 ALA B   75     SER B   76          7      -140.50                    
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  1 ARG B  63         0.08    SIDE CHAIN                              
REMARK 500  1 PHE B  81         0.08    SIDE CHAIN                              
REMARK 500  2 PHE A  14         0.13    SIDE CHAIN                              
REMARK 500  7 HIS A  33         0.07    SIDE CHAIN                              
REMARK 500  7 HIS B  22         0.11    SIDE CHAIN                              
REMARK 500  7 GLU B  69         0.07    SIDE CHAIN                              
REMARK 500  8 ARG B  60         0.07    SIDE CHAIN                              
REMARK 500 10 ARG A  57         0.09    SIDE CHAIN                              
REMARK 500 11 PHE A  49         0.07    SIDE CHAIN                              
REMARK 500 11 ARG A  63         0.07    SIDE CHAIN                              
REMARK 500 14 PHE A  14         0.08    SIDE CHAIN                              
REMARK 500 14 PHE A  81         0.08    SIDE CHAIN                              
REMARK 500 15 GLU A  12         0.07    SIDE CHAIN                              
REMARK 500 15 PHE A  14         0.08    SIDE CHAIN                              
REMARK 500 15 PHE A  81         0.07    SIDE CHAIN                              
REMARK 500 15 PHE B  31         0.09    SIDE CHAIN                              
REMARK 500 15 ARG B  63         0.11    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  5 THR B  67         10.02                                           
REMARK 500  9 ILE B  10        -11.99                                           
REMARK 500 15 LEU B  38        -10.84                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 34163   RELATED DB: BMRB                                 
REMARK 900 STRUCTURE OF DNA-BINDING HU PROTEIN FROM MICOPLASMA SPIROPLASMA      
REMARK 900 MELLIFERUM                                                           
DBREF1 5OGU A    1    93  UNP                  A0A037USE5_SPIME                 
DBREF2 5OGU A     A0A037USE5                          1          93             
DBREF1 5OGU B    1    93  UNP                  A0A037USE5_SPIME                 
DBREF2 5OGU B     A0A037USE5                          1          93             
SEQADV 5OGU GLY A   -1  UNP  A0A037USE           EXPRESSION TAG                 
SEQADV 5OGU HIS A    0  UNP  A0A037USE           EXPRESSION TAG                 
SEQADV 5OGU GLY B   -1  UNP  A0A037USE           EXPRESSION TAG                 
SEQADV 5OGU HIS B    0  UNP  A0A037USE           EXPRESSION TAG                 
SEQRES   1 A   95  GLY HIS MET SER LYS LYS GLU LEU ALA ALA GLN ILE ALA          
SEQRES   2 A   95  GLU LYS PHE THR ASP VAL LEU SER LYS THR HIS ALA GLU          
SEQRES   3 A   95  GLU ILE THR ASN PHE VAL PHE ASP HIS ILE LYS LYS ALA          
SEQRES   4 A   95  LEU VAL ALA GLY LYS GLU VAL SER ILE ALA GLY PHE GLY          
SEQRES   5 A   95  LYS PHE ALA VAL THR GLU ARG ALA ALA ARG ASP GLY ARG          
SEQRES   6 A   95  ASN PRO SER THR GLY GLU THR ILE LYS ILE PRO ALA SER          
SEQRES   7 A   95  LYS SER ALA LYS PHE LYS ALA GLY LYS GLN LEU LYS THR          
SEQRES   8 A   95  ASP LEU ASN ASN                                              
SEQRES   1 B   95  GLY HIS MET SER LYS LYS GLU LEU ALA ALA GLN ILE ALA          
SEQRES   2 B   95  GLU LYS PHE THR ASP VAL LEU SER LYS THR HIS ALA GLU          
SEQRES   3 B   95  GLU ILE THR ASN PHE VAL PHE ASP HIS ILE LYS LYS ALA          
SEQRES   4 B   95  LEU VAL ALA GLY LYS GLU VAL SER ILE ALA GLY PHE GLY          
SEQRES   5 B   95  LYS PHE ALA VAL THR GLU ARG ALA ALA ARG ASP GLY ARG          
SEQRES   6 B   95  ASN PRO SER THR GLY GLU THR ILE LYS ILE PRO ALA SER          
SEQRES   7 B   95  LYS SER ALA LYS PHE LYS ALA GLY LYS GLN LEU LYS THR          
SEQRES   8 B   95  ASP LEU ASN ASN                                              
HELIX    1 AA1 SER A    2  PHE A   14  1                                  13    
HELIX    2 AA2 SER A   19  VAL A   39  1                                  21    
HELIX    3 AA3 LYS A   85  LYS A   88  5                                   4    
HELIX    4 AA4 SER B    2  GLU B   12  1                                  11    
HELIX    5 AA5 THR B   21  GLY B   41  1                                  21    
SHEET    1 AA1 4 HIS A   0  MET A   1  0                                        
SHEET    2 AA1 4 GLU B  43  ILE B  46  1  O  SER B  45   N  MET A   1           
SHEET    3 AA1 4 GLY B  50  GLU B  56 -1  O  GLY B  50   N  ILE B  46           
SHEET    4 AA1 4 LYS B  77  ALA B  83 -1  O  LYS B  82   N  LYS B  51           
SHEET    1 AA2 4 SER A  76  ALA A  83  0                                        
SHEET    2 AA2 4 GLY A  50  ARG A  57 -1  N  ARG A  57   O  SER A  76           
SHEET    3 AA2 4 GLU A  43  ILE A  46 -1  N  VAL A  44   O  PHE A  52           
SHEET    4 AA2 4 HIS B   0  MET B   1  1  O  MET B   1   N  SER A  45           
SHEET    1 AA3 2 ARG A  60  ARG A  63  0                                        
SHEET    2 AA3 2 THR A  70  ILE A  73 -1  O  ILE A  73   N  ARG A  60           
SHEET    1 AA4 2 ARG B  60  ARG B  63  0                                        
SHEET    2 AA4 2 THR B  70  ILE B  73 -1  O  ILE B  71   N  GLY B  62           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011217  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011217        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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