Header list of 1bfm.pdb file
Complete list - b 16 2 Bytes
HEADER HISTONE PROTEIN 28-SEP-95 1BFM
TITLE HISTONE B FROM METHANOTHERMUS FERVIDUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HMFB, RHMFB, ARCHAEAL HISTONE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMUS FERVIDUS;
SOURCE 3 ORGANISM_TAXID: 2180;
SOURCE 4 CELL_LINE: JM105;
SOURCE 5 GENE: HMFB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK223-3;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HMFB
KEYWDS ARCHAEAL HISTONE PROTEIN, DNA BINDING PROTEIN HMF-2, HISTONE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 33
AUTHOR M.R.STARICH,K.SANDMAN,J.N.REEVE,M.F.SUMMERS
REVDAT 3 16-FEB-22 1BFM 1 REMARK
REVDAT 2 24-FEB-09 1BFM 1 VERSN
REVDAT 1 29-JAN-96 1BFM 0
JRNL AUTH M.R.STARICH,K.SANDMAN,J.N.REEVE,M.F.SUMMERS
JRNL TITL NMR STRUCTURE OF HMFB FROM THE HYPERTHERMOPHILE,
JRNL TITL 2 METHANOTHERMUS FERVIDUS, CONFIRMS THAT THIS ARCHAEAL PROTEIN
JRNL TITL 3 IS A HISTONE.
JRNL REF J.MOL.BIOL. V. 255 187 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8568866
JRNL DOI 10.1006/JMBI.1996.0016
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BFM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171697.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 33
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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: 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 14 PHE A 67 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 19 PHE B 67 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 23 PHE B 67 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 32 PHE A 67 CB - CG - CD1 ANGL. DEV. = -4.4 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 1 GLU A 2 -162.69 -163.04
REMARK 500 1 LEU A 3 102.29 -57.22
REMARK 500 1 ILE A 31 -73.23 -61.42
REMARK 500 1 ARG A 52 114.93 172.47
REMARK 500 1 LYS A 53 28.81 178.66
REMARK 500 1 THR A 54 150.14 63.45
REMARK 500 1 ARG A 66 -76.60 -64.68
REMARK 500 1 GLU B 2 47.42 -97.67
REMARK 500 1 LEU B 3 86.28 58.56
REMARK 500 1 ARG B 19 100.01 66.53
REMARK 500 1 ILE B 31 -72.56 -61.14
REMARK 500 1 ALA B 40 -70.53 -61.88
REMARK 500 1 PHE B 67 -73.20 -60.85
REMARK 500 1 LYS B 68 -62.72 178.43
REMARK 500 2 LEU A 3 81.16 60.30
REMARK 500 2 GLU A 18 -75.32 -122.55
REMARK 500 2 ARG A 52 -162.71 55.21
REMARK 500 2 LYS A 53 -81.28 70.23
REMARK 500 2 LYS A 68 -170.57 60.97
REMARK 500 2 ILE B 31 -73.46 -61.15
REMARK 500 2 ALA B 40 -70.90 -61.92
REMARK 500 2 ARG B 52 -163.80 178.71
REMARK 500 2 LYS B 53 -93.58 76.02
REMARK 500 3 GLU A 2 112.33 58.67
REMARK 500 3 ARG A 19 107.71 -160.96
REMARK 500 3 ARG A 52 80.05 54.21
REMARK 500 3 LYS A 68 -169.63 178.69
REMARK 500 3 GLU B 18 -25.67 -171.05
REMARK 500 3 THR B 54 -176.59 60.34
REMARK 500 3 LYS B 68 -169.15 61.59
REMARK 500 4 GLU A 2 103.17 58.48
REMARK 500 4 ALA A 17 -163.85 -66.51
REMARK 500 4 ALA A 40 -74.56 -61.72
REMARK 500 4 VAL A 64 -72.01 -66.09
REMARK 500 4 LYS A 68 82.93 64.64
REMARK 500 4 GLU B 2 -159.20 -134.24
REMARK 500 4 GLU B 18 -74.65 -82.27
REMARK 500 4 ILE B 31 -72.78 -61.04
REMARK 500 4 LYS B 68 -76.58 62.17
REMARK 500 5 GLU A 2 -161.48 58.44
REMARK 500 5 ILE A 31 -72.95 -61.42
REMARK 500 5 ARG A 52 -167.03 58.64
REMARK 500 5 LYS A 53 98.13 64.82
REMARK 500 5 THR A 54 117.47 71.65
REMARK 500 5 VAL A 64 -73.64 -61.22
REMARK 500 5 GLU B 2 -166.44 58.57
REMARK 500 5 GLU B 18 -72.37 -161.25
REMARK 500 5 ILE B 31 -70.05 -60.87
REMARK 500 5 ALA B 40 -75.11 -64.20
REMARK 500 5 THR B 54 127.36 70.10
REMARK 500
REMARK 500 THIS ENTRY HAS 413 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 19 PHE B 67 0.09 SIDE CHAIN
REMARK 500 23 PHE B 67 0.08 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 1 ALA A 29 -10.51
REMARK 500 1 ARG A 48 -12.30
REMARK 500 1 ALA A 50 11.20
REMARK 500 1 ALA B 15 10.92
REMARK 500 1 ALA B 29 -10.46
REMARK 500 1 GLU B 61 -11.70
REMARK 500 1 LEU B 62 -10.26
REMARK 500 2 LEU A 32 -10.29
REMARK 500 2 ALA A 50 10.74
REMARK 500 2 LEU A 62 -10.84
REMARK 500 2 ASP B 14 -10.70
REMARK 500 2 ALA B 15 10.43
REMARK 500 2 THR B 27 -10.04
REMARK 500 2 LEU B 28 -12.18
REMARK 500 2 ALA B 29 -11.51
REMARK 500 2 ARG B 48 -11.20
REMARK 500 2 GLU B 61 -12.59
REMARK 500 3 LYS A 13 -11.58
REMARK 500 3 ALA A 29 -12.50
REMARK 500 3 MET A 35 -10.50
REMARK 500 3 ARG A 37 -11.83
REMARK 500 3 ALA A 50 10.56
REMARK 500 3 PHE A 67 10.03
REMARK 500 3 GLU B 2 12.25
REMARK 500 3 ASP B 14 -11.21
REMARK 500 3 ALA B 15 10.58
REMARK 500 3 LEU B 28 -13.49
REMARK 500 3 LEU B 32 -14.02
REMARK 500 3 GLU B 33 11.06
REMARK 500 4 ASP A 14 -10.18
REMARK 500 4 ALA A 15 10.23
REMARK 500 4 LEU A 28 -10.88
REMARK 500 4 ALA A 29 -11.90
REMARK 500 4 LEU A 32 -10.98
REMARK 500 4 GLU A 34 -10.54
REMARK 500 4 THR B 27 -10.13
REMARK 500 4 ALA B 29 -11.61
REMARK 500 5 ASP A 14 -10.66
REMARK 500 5 LYS A 45 -10.06
REMARK 500 5 ALA A 50 10.58
REMARK 500 5 GLU A 58 -10.31
REMARK 500 5 ASP A 59 10.08
REMARK 500 5 ALA A 63 -12.94
REMARK 500 5 ILE B 8 -10.65
REMARK 500 5 ASP B 14 -11.16
REMARK 500 5 ALA B 15 10.37
REMARK 500 5 THR B 27 -10.11
REMARK 500 5 LEU B 32 -10.53
REMARK 500 5 LEU B 62 -10.73
REMARK 500 6 MET A 35 -10.81
REMARK 500
REMARK 500 THIS ENTRY HAS 240 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BFM A 1 69 UNP P19267 HMFB_METFE 1 69
DBREF 1BFM B 1 69 UNP P19267 HMFB_METFE 1 69
SEQRES 1 A 69 MET GLU LEU PRO ILE ALA PRO ILE GLY ARG ILE ILE LYS
SEQRES 2 A 69 ASP ALA GLY ALA GLU ARG VAL SER ASP ASP ALA ARG ILE
SEQRES 3 A 69 THR LEU ALA LYS ILE LEU GLU GLU MET GLY ARG ASP ILE
SEQRES 4 A 69 ALA SER GLU ALA ILE LYS LEU ALA ARG HIS ALA GLY ARG
SEQRES 5 A 69 LYS THR ILE LYS ALA GLU ASP ILE GLU LEU ALA VAL ARG
SEQRES 6 A 69 ARG PHE LYS LYS
SEQRES 1 B 69 MET GLU LEU PRO ILE ALA PRO ILE GLY ARG ILE ILE LYS
SEQRES 2 B 69 ASP ALA GLY ALA GLU ARG VAL SER ASP ASP ALA ARG ILE
SEQRES 3 B 69 THR LEU ALA LYS ILE LEU GLU GLU MET GLY ARG ASP ILE
SEQRES 4 B 69 ALA SER GLU ALA ILE LYS LEU ALA ARG HIS ALA GLY ARG
SEQRES 5 B 69 LYS THR ILE LYS ALA GLU ASP ILE GLU LEU ALA VAL ARG
SEQRES 6 B 69 ARG PHE LYS LYS
HELIX 1 1 ILE A 5 ALA A 15 1 11
HELIX 2 2 ASP A 22 ALA A 50 1 29
HELIX 3 3 ALA A 57 PHE A 67 1 11
HELIX 4 4 ILE B 5 ALA B 15 1 11
HELIX 5 5 ASP B 22 ALA B 50 1 29
HELIX 6 6 ALA B 57 PHE B 67 1 11
SHEET 1 A 2 ARG A 19 VAL A 20 0
SHEET 2 A 2 THR B 54 ILE B 55 1 N ILE B 55 O ARG A 19
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes