Header list of 1yua.pdb file
Complete list - v 29 2 Bytes
HEADER DNA BINDING PROTEIN 02-MAR-95 1YUA
TITLE C-TERMINAL DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOPOISOMERASE I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 122 C-TERMINAL RESIDUES;
COMPND 5 EC: 5.99.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: DH5AI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PJW312;
SOURCE 8 EXPRESSION_SYSTEM_GENE: C-TERMINAL FRAGMENT OF ESCHERICHIA COLI
SOURCE 9 TOPOISOMERASE I
KEYWDS GENE-REGULATING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR L.YU,C.-X.ZHU,Y.-C.TSE-DINH,S.W.FESIK
REVDAT 4 29-NOV-17 1YUA 1 REMARK HELIX
REVDAT 3 24-FEB-09 1YUA 1 VERSN
REVDAT 2 01-APR-03 1YUA 1 JRNL
REVDAT 1 08-MAR-96 1YUA 0
JRNL AUTH L.YU,C.X.ZHU,Y.C.TSE-DINH,S.W.FESIK
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL SINGLE-STRANDED
JRNL TITL 2 DNA-BINDING DOMAIN OF ESCHERICHIA COLI TOPOISOMERASE I.
JRNL REF BIOCHEMISTRY V. 34 7622 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7779808
JRNL DOI 10.1021/BI00023A008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YUA 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_1000177443.
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 : 26
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASN A 2 109.09 -43.99
REMARK 500 1 VAL A 5 133.89 79.61
REMARK 500 1 ALA A 6 75.89 45.64
REMARK 500 1 GLU A 10 117.51 166.78
REMARK 500 1 PRO A 12 -92.13 -75.79
REMARK 500 1 VAL A 13 75.45 -113.77
REMARK 500 1 PRO A 16 -24.90 -35.77
REMARK 500 1 GLU A 17 22.46 -78.62
REMARK 500 1 PRO A 19 150.25 -47.51
REMARK 500 1 CYS A 20 -92.49 -95.51
REMARK 500 1 GLU A 21 -70.49 -103.84
REMARK 500 1 LYS A 22 33.33 178.13
REMARK 500 1 PHE A 37 -171.32 -176.82
REMARK 500 1 PHE A 43 144.04 -38.56
REMARK 500 1 GLU A 48 89.60 -58.13
REMARK 500 1 ARG A 50 157.44 162.33
REMARK 500 1 ALA A 51 156.17 -44.40
REMARK 500 1 GLU A 66 -35.81 75.51
REMARK 500 1 GLN A 77 -172.90 164.04
REMARK 500 1 ASN A 82 96.58 -41.05
REMARK 500 1 LYS A 83 151.66 -40.46
REMARK 500 1 THR A 92 11.69 -145.58
REMARK 500 1 ASP A 102 -86.90 67.49
REMARK 500 1 ALA A 105 78.13 44.43
REMARK 500 1 THR A 106 -72.41 -43.74
REMARK 500 1 VAL A 113 -143.76 -89.87
REMARK 500 1 ASP A 114 85.99 -69.07
REMARK 500 2 ASN A 2 76.69 178.49
REMARK 500 2 VAL A 5 98.07 -167.47
REMARK 500 2 ALA A 6 76.29 60.88
REMARK 500 2 PRO A 7 -176.37 -50.40
REMARK 500 2 GLU A 10 -84.77 -155.16
REMARK 500 2 PRO A 12 -92.36 -78.29
REMARK 500 2 PRO A 16 -38.22 -39.47
REMARK 500 2 CYS A 20 -86.27 -101.79
REMARK 500 2 GLU A 21 -82.77 -107.86
REMARK 500 2 LYS A 22 21.41 -156.70
REMARK 500 2 SER A 23 -154.50 -120.25
REMARK 500 2 PHE A 37 -169.59 -174.74
REMARK 500 2 PHE A 43 143.81 -38.19
REMARK 500 2 ARG A 47 41.10 -89.48
REMARK 500 2 ARG A 50 151.14 167.11
REMARK 500 2 LEU A 64 109.15 -55.80
REMARK 500 2 PRO A 65 -72.76 -51.51
REMARK 500 2 GLU A 66 -31.65 176.34
REMARK 500 2 LYS A 67 4.09 -68.69
REMARK 500 2 GLN A 77 -21.23 160.48
REMARK 500 2 ASP A 78 165.86 78.03
REMARK 500 2 LYS A 83 138.39 59.83
REMARK 500 2 ASP A 102 20.84 49.01
REMARK 500
REMARK 500 THIS ENTRY HAS 719 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 1 ARG A 30 0.27 SIDE CHAIN
REMARK 500 1 ARG A 47 0.28 SIDE CHAIN
REMARK 500 1 ARG A 50 0.15 SIDE CHAIN
REMARK 500 1 ARG A 59 0.14 SIDE CHAIN
REMARK 500 1 ARG A 61 0.23 SIDE CHAIN
REMARK 500 1 ARG A 63 0.23 SIDE CHAIN
REMARK 500 1 ARG A 69 0.31 SIDE CHAIN
REMARK 500 1 ARG A 87 0.31 SIDE CHAIN
REMARK 500 1 ARG A 90 0.32 SIDE CHAIN
REMARK 500 2 ARG A 30 0.29 SIDE CHAIN
REMARK 500 2 ARG A 47 0.28 SIDE CHAIN
REMARK 500 2 ARG A 50 0.31 SIDE CHAIN
REMARK 500 2 ARG A 59 0.30 SIDE CHAIN
REMARK 500 2 ARG A 61 0.30 SIDE CHAIN
REMARK 500 2 ARG A 63 0.24 SIDE CHAIN
REMARK 500 2 ARG A 69 0.30 SIDE CHAIN
REMARK 500 2 ARG A 87 0.28 SIDE CHAIN
REMARK 500 2 ARG A 90 0.24 SIDE CHAIN
REMARK 500 3 ARG A 30 0.31 SIDE CHAIN
REMARK 500 3 ARG A 47 0.14 SIDE CHAIN
REMARK 500 3 ARG A 50 0.31 SIDE CHAIN
REMARK 500 3 ARG A 59 0.30 SIDE CHAIN
REMARK 500 3 ARG A 61 0.28 SIDE CHAIN
REMARK 500 3 ARG A 63 0.17 SIDE CHAIN
REMARK 500 3 ARG A 69 0.18 SIDE CHAIN
REMARK 500 3 ARG A 87 0.28 SIDE CHAIN
REMARK 500 3 ARG A 90 0.31 SIDE CHAIN
REMARK 500 4 ARG A 30 0.31 SIDE CHAIN
REMARK 500 4 ARG A 47 0.32 SIDE CHAIN
REMARK 500 4 ARG A 50 0.29 SIDE CHAIN
REMARK 500 4 ARG A 59 0.23 SIDE CHAIN
REMARK 500 4 ARG A 61 0.28 SIDE CHAIN
REMARK 500 4 ARG A 63 0.31 SIDE CHAIN
REMARK 500 4 ARG A 69 0.09 SIDE CHAIN
REMARK 500 4 ARG A 87 0.20 SIDE CHAIN
REMARK 500 4 ARG A 90 0.08 SIDE CHAIN
REMARK 500 5 ARG A 30 0.31 SIDE CHAIN
REMARK 500 5 ARG A 47 0.26 SIDE CHAIN
REMARK 500 5 ARG A 50 0.26 SIDE CHAIN
REMARK 500 5 ARG A 59 0.31 SIDE CHAIN
REMARK 500 5 ARG A 61 0.28 SIDE CHAIN
REMARK 500 5 ARG A 63 0.18 SIDE CHAIN
REMARK 500 5 ARG A 69 0.29 SIDE CHAIN
REMARK 500 5 ARG A 87 0.30 SIDE CHAIN
REMARK 500 5 ARG A 90 0.18 SIDE CHAIN
REMARK 500 6 ARG A 30 0.23 SIDE CHAIN
REMARK 500 6 ARG A 47 0.26 SIDE CHAIN
REMARK 500 6 ARG A 50 0.30 SIDE CHAIN
REMARK 500 6 ARG A 59 0.24 SIDE CHAIN
REMARK 500 6 ARG A 61 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 225 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1YUA A 2 122 UNP P06612 TOP1_ECOLI 745 865
SEQRES 1 A 122 MET ASN GLY GLU VAL ALA PRO PRO LYS GLU ASP PRO VAL
SEQRES 2 A 122 PRO LEU PRO GLU LEU PRO CYS GLU LYS SER ASP ALA TYR
SEQRES 3 A 122 PHE VAL LEU ARG ASP GLY ALA ALA GLY VAL PHE LEU ALA
SEQRES 4 A 122 ALA ASN THR PHE PRO LYS SER ARG GLU THR ARG ALA PRO
SEQRES 5 A 122 LEU VAL GLU GLU LEU TYR ARG PHE ARG ASP ARG LEU PRO
SEQRES 6 A 122 GLU LYS LEU ARG TYR LEU ALA ASP ALA PRO GLN GLN ASP
SEQRES 7 A 122 PRO GLU GLY ASN LYS THR MET VAL ARG PHE SER ARG LYS
SEQRES 8 A 122 THR LYS GLN GLN TYR VAL SER SER GLU LYS ASP GLY LYS
SEQRES 9 A 122 ALA THR GLY TRP SER ALA PHE TYR VAL ASP GLY LYS TRP
SEQRES 10 A 122 VAL GLU GLY LYS LYS
HELIX 1 H1 LEU A 53 ARG A 59 1 7
HELIX 2 H2 ARG A 69 ASP A 73 1 5
SHEET 1 SH1 4 VAL A 13 PRO A 16 0
SHEET 2 SH1 4 TYR A 26 GLY A 32 -1 N LEU A 29 O VAL A 13
SHEET 3 SH1 4 GLY A 35 ALA A 40 -1 N PHE A 37 O ARG A 30
SHEET 4 SH1 4 THR A 49 ALA A 51 -1 N ARG A 50 O LEU A 38
SHEET 1 SH2 4 THR A 84 ARG A 90 0
SHEET 2 SH2 4 LYS A 93 SER A 99 -1 N GLN A 94 O SER A 89
SHEET 3 SH2 4 TRP A 108 VAL A 113 -1 N ALA A 110 O VAL A 97
SHEET 4 SH2 4 LYS A 116 GLU A 119 -1 N VAL A 118 O PHE A 111
CISPEP 1 PHE A 43 PRO A 44 1 -0.33
CISPEP 2 PHE A 43 PRO A 44 2 -0.72
CISPEP 3 PHE A 43 PRO A 44 3 -0.29
CISPEP 4 PHE A 43 PRO A 44 4 -0.29
CISPEP 5 PHE A 43 PRO A 44 5 -0.34
CISPEP 6 PHE A 43 PRO A 44 6 -0.33
CISPEP 7 PHE A 43 PRO A 44 7 -0.34
CISPEP 8 PHE A 43 PRO A 44 8 -0.24
CISPEP 9 PHE A 43 PRO A 44 9 -0.73
CISPEP 10 PHE A 43 PRO A 44 10 -0.64
CISPEP 11 PHE A 43 PRO A 44 11 -0.21
CISPEP 12 PHE A 43 PRO A 44 12 -0.30
CISPEP 13 PHE A 43 PRO A 44 13 -0.48
CISPEP 14 PHE A 43 PRO A 44 14 -0.55
CISPEP 15 PHE A 43 PRO A 44 15 -0.39
CISPEP 16 PHE A 43 PRO A 44 16 -0.35
CISPEP 17 PHE A 43 PRO A 44 17 -0.28
CISPEP 18 PHE A 43 PRO A 44 18 -0.43
CISPEP 19 PHE A 43 PRO A 44 19 -0.56
CISPEP 20 PHE A 43 PRO A 44 20 -0.53
CISPEP 21 PHE A 43 PRO A 44 21 -0.32
CISPEP 22 PHE A 43 PRO A 44 22 -0.79
CISPEP 23 PHE A 43 PRO A 44 23 -0.35
CISPEP 24 PHE A 43 PRO A 44 24 -0.42
CISPEP 25 PHE A 43 PRO A 44 25 -0.54
CISPEP 26 PHE A 43 PRO A 44 26 -0.20
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 - v 29 2 Bytes