Header list of 1wtu.pdb file
Complete list - 2 20 Bytes
HEADER TRANSCRIPTION FACTOR 29-JUL-96 1WTU
TITLE TRANSCRIPTION FACTOR 1, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TF1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: THIS PROTEIN IS THE BACILLUS SUBTILIS PHAGE SPO1-
COMPND 7 ENCODED TYPE II DNA-BINDING PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PHAGE SPO1;
SOURCE 3 ORGANISM_TAXID: 10685;
SOURCE 4 GENE: TF1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKJB842;
SOURCE 8 EXPRESSION_SYSTEM_GENE: TF1
KEYWDS TRANSCRIPTION FACTOR, TYPE II DNA-BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR X.JIA,A.GROVE,M.IVANCIC,V.L.HSU,E.P.GEIDUSCHEK,D.R.KEARNS
REVDAT 3 02-MAR-22 1WTU 1 REMARK
REVDAT 2 24-FEB-09 1WTU 1 VERSN
REVDAT 1 12-FEB-97 1WTU 0
JRNL AUTH X.JIA,A.GROVE,M.IVANCIC,V.L.HSU,E.P.GEIDUSCHECK,D.R.KEARNS
JRNL TITL STRUCTURE OF THE BACILLUS SUBTILIS PHAGE SPO1-ENCODED TYPE
JRNL TITL 2 II DNA-BINDING PROTEIN TF1 IN SOLUTION.
JRNL REF J.MOL.BIOL. V. 263 259 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8913305
JRNL DOI 10.1006/JMBI.1996.0573
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.JIA,J.M.REISMAN,V.L.HSU,E.P.GEIDUSCHEK,J.PARELLO,
REMARK 1 AUTH 2 D.R.KEARNS
REMARK 1 TITL PROTON AND NITROGEN NMR SEQUENCE-SPECIFIC ASSIGNMENTS AND
REMARK 1 TITL 2 SECONDARY STRUCTURE DETERMINATION OF THE BACILLUS SUBTILIS
REMARK 1 TITL 3 SPO1-ENCODED TRANSCRIPTION FACTOR 1
REMARK 1 REF BIOCHEMISTRY V. 33 8842 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH I.TANAKA,K.APPELT,J.DIJK,S.W.WHITE,K.S.WILSON
REMARK 1 TITL 3-A RESOLUTION STRUCTURE OF A PROTEIN WITH HISTONE-LIKE
REMARK 1 TITL 2 PROPERTIES IN PROKARYOTES
REMARK 1 REF NATURE V. 310 376 1984
REMARK 1 REFN ISSN 0028-0836
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 1WTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177234.
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 : 1
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 SER A 74 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 TYR A 94 CB - CG - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 TYR A 94 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 PHE A 97 CB - CG - CD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 PRO B 63 C - N - CD ANGL. DEV. = -13.6 DEGREES
REMARK 500 PRO B 73 C - N - CD ANGL. DEV. = -13.7 DEGREES
REMARK 500 TYR B 94 CB - CG - CD2 ANGL. DEV. = -4.6 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 ASN A 2 -90.62 63.41
REMARK 500 ASP A 13 -80.21 -109.98
REMARK 500 LEU A 16 -61.48 -6.46
REMARK 500 THR A 33 -52.71 -26.77
REMARK 500 THR A 35 -75.80 -59.36
REMARK 500 ALA A 37 -74.02 -46.63
REMARK 500 ASP A 40 -54.85 -27.15
REMARK 500 LYS A 41 105.70 -43.00
REMARK 500 THR A 45 50.43 34.99
REMARK 500 PHE A 47 -51.62 -136.40
REMARK 500 LYS A 51 108.84 -163.12
REMARK 500 ARG A 55 85.36 -165.43
REMARK 500 GLN A 56 -51.11 -135.44
REMARK 500 ALA A 57 102.17 55.16
REMARK 500 ARG A 58 97.83 177.04
REMARK 500 LYS A 59 -93.68 -75.25
REMARK 500 ASN A 62 172.84 163.90
REMARK 500 GLN A 64 -80.47 -157.31
REMARK 500 GLN A 66 30.85 131.25
REMARK 500 GLU A 67 86.16 40.94
REMARK 500 ALA A 68 -87.57 -172.35
REMARK 500 LEU A 69 -81.17 80.21
REMARK 500 GLU A 70 -112.13 -121.28
REMARK 500 VAL A 75 154.67 172.29
REMARK 500 GLU A 83 -25.49 -33.41
REMARK 500 ALA A 89 10.72 -66.53
REMARK 500 ASN B 2 -84.39 -137.56
REMARK 500 ASP B 13 -80.65 -109.98
REMARK 500 THR B 14 -165.34 -74.15
REMARK 500 GLU B 15 19.43 49.84
REMARK 500 LEU B 16 -47.10 -23.51
REMARK 500 THR B 35 -82.57 -53.59
REMARK 500 ASP B 40 -71.91 -19.78
REMARK 500 LYS B 41 113.89 -29.78
REMARK 500 PHE B 47 -42.04 -132.70
REMARK 500 LYS B 51 88.82 -156.55
REMARK 500 ARG B 55 72.70 -153.63
REMARK 500 GLN B 56 -165.06 28.53
REMARK 500 LYS B 59 98.99 39.37
REMARK 500 ASN B 62 -159.47 165.44
REMARK 500 GLN B 64 -61.66 -175.70
REMARK 500 GLN B 66 130.75 1.18
REMARK 500 GLU B 67 93.42 0.02
REMARK 500 ALA B 68 -106.96 -163.37
REMARK 500 LEU B 69 175.46 56.65
REMARK 500 GLU B 70 63.41 -110.96
REMARK 500 ALA B 72 -38.95 -176.85
REMARK 500 SER B 74 -156.23 56.93
REMARK 500 VAL B 75 -48.31 -130.34
REMARK 500 PRO B 81 -158.86 -99.71
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 ALA B 54 ARG B 55 138.50
REMARK 500 PHE B 61 ASN B 62 -144.98
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 ARG A 55 0.22 SIDE CHAIN
REMARK 500 ARG A 58 0.27 SIDE CHAIN
REMARK 500 TYR A 94 0.22 SIDE CHAIN
REMARK 500 PHE A 97 0.13 SIDE CHAIN
REMARK 500 ARG B 55 0.32 SIDE CHAIN
REMARK 500 ARG B 58 0.23 SIDE CHAIN
REMARK 500 TYR B 94 0.14 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 TYR A 94 12.31
REMARK 500 ALA B 54 -11.83
REMARK 500 ARG B 55 -10.49
REMARK 500 PHE B 61 13.54
REMARK 500 TYR B 94 10.26
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WTU A 1 99 UNP P04445 TF1_BPSP1 1 99
DBREF 1WTU B 1 99 UNP P04445 TF1_BPSP1 1 99
SEQRES 1 A 99 MET ASN LYS THR GLU LEU ILE LYS ALA ILE ALA GLN ASP
SEQRES 2 A 99 THR GLU LEU THR GLN VAL SER VAL SER LYS MET LEU ALA
SEQRES 3 A 99 SER PHE GLU LYS ILE THR THR GLU THR VAL ALA LYS GLY
SEQRES 4 A 99 ASP LYS VAL GLN LEU THR GLY PHE LEU ASN ILE LYS PRO
SEQRES 5 A 99 VAL ALA ARG GLN ALA ARG LYS GLY PHE ASN PRO GLN THR
SEQRES 6 A 99 GLN GLU ALA LEU GLU ILE ALA PRO SER VAL GLY VAL SER
SEQRES 7 A 99 VAL LYS PRO GLY GLU SER LEU LYS LYS ALA ALA GLU GLY
SEQRES 8 A 99 LEU LYS TYR GLU ASP PHE ALA LYS
SEQRES 1 B 99 MET ASN LYS THR GLU LEU ILE LYS ALA ILE ALA GLN ASP
SEQRES 2 B 99 THR GLU LEU THR GLN VAL SER VAL SER LYS MET LEU ALA
SEQRES 3 B 99 SER PHE GLU LYS ILE THR THR GLU THR VAL ALA LYS GLY
SEQRES 4 B 99 ASP LYS VAL GLN LEU THR GLY PHE LEU ASN ILE LYS PRO
SEQRES 5 B 99 VAL ALA ARG GLN ALA ARG LYS GLY PHE ASN PRO GLN THR
SEQRES 6 B 99 GLN GLU ALA LEU GLU ILE ALA PRO SER VAL GLY VAL SER
SEQRES 7 B 99 VAL LYS PRO GLY GLU SER LEU LYS LYS ALA ALA GLU GLY
SEQRES 8 B 99 LEU LYS TYR GLU ASP PHE ALA LYS
HELIX 1 1 LYS A 3 GLN A 12 1 10
HELIX 2 2 GLN A 18 GLY A 39 1 22
HELIX 3 3 GLU A 83 GLU A 90 1 8
HELIX 4 4 LYS A 93 ASP A 96 1 4
HELIX 5 5 LYS B 3 GLN B 12 1 10
HELIX 6 6 GLN B 18 GLY B 39 1 22
HELIX 7 7 SER B 84 ALA B 89 1 6
SHEET 1 A 2 ASN A 49 PRO A 52 0
SHEET 2 A 2 VAL A 77 LYS A 80 -1 N LYS A 80 O ASN A 49
SHEET 1 B 2 ASN B 49 VAL B 53 0
SHEET 2 B 2 GLY B 76 LYS B 80 -1 N LYS B 80 O ASN B 49
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
Complete list - 2 20 Bytes