Header list of 1pou.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 14-JUN-93 1POU
TITLE THE SOLUTION STRUCTURE OF THE OCT-1 POU-SPECIFIC DOMAIN REVEALS A
TITLE 2 STRIKING SIMILARITY TO THE BACTERIOPHAGE LAMBDA REPRESSOR DNA-BINDING
TITLE 3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OCT-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.ASSA-MUNT,R.J.MORTISHIRE-SMITH,R.AURORA,W.HERR,P.E.WRIGHT
REVDAT 3 02-MAR-22 1POU 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 1POU 1 VERSN
REVDAT 1 15-OCT-94 1POU 0
JRNL AUTH N.ASSA-MUNT,R.J.MORTISHIRE-SMITH,R.AURORA,W.HERR,P.E.WRIGHT
JRNL TITL THE SOLUTION STRUCTURE OF THE OCT-1 POU-SPECIFIC DOMAIN
JRNL TITL 2 REVEALS A STRIKING SIMILARITY TO THE BACTERIOPHAGE LAMBDA
JRNL TITL 3 REPRESSOR DNA-BINDING DOMAIN.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 73 193 1993
JRNL REFN ISSN 0092-8674
JRNL PMID 8462099
JRNL DOI 10.1016/0092-8674(93)90171-L
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, AMBER
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1POU 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_1000175774.
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 : 20
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 GLN A 27 -71.87 59.51
REMARK 500 1 GLN A 44 -53.03 72.53
REMARK 500 1 THR A 45 -70.80 -41.66
REMARK 500 1 ASN A 54 35.22 -83.90
REMARK 500 1 SER A 56 60.84 28.64
REMARK 500 1 PHE A 57 -58.59 68.89
REMARK 500 2 GLN A 27 -107.40 50.38
REMARK 500 2 THR A 45 -73.59 -53.04
REMARK 500 2 SER A 56 101.54 -33.73
REMARK 500 2 PHE A 57 -58.24 68.65
REMARK 500 3 TYR A 38 -63.53 -145.16
REMARK 500 3 ASP A 41 -151.86 -81.64
REMARK 500 3 GLN A 44 -67.36 66.39
REMARK 500 3 THR A 45 -73.40 -28.45
REMARK 500 3 SER A 56 85.43 -24.17
REMARK 500 3 PHE A 57 -57.76 68.43
REMARK 500 4 TYR A 38 -61.40 -146.24
REMARK 500 4 ASN A 40 38.87 -78.73
REMARK 500 4 ASP A 41 41.75 -81.38
REMARK 500 4 PHE A 42 33.81 -147.45
REMARK 500 4 GLN A 44 -60.56 68.96
REMARK 500 4 SER A 56 -65.16 69.91
REMARK 500 4 PHE A 57 -53.28 -166.18
REMARK 500 5 TYR A 38 -59.05 -126.30
REMARK 500 5 PHE A 42 47.17 -148.13
REMARK 500 5 GLN A 44 -54.25 -159.29
REMARK 500 5 LEU A 53 44.88 36.83
REMARK 500 5 SER A 56 -179.89 -68.11
REMARK 500 6 GLN A 27 -72.21 57.95
REMARK 500 6 TYR A 38 -65.19 -148.96
REMARK 500 6 ASP A 41 -155.04 -92.24
REMARK 500 6 GLN A 44 -42.28 67.29
REMARK 500 6 THR A 45 -70.49 -42.26
REMARK 500 6 PHE A 57 -50.81 67.84
REMARK 500 7 GLN A 27 -75.30 54.27
REMARK 500 7 TYR A 38 -61.37 -145.88
REMARK 500 7 ASN A 40 36.44 -78.07
REMARK 500 7 ASP A 41 38.51 -83.33
REMARK 500 7 PHE A 42 42.79 -152.75
REMARK 500 7 GLN A 44 -47.64 -154.43
REMARK 500 7 LEU A 55 46.17 -81.18
REMARK 500 7 SER A 56 85.35 -21.93
REMARK 500 7 PHE A 57 -57.37 69.25
REMARK 500 8 THR A 26 35.55 -77.52
REMARK 500 8 GLN A 27 -57.97 63.08
REMARK 500 8 TYR A 38 -56.59 -133.32
REMARK 500 8 GLN A 44 -69.62 72.41
REMARK 500 8 LEU A 55 45.19 -81.24
REMARK 500 8 SER A 56 77.00 -15.54
REMARK 500 8 PHE A 57 -57.11 69.22
REMARK 500
REMARK 500 THIS ENTRY HAS 133 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 20 0.09 SIDE CHAIN
REMARK 500 1 TYR A 38 0.07 SIDE CHAIN
REMARK 500 2 PHE A 16 0.08 SIDE CHAIN
REMARK 500 2 ARG A 20 0.12 SIDE CHAIN
REMARK 500 3 PHE A 12 0.08 SIDE CHAIN
REMARK 500 3 TYR A 38 0.13 SIDE CHAIN
REMARK 500 4 TYR A 38 0.08 SIDE CHAIN
REMARK 500 4 PHE A 42 0.08 SIDE CHAIN
REMARK 500 6 TYR A 38 0.07 SIDE CHAIN
REMARK 500 8 PHE A 50 0.09 SIDE CHAIN
REMARK 500 9 TYR A 38 0.10 SIDE CHAIN
REMARK 500 9 PHE A 50 0.09 SIDE CHAIN
REMARK 500 11 TYR A 38 0.10 SIDE CHAIN
REMARK 500 11 PHE A 50 0.08 SIDE CHAIN
REMARK 500 12 TYR A 38 0.08 SIDE CHAIN
REMARK 500 14 PHE A 50 0.09 SIDE CHAIN
REMARK 500 14 PHE A 57 0.16 SIDE CHAIN
REMARK 500 15 ARG A 20 0.09 SIDE CHAIN
REMARK 500 16 PHE A 12 0.08 SIDE CHAIN
REMARK 500 16 ARG A 20 0.08 SIDE CHAIN
REMARK 500 17 PHE A 42 0.09 SIDE CHAIN
REMARK 500 18 TYR A 38 0.08 SIDE CHAIN
REMARK 500 20 TYR A 38 0.09 SIDE CHAIN
REMARK 500 20 PHE A 42 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1POU A 5 75 UNP P14859 PO2F1_HUMAN 284 354
SEQRES 1 A 71 ASP LEU GLU GLU LEU GLU GLN PHE ALA LYS THR PHE LYS
SEQRES 2 A 71 GLN ARG ARG ILE LYS LEU GLY PHE THR GLN GLY ASP VAL
SEQRES 3 A 71 GLY LEU ALA MET GLY LYS LEU TYR GLY ASN ASP PHE SER
SEQRES 4 A 71 GLN THR THR ILE SER ARG PHE GLU ALA LEU ASN LEU SER
SEQRES 5 A 71 PHE LYS ASN MET CYS LYS LEU LYS PRO LEU LEU GLU LYS
SEQRES 6 A 71 TRP LEU ASN ASP ALA GLU
HELIX 1 1 ASP A 5 LEU A 23 1 19
HELIX 2 2 GLN A 27 LEU A 37 1 11
HELIX 3 3 GLN A 44 ALA A 52 1 9
HELIX 4 4 PHE A 57 ALA A 74 1 18
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 - r 2 2 Bytes