Header list of 2r63.pdb file
Complete list - v 3 2 Bytes
HEADER GENE REGULATING PROTEIN 13-NOV-96 2R63
TITLE STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR DNA-
TITLE 2 BINDING DOMAIN, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REPRESSOR PROTEIN FROM BACTERIOPHAGE 434;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 1 - 63;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PHAGE 434;
SOURCE 3 ORGANISM_TAXID: 10712;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GENE REGULATING PROTEIN, PHAGE 434 REPRESSOR, HELIX-TURN-HELIX, DNA-
KEYWDS 2 BINDING DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.V.PERVUSHIN,M.BILLETER,G.SIEGAL,K.WUTHRICH
REVDAT 3 03-NOV-21 2R63 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2R63 1 VERSN
REVDAT 1 16-JUN-97 2R63 0
JRNL AUTH K.PERVUSHIN,M.BILLETER,G.SIEGAL,K.WUTHRICH
JRNL TITL STRUCTURAL ROLE OF A BURIED SALT BRIDGE IN THE 434 REPRESSOR
JRNL TITL 2 DNA-BINDING DOMAIN.
JRNL REF J.MOL.BIOL. V. 264 1002 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 9000626
JRNL DOI 10.1006/JMBI.1996.0692
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.NERI,M.BILLETER,K.WUTHRICH
REMARK 1 TITL DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE SOLUTION
REMARK 1 TITL 2 STRUCTURE OF THE DNA-BINDING DOMAIN (RESIDUES 1 TO 69) OF
REMARK 1 TITL 3 THE 434 REPRESSOR AND COMPARISON WITH THE X-RAY CRYSTAL
REMARK 1 TITL 4 STRUCTURE
REMARK 1 REF J.MOL.BIOL. V. 223 743 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.MONDRAGON,S.SUBBIAH,S.C.ALMO,M.DROTTAR,S.C.HARRISON
REMARK 1 TITL STRUCTURE OF THE AMINO-TERMINAL DOMAIN OF PHAGE 434
REMARK 1 TITL 2 REPRESSOR AT 2.0 A RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 205 189 1989
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPAL
REMARK 3 AUTHORS : LUGINBUHL,GUNTERT,BILLETER,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R63 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_1000178544.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 286
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; E.COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY PLUS 750
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VARIAN VNMR VNMR, DIANA, OPAL
REMARK 210 METHOD USED : DISTANCE GEOMETRY WITH DIANA,
REMARK 210 ENERGY MINIMIZATION WITH OPAL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : DIANA PENALTY FUNCTION
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: 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 9 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 11 ARG A 5 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 13 ARG A 41 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ARG A 43 33.81 -80.39
REMARK 500 1 PHE A 44 24.24 -167.36
REMARK 500 1 ASN A 61 -83.21 -83.71
REMARK 500 2 LYS A 40 -82.75 -85.89
REMARK 500 2 PHE A 44 39.22 -73.58
REMARK 500 2 LEU A 60 -72.99 -71.12
REMARK 500 2 ASN A 61 51.49 -156.72
REMARK 500 4 LYS A 38 -80.47 -105.29
REMARK 500 4 THR A 39 117.79 55.77
REMARK 500 4 PHE A 44 48.76 -75.87
REMARK 500 4 ASN A 61 -71.59 -137.46
REMARK 500 5 PHE A 44 35.21 -77.33
REMARK 500 5 ASN A 61 -80.38 -156.15
REMARK 500 6 LYS A 40 -69.74 -91.12
REMARK 500 6 PHE A 44 42.75 -80.77
REMARK 500 6 ASN A 61 -71.80 -100.74
REMARK 500 7 VAL A 6 -71.48 -65.18
REMARK 500 7 ASN A 36 7.83 -69.50
REMARK 500 7 LYS A 38 -62.89 -92.79
REMARK 500 7 LYS A 40 -79.48 -80.02
REMARK 500 7 ARG A 43 47.42 -79.05
REMARK 500 7 PHE A 44 19.32 -177.87
REMARK 500 7 LEU A 60 -73.09 -52.36
REMARK 500 7 ASN A 61 65.96 -156.87
REMARK 500 8 ASN A 36 0.31 -65.02
REMARK 500 8 LYS A 40 -63.72 -107.43
REMARK 500 8 PHE A 44 44.36 -80.36
REMARK 500 8 ASN A 61 -93.70 -130.96
REMARK 500 9 PRO A 42 -176.59 -66.44
REMARK 500 9 ASN A 61 13.23 -155.54
REMARK 500 10 LYS A 38 36.75 -90.55
REMARK 500 10 THR A 39 179.63 67.36
REMARK 500 10 PHE A 44 47.02 -80.02
REMARK 500 10 ASN A 61 -78.73 -96.33
REMARK 500 11 PHE A 44 40.20 -76.08
REMARK 500 11 ASN A 61 16.61 -152.18
REMARK 500 12 LYS A 40 -74.81 -66.51
REMARK 500 12 ARG A 43 34.46 -89.80
REMARK 500 12 PHE A 44 30.28 -154.10
REMARK 500 12 ASN A 61 -76.53 -99.22
REMARK 500 13 LYS A 9 -70.89 -60.84
REMARK 500 13 LYS A 38 35.86 -76.39
REMARK 500 13 THR A 39 164.41 72.80
REMARK 500 13 PHE A 44 36.62 -72.79
REMARK 500 13 ASN A 61 15.69 -156.76
REMARK 500 14 LYS A 40 -68.54 -108.61
REMARK 500 14 PHE A 44 44.74 -79.15
REMARK 500 15 ILE A 2 -53.85 -159.44
REMARK 500 15 ARG A 43 48.66 -77.90
REMARK 500 15 PHE A 44 25.69 -170.51
REMARK 500
REMARK 500 THIS ENTRY HAS 67 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 5 ARG A 43 0.11 SIDE CHAIN
REMARK 500 8 ARG A 41 0.09 SIDE CHAIN
REMARK 500 8 ARG A 43 0.07 SIDE CHAIN
REMARK 500 9 ARG A 5 0.15 SIDE CHAIN
REMARK 500 10 ARG A 5 0.10 SIDE CHAIN
REMARK 500 10 ARG A 43 0.10 SIDE CHAIN
REMARK 500 14 ARG A 5 0.10 SIDE CHAIN
REMARK 500 14 ARG A 41 0.14 SIDE CHAIN
REMARK 500 14 ARG A 43 0.11 SIDE CHAIN
REMARK 500 15 ARG A 5 0.09 SIDE CHAIN
REMARK 500 16 ARG A 41 0.10 SIDE CHAIN
REMARK 500 17 ARG A 5 0.11 SIDE CHAIN
REMARK 500 17 ARG A 41 0.09 SIDE CHAIN
REMARK 500 19 ARG A 41 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2R63 A 1 63 UNP P16117 RPC1_BP434 1 63
SEQADV 2R63 MET A 10 UNP P16117 ARG 10 ENGINEERED MUTATION
SEQRES 1 A 63 SER ILE SER SER ARG VAL LYS SER LYS MET ILE GLN LEU
SEQRES 2 A 63 GLY LEU ASN GLN ALA GLU LEU ALA GLN LYS VAL GLY THR
SEQRES 3 A 63 THR GLN GLN SER ILE GLU GLN LEU GLU ASN GLY LYS THR
SEQRES 4 A 63 LYS ARG PRO ARG PHE LEU PRO GLU LEU ALA SER ALA LEU
SEQRES 5 A 63 GLY VAL SER VAL ASP TRP LEU LEU ASN GLY THR
HELIX 1 H1 ILE A 2 LEU A 13 5 12
HELIX 2 H2 GLN A 17 VAL A 24 5 8
HELIX 3 H3 GLN A 28 GLU A 35 5 8
HELIX 4 H4 LEU A 45 LEU A 52 5 8
HELIX 5 H5 VAL A 56 ASN A 61 5 6
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 3 2 Bytes