Header list of 1kdx.pdb file
Complete list - v 3 2 Bytes
HEADER TRANSCRIPTION REGULATION COMPLEX 16-SEP-97 1KDX
TITLE KIX DOMAIN OF MOUSE CBP (CREB BINDING PROTEIN) IN COMPLEX WITH
TITLE 2 PHOSPHORYLATED KINASE INDUCIBLE DOMAIN (PKID) OF RAT CREB (CYCLIC AMP
TITLE 3 RESPONSE ELEMENT BINDING PROTEIN), NMR 17 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CBP;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KIX, RESIDUES 586-666;
COMPND 5 SYNONYM: CREB-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: PHOSPHORYLATED AT SER 133;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CREB;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: KID, RESIDUES 101-160;
COMPND 12 SYNONYM: CAMP-RESPONSE ELEMENT BINDING PROTEIN, CREB;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: PHOSPHORYLATED AT SER 133
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 12 ORGANISM_COMMON: NORWAY RAT;
SOURCE 13 ORGANISM_TAXID: 10116;
SOURCE 14 CELL_LINE: BL21;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET24A(+)
KEYWDS COMPLEX (TRANSCRIPTION ACTIVATOR-CO-ACTIVATOR), PROTEIN-PROTEIN
KEYWDS 2 INTERACTION, PHOSPHOSERINE RECOGNITION, TRANSCRIPTION REGULATION
KEYWDS 3 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR I.RADHAKRISHNAN,G.C.PEREZ-ALVARADO,H.J.DYSON,P.E.WRIGHT
REVDAT 3 03-NOV-21 1KDX 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1KDX 1 VERSN
REVDAT 1 25-NOV-98 1KDX 0
JRNL AUTH I.RADHAKRISHNAN,G.C.PEREZ-ALVARADO,D.PARKER,H.J.DYSON,
JRNL AUTH 2 M.R.MONTMINY,P.E.WRIGHT
JRNL TITL SOLUTION STRUCTURE OF THE KIX DOMAIN OF CBP BOUND TO THE
JRNL TITL 2 TRANSACTIVATION DOMAIN OF CREB: A MODEL FOR
JRNL TITL 3 ACTIVATOR:COACTIVATOR INTERACTIONS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 91 741 1997
JRNL REFN ISSN 0092-8674
JRNL PMID 9413984
JRNL DOI 10.1016/S0092-8674(00)80463-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : WUTHRICH PROGRAM 2 : AMBER 4.1 AUTHORS 2 :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, FERGUSON,
REMARK 3 SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KDX 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_1000174417.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 315
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 0.07
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O OR D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE-RESONANCE EXPERIMENTS:
REMARK 210 HNCA; HN(CO)CA; CBCA(CO)NH;
REMARK 210 HNCACB; DOUBLE-RESONANCE: 15N-
REMARK 210 EDITED TOCSY; HCCH-TOCSY; HCCH-
REMARK 210 COSY; FOR RESTRAINT GENERATION:
REMARK 210 15N- AND 13C-EDITED NOESYS;
REMARK 210 SELECT-FILTERED NOESY; DOUBLE
REMARK 210 HALF-FILTERED NOESY; HNHA;
REMARK 210 CONSTANT-TIME SPIN-ECHO
REMARK 210 DIFFERENCE EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MSI FELIX95 FELIX95
REMARK 210 METHOD USED : DG, SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST CONSTRAINT ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING RESTRAINTS DERIVED FROM
REMARK 210 15N- AND 13C-EDITED NOESYS, SELECT-FILTERED NOESY, DOUBLE HALF-
REMARK 210 FILTERED NOESY, HNHA AND CONSTANT TIME SPIN-ECHO-DIFFERENCE
REMARK 210 EXPERIMENTS.
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 6 ARG A 623 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 7 TYR B 134 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 11 ARG A 600 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 14 TYR B 134 CB - CG - CD2 ANGL. DEV. = -3.6 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 1 VAL A 587 -145.49 44.61
REMARK 500 1 PRO A 613 97.21 -67.20
REMARK 500 1 GLU A 641 20.88 -79.72
REMARK 500 1 SER A 642 -48.35 -132.10
REMARK 500 1 GLN A 661 -61.94 -101.12
REMARK 500 1 LEU A 664 -72.19 -64.81
REMARK 500 1 PRO B 132 -9.71 -55.66
REMARK 500 2 LYS A 589 166.26 61.97
REMARK 500 2 GLU A 665 -42.43 72.70
REMARK 500 2 ASP B 120 -58.53 -29.28
REMARK 500 2 ARG B 131 135.27 -176.75
REMARK 500 2 PRO B 132 -166.68 -73.73
REMARK 500 2 SEP B 133 -59.39 74.28
REMARK 500 3 VAL A 587 -136.31 44.50
REMARK 500 3 LYS A 589 49.93 39.49
REMARK 500 3 SER A 642 -55.28 -169.06
REMARK 500 3 GLN A 661 -64.57 -105.81
REMARK 500 3 GLU A 665 -55.77 71.96
REMARK 500 3 ARG B 130 46.44 -80.44
REMARK 500 3 ARG B 131 82.96 -156.40
REMARK 500 3 PRO B 132 -38.36 -34.56
REMARK 500 4 ARG A 588 -143.21 -149.33
REMARK 500 4 THR A 596 153.38 -47.93
REMARK 500 4 PRO A 615 -111.71 -81.04
REMARK 500 4 GLU A 641 31.24 -91.76
REMARK 500 4 SER A 642 -64.94 -137.83
REMARK 500 5 VAL A 587 -145.26 44.22
REMARK 500 5 LYS A 589 81.26 61.67
REMARK 500 5 TRP A 591 -19.27 -47.79
REMARK 500 5 PRO A 613 93.41 -67.89
REMARK 500 5 SER A 642 -54.33 -167.61
REMARK 500 5 GLN A 661 -80.42 -92.56
REMARK 500 5 ARG B 131 -40.76 124.68
REMARK 500 5 SEP B 133 30.63 -43.96
REMARK 500 6 VAL A 587 -138.97 46.17
REMARK 500 6 ARG A 588 -105.56 -135.22
REMARK 500 6 PRO A 613 99.11 -43.10
REMARK 500 6 SER A 642 -55.22 -121.71
REMARK 500 6 ALA A 643 108.87 -54.50
REMARK 500 6 ASN A 644 43.66 -83.62
REMARK 500 6 SER A 645 147.15 175.36
REMARK 500 6 GLN A 661 -73.14 -104.29
REMARK 500 6 ARG B 130 -52.76 -138.54
REMARK 500 7 ARG A 588 -159.51 -151.50
REMARK 500 7 LYS A 589 106.38 -42.94
REMARK 500 7 PRO A 613 82.37 -69.86
REMARK 500 7 SER A 642 -54.09 -128.49
REMARK 500 7 GLN A 661 -67.74 -97.90
REMARK 500 8 GLN A 661 -65.02 -103.35
REMARK 500 8 GLU B 126 -78.39 -46.82
REMARK 500
REMARK 500 THIS ENTRY HAS 97 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 PHE A 612 0.10 SIDE CHAIN
REMARK 500 1 TYR A 640 0.13 SIDE CHAIN
REMARK 500 1 TYR A 649 0.10 SIDE CHAIN
REMARK 500 1 TYR A 658 0.08 SIDE CHAIN
REMARK 500 1 ARG B 130 0.14 SIDE CHAIN
REMARK 500 1 TYR B 134 0.10 SIDE CHAIN
REMARK 500 2 PHE A 612 0.12 SIDE CHAIN
REMARK 500 2 TYR A 640 0.14 SIDE CHAIN
REMARK 500 2 TYR A 649 0.18 SIDE CHAIN
REMARK 500 2 TYR A 650 0.10 SIDE CHAIN
REMARK 500 2 TYR B 134 0.07 SIDE CHAIN
REMARK 500 3 PHE A 612 0.14 SIDE CHAIN
REMARK 500 3 TYR A 640 0.09 SIDE CHAIN
REMARK 500 3 TYR A 649 0.12 SIDE CHAIN
REMARK 500 3 TYR A 650 0.06 SIDE CHAIN
REMARK 500 3 TYR B 134 0.10 SIDE CHAIN
REMARK 500 4 ARG A 588 0.09 SIDE CHAIN
REMARK 500 4 PHE A 612 0.10 SIDE CHAIN
REMARK 500 4 TYR A 640 0.08 SIDE CHAIN
REMARK 500 4 TYR A 649 0.12 SIDE CHAIN
REMARK 500 4 TYR B 134 0.08 SIDE CHAIN
REMARK 500 4 ARG B 135 0.09 SIDE CHAIN
REMARK 500 5 PHE A 612 0.09 SIDE CHAIN
REMARK 500 5 TYR A 649 0.14 SIDE CHAIN
REMARK 500 5 TYR A 658 0.14 SIDE CHAIN
REMARK 500 5 ARG B 130 0.10 SIDE CHAIN
REMARK 500 5 ARG B 131 0.08 SIDE CHAIN
REMARK 500 6 PHE A 612 0.10 SIDE CHAIN
REMARK 500 6 TYR A 640 0.10 SIDE CHAIN
REMARK 500 6 TYR A 649 0.13 SIDE CHAIN
REMARK 500 6 TYR A 650 0.08 SIDE CHAIN
REMARK 500 6 TYR A 658 0.21 SIDE CHAIN
REMARK 500 7 TYR A 649 0.07 SIDE CHAIN
REMARK 500 7 TYR A 658 0.17 SIDE CHAIN
REMARK 500 7 TYR B 134 0.10 SIDE CHAIN
REMARK 500 8 ARG A 600 0.08 SIDE CHAIN
REMARK 500 8 TYR A 649 0.13 SIDE CHAIN
REMARK 500 8 TYR B 134 0.10 SIDE CHAIN
REMARK 500 9 TYR A 640 0.11 SIDE CHAIN
REMARK 500 9 TYR A 649 0.10 SIDE CHAIN
REMARK 500 9 TYR B 134 0.07 SIDE CHAIN
REMARK 500 10 PHE A 612 0.12 SIDE CHAIN
REMARK 500 10 TYR A 649 0.09 SIDE CHAIN
REMARK 500 11 PHE A 612 0.10 SIDE CHAIN
REMARK 500 11 TYR A 640 0.14 SIDE CHAIN
REMARK 500 11 TYR A 649 0.12 SIDE CHAIN
REMARK 500 11 ARG B 125 0.09 SIDE CHAIN
REMARK 500 11 TYR B 134 0.12 SIDE CHAIN
REMARK 500 12 ARG A 588 0.20 SIDE CHAIN
REMARK 500 12 PHE A 612 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 69 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KDX A 586 666 UNP P45481 CBP_MOUSE 586 666
DBREF 1KDX B 119 146 UNP P15337 CREB1_RAT 119 146
SEQADV 1KDX SEP B 133 UNP P15337 SER 133 ENGINEERED MUTATION
SEQRES 1 A 81 GLY VAL ARG LYS GLY TRP HIS GLU HIS VAL THR GLN ASP
SEQRES 2 A 81 LEU ARG SER HIS LEU VAL HIS LYS LEU VAL GLN ALA ILE
SEQRES 3 A 81 PHE PRO THR PRO ASP PRO ALA ALA LEU LYS ASP ARG ARG
SEQRES 4 A 81 MET GLU ASN LEU VAL ALA TYR ALA LYS LYS VAL GLU GLY
SEQRES 5 A 81 ASP MET TYR GLU SER ALA ASN SER ARG ASP GLU TYR TYR
SEQRES 6 A 81 HIS LEU LEU ALA GLU LYS ILE TYR LYS ILE GLN LYS GLU
SEQRES 7 A 81 LEU GLU GLU
SEQRES 1 B 28 THR ASP SER GLN LYS ARG ARG GLU ILE LEU SER ARG ARG
SEQRES 2 B 28 PRO SEP TYR ARG LYS ILE LEU ASN ASP LEU SER SER ASP
SEQRES 3 B 28 ALA PRO
MODRES 1KDX SEP B 133 SER PHOSPHOSERINE
HET SEP B 133 14
HETNAM SEP PHOSPHOSERINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 2 SEP C3 H8 N O6 P
HELIX 1 1 TRP A 591 HIS A 594 5 4
HELIX 2 2 GLN A 597 ILE A 611 1 15
HELIX 3 3 PRO A 617 LYS A 621 5 5
HELIX 4 4 ARG A 623 TYR A 640 1 18
HELIX 5 5 ARG A 646 LYS A 662 1 17
HELIX 6 6 ASP B 120 SER B 129 1 10
HELIX 7 7 PRO B 132 ASP B 144 1 13
LINK C PRO B 132 N SEP B 133 1555 1555 1.34
LINK C SEP B 133 N TYR B 134 1555 1555 1.34
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