HEADER PROTEIN BINDING 27-APR-06 2DO7
TITLE SOLUTION STRUCTURE OF THE WINGED HELIX-TURN-HELIX MOTIF OF HUMAN CUL-
TITLE 2 4B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CULLIN-4B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: WINGED HELIX-TURN-HELIX MOTIF;
COMPND 5 SYNONYM: CUL-4B;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CUL4B, KIAA0695;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050822-14;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS HELIX-TURN-HELIX MOTIF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DO7 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DO7 1 VERSN
REVDAT 1 17-APR-07 2DO7 0
JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE WINGED HELIX-TURN-HELIX MOTIF OF
JRNL TITL 2 HUMAN CUL-4B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DO7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000025645.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM 13C/15N-PROTEIN, 20MM D
REMARK 210 -TRIS-HCL(PH7.0), 100MM NACL,
REMARK 210 1MM D-DTT, 0.02% NAN3, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, OLIVIA 1.10.5,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 SER A 805 43.43 39.25
REMARK 500 1 MET A 810 116.29 -172.40
REMARK 500 1 GLU A 812 125.04 -172.34
REMARK 500 1 SER A 819 164.52 -42.67
REMARK 500 1 ILE A 832 -71.57 -73.42
REMARK 500 1 LYS A 885 -38.58 -38.75
REMARK 500 1 PRO A 888 1.45 -69.74
REMARK 500 1 ALA A 895 140.99 -34.12
REMARK 500 2 GLN A 817 107.26 -163.58
REMARK 500 2 THR A 821 131.57 -37.59
REMARK 500 2 ARG A 828 -71.10 -47.53
REMARK 500 3 SER A 805 116.92 -166.95
REMARK 500 3 THR A 820 91.73 -65.74
REMARK 500 3 GLU A 822 -34.44 -34.18
REMARK 500 3 ASP A 827 -37.64 -36.14
REMARK 500 3 ARG A 828 -73.89 -68.79
REMARK 500 3 GLN A 829 -33.44 -39.63
REMARK 500 3 LYS A 864 152.81 -38.34
REMARK 500 3 PRO A 888 1.12 -69.84
REMARK 500 3 ALA A 895 140.70 -34.13
REMARK 500 4 ASP A 827 -33.09 -38.33
REMARK 500 4 ARG A 828 -70.52 -70.48
REMARK 500 4 GLN A 829 -32.79 -38.58
REMARK 500 4 LYS A 864 153.35 -48.48
REMARK 500 4 SER A 899 112.32 -168.08
REMARK 500 4 SER A 900 105.32 -59.01
REMARK 500 5 SER A 802 113.53 -170.77
REMARK 500 5 GLU A 812 152.95 -38.86
REMARK 500 5 ARG A 828 -70.69 -72.15
REMARK 500 5 ILE A 832 -72.84 -69.90
REMARK 500 5 ARG A 878 32.01 -88.33
REMARK 500 5 ALA A 895 143.57 -35.45
REMARK 500 5 PRO A 898 86.33 -69.72
REMARK 500 6 LYS A 811 97.77 -55.36
REMARK 500 6 GLU A 815 135.49 -36.78
REMARK 500 6 ASP A 827 -35.70 -34.45
REMARK 500 6 ARG A 828 -70.39 -65.76
REMARK 500 6 ALA A 895 148.14 -35.06
REMARK 500 7 GLN A 809 134.88 -172.65
REMARK 500 7 GLU A 812 162.16 -41.84
REMARK 500 7 THR A 820 103.32 -38.12
REMARK 500 7 ARG A 823 -33.12 -39.12
REMARK 500 7 ARG A 828 -72.96 -62.56
REMARK 500 7 LYS A 844 -32.89 -39.76
REMARK 500 7 LEU A 851 -70.11 -51.45
REMARK 500 7 ALA A 895 132.59 -36.80
REMARK 500 7 PRO A 898 1.90 -69.75
REMARK 500 7 SER A 899 103.22 -41.29
REMARK 500 8 THR A 820 88.59 -56.30
REMARK 500 8 ASP A 827 -33.36 -35.32
REMARK 500
REMARK 500 THIS ENTRY HAS 125 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2DO7 A 808 895 UNP Q13620 CUL4B_HUMAN 808 895
SEQADV 2DO7 GLY A 801 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 802 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 803 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 GLY A 804 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 805 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 806 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 GLY A 807 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 896 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 GLY A 897 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 PRO A 898 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 899 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 SER A 900 UNP Q13620 CLONING ARTIFACT
SEQADV 2DO7 GLY A 901 UNP Q13620 CLONING ARTIFACT
SEQRES 1 A 101 GLY SER SER GLY SER SER GLY ILE GLN MET LYS GLU THR
SEQRES 2 A 101 VAL GLU GLU GLN ALA SER THR THR GLU ARG VAL PHE GLN
SEQRES 3 A 101 ASP ARG GLN TYR GLN ILE ASP ALA ALA ILE VAL ARG ILE
SEQRES 4 A 101 MET LYS MET ARG LYS THR LEU SER HIS ASN LEU LEU VAL
SEQRES 5 A 101 SER GLU VAL TYR ASN GLN LEU LYS PHE PRO VAL LYS PRO
SEQRES 6 A 101 ALA ASP LEU LYS LYS ARG ILE GLU SER LEU ILE ASP ARG
SEQRES 7 A 101 ASP TYR MET GLU ARG ASP LYS GLU ASN PRO ASN GLN TYR
SEQRES 8 A 101 ASN TYR ILE ALA SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 822 ARG A 843 1 22
HELIX 2 2 HIS A 848 LEU A 859 1 12
HELIX 3 3 LYS A 864 ARG A 878 1 15
SHEET 1 A 3 THR A 845 SER A 847 0
SHEET 2 A 3 GLN A 890 TYR A 893 -1 O TYR A 891 N LEU A 846
SHEET 3 A 3 MET A 881 ARG A 883 -1 N GLU A 882 O ASN A 892
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
(ATOM LINES ARE NOT SHOWN.)
END
