HEADER TRANSCRIPTION REGULATOR 22-JUL-10 2L12
TITLE SOLUTION NMR STRUCTURE OF THE CHROMOBOX PROTEIN 7 WITH H3K9ME3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHROMOBOX HOMOLOG 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 7-62;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H3;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 2-16;
COMPND 10 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: CBX7, RP4-742C19.7-003;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 13 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 14 ORGANISM_TAXID: 8355;
SOURCE 15 OTHER_DETAILS: H3K9ME3 15-MER PEPTIDE
KEYWDS CHROMODOMAIN, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 2 SGC, TRANSCRIPTION REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.KAUSTOV,A.LEMAK,A.GUTMANAS,C.FARES,H.QUANG,P.LOPPNAU,J.MIN,
AUTHOR 2 A.EDWARDS,C.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 05-FEB-20 2L12 1 REMARK LINK
REVDAT 2 06-APR-11 2L12 1 JRNL
REVDAT 1 04-AUG-10 2L12 0
JRNL AUTH L.KAUSTOV,H.OUYANG,M.AMAYA,A.LEMAK,N.NADY,S.DUAN,G.A.WASNEY,
JRNL AUTH 2 Z.LI,M.VEDADI,M.SCHAPIRA,J.MIN,C.H.ARROWSMITH
JRNL TITL RECOGNITION AND SPECIFICITY DETERMINANTS OF THE HUMAN CBX
JRNL TITL 2 CHROMODOMAINS.
JRNL REF J.BIOL.CHEM. V. 286 521 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21047797
JRNL DOI 10.1074/JBC.M110.191411
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ABACUS, CNS
REMARK 3 AUTHORS : (ABACUS)-GRISHAEV (ABACUS), BRUNGER, ADAMS, CLORE,
REMARK 3 GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000101822.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 300
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM SODIUM PHOSPHATE, 300 MM
REMARK 210 SODIUM CHLORIDE, 1 MM TCEP, 1 MM
REMARK 210 BENZAMIDINE, 0.5 MM PMSF, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCO; 3D HNCA; 3D CBCA(CO)NH;
REMARK 210 3D HBHA(CO)NH; 3D HCCH-TOCSY; 3D
REMARK 210 1H-15N NOESY; 3D 1H-13C NOESY;
REMARK 210 13C/15N-FILTERED/EDITED NOESY;
REMARK 210 3D ARO 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRPIPE, SPARKY
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 GLU A 8 -79.99 -82.08
REMARK 500 2 GLU A 8 -74.01 -83.22
REMARK 500 2 THR B 3 104.81 64.38
REMARK 500 2 LYS B 4 81.55 -160.08
REMARK 500 2 SER B 10 89.95 -63.71
REMARK 500 3 GLU A 8 -62.33 -94.19
REMARK 500 3 SER B 10 84.56 -66.87
REMARK 500 4 LEU A 23 81.64 -66.61
REMARK 500 4 GLN B 5 98.01 -64.30
REMARK 500 5 SER B 10 95.19 -59.05
REMARK 500 6 LEU A 23 88.18 -67.25
REMARK 500 7 GLU A 55 -15.69 80.38
REMARK 500 7 LYS B 4 82.88 -69.48
REMARK 500 8 LYS B 4 78.45 55.05
REMARK 500 9 GLU A 8 -65.64 -91.23
REMARK 500 9 LEU A 23 89.44 -68.87
REMARK 500 9 THR B 3 89.28 -67.10
REMARK 500 9 SER B 10 87.97 -68.88
REMARK 500 10 LYS B 4 72.10 -118.88
REMARK 500 11 LEU A 23 86.91 -69.20
REMARK 500 11 THR B 3 79.29 -106.98
REMARK 500 11 GLN B 5 69.55 61.49
REMARK 500 12 GLU A 2 90.66 -66.57
REMARK 500 12 SER A 9 -178.65 -174.95
REMARK 500 12 LYS A 27 -91.15 52.56
REMARK 500 12 GLU A 39 -33.08 -38.37
REMARK 500 12 GLU A 53 52.66 -105.22
REMARK 500 12 SER B 10 101.90 -54.14
REMARK 500 13 SER B 10 -168.78 -173.82
REMARK 500 14 SER A 9 -162.34 -164.64
REMARK 500 14 LEU A 23 87.73 -66.15
REMARK 500 14 LYS B 4 -155.05 -135.51
REMARK 500 15 GLU A 8 -72.38 -73.62
REMARK 500 15 PRO A 31 -8.82 -59.17
REMARK 500 15 GLU A 53 63.19 61.01
REMARK 500 15 THR B 3 93.57 -62.40
REMARK 500 15 SER B 10 100.95 -58.52
REMARK 500 15 THR B 11 95.02 -62.73
REMARK 500 16 GLU A 8 -78.50 -81.95
REMARK 500 16 LEU A 23 84.51 -65.96
REMARK 500 16 ARG B 2 17.54 59.92
REMARK 500 16 SER B 10 82.39 -68.71
REMARK 500 17 GLU A 39 -19.89 -49.89
REMARK 500 17 GLN B 5 97.09 -62.43
REMARK 500 17 SER B 10 89.95 -60.76
REMARK 500 18 GLU A 2 98.92 65.94
REMARK 500 18 SER A 9 -167.79 -164.99
REMARK 500 18 PRO A 31 0.44 -65.00
REMARK 500 18 PRO A 38 172.35 -53.63
REMARK 500 18 ARG B 2 39.34 37.98
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17072 RELATED DB: BMRB
DBREF 2L12 A 1 56 UNP B0QYP2 B0QYP2_HUMAN 7 62
DBREF 2L12 B 1 15 UNP Q92133 Q92133_XENLA 2 16
SEQRES 1 A 56 GLY GLU GLN VAL PHE ALA VAL GLU SER ILE ARG LYS LYS
SEQRES 2 A 56 ARG VAL ARG LYS GLY LYS VAL GLU TYR LEU VAL LYS TRP
SEQRES 3 A 56 LYS GLY TRP PRO PRO LYS TYR SER THR TRP GLU PRO GLU
SEQRES 4 A 56 GLU HIS ILE LEU ASP PRO ARG LEU VAL MET ALA TYR GLU
SEQRES 5 A 56 GLU LYS GLU GLU
SEQRES 1 B 15 ALA ARG THR LYS GLN THR ALA ARG M3L SER THR GLY GLY
SEQRES 2 B 15 LYS ALA
MODRES 2L12 M3L B 9 LYS N-TRIMETHYLLYSINE
HET M3L B 9 31
HETNAM M3L N-TRIMETHYLLYSINE
FORMUL 2 M3L C9 H21 N2 O2 1+
HELIX 1 1 PRO A 30 SER A 34 5 5
HELIX 2 2 ASP A 44 GLU A 52 1 9
SHEET 1 A 4 THR A 35 PRO A 38 0
SHEET 2 A 4 LYS A 19 TRP A 26 -1 N TYR A 22 O GLU A 37
SHEET 3 A 4 VAL A 4 ARG A 16 -1 N GLU A 8 O LYS A 25
SHEET 4 A 4 THR B 6 ARG B 8 -1 O ALA B 7 N PHE A 5
LINK C ARG B 8 N M3L B 9 1555 1555 1.34
LINK C M3L B 9 N SER B 10 1555 1555 1.35
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
