HEADER TRANSFERASE 16-DEC-10 2L7P
TITLE ASHH2 A CW DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE ASHH2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CW-TYPE ZINC FINGER RESIDUES 849-937;
COMPND 5 SYNONYM: ASH1 HOMOLOG 2, H3-K4-HMTASE, HISTONE H3-K36
COMPND 6 METHYLTRANSFERASE 8, H3-K36-HMTASE 8, PROTEIN EARLY FLOWERING IN
COMPND 7 SHORT DAYS, PROTEIN SET DOMAIN GROUP 8;
COMPND 8 EC: 2.1.1.43;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: ASHH2, EFS, SDG8, SET8, AT1G77300, T14N5.15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PSXG
KEYWDS CW-DOMAIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.KRISTIANSEN,V.HOPPMANN,T.THORSTENSEN,R.B.AALEN,R.AASLAND,K.FINNE,
AUTHOR 2 S.VEISETH
REVDAT 3 01-MAY-24 2L7P 1 REMARK SEQADV LINK
REVDAT 2 08-JUN-11 2L7P 1 JRNL
REVDAT 1 11-MAY-11 2L7P 0
JRNL AUTH V.HOPPMANN,T.THORSTENSEN,P.E.KRISTIANSEN,S.V.VEISETH,
JRNL AUTH 2 M.A.RAHMAN,K.FINNE,R.B.AALEN,R.AASLAND
JRNL TITL THE CW DOMAIN, A NEW HISTONE RECOGNITION MODULE IN CHROMATIN
JRNL TITL 2 PROTEINS.
JRNL REF EMBO J. V. 30 1939 2011
JRNL REFN ISSN 0261-4189
JRNL PMID 21522130
JRNL DOI 10.1038/EMBOJ.2011.108
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1, CYANA 2.1
REMARK 3 AUTHORS : HERRMANN, GUNTERT AND WUTHRICH (CYANA), HERRMANN,
REMARK 3 GUNTERT AND WUTHRICH (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L7P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000102060.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM [U-98% 13C; U-98% 15N]
REMARK 210 PROTEIN, 10 UM ZINC ION, 0.2 MM
REMARK 210 DSS, 1.0 MM DTT, 20 MM POTASSIUM
REMARK 210 PHOSPHATE, 50 MM POTASSIUM
REMARK 210 CHLORIDE, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D HNCO; 3D HNCA;
REMARK 210 3D HNCACB; 3D HBHA(CO)NH; 3D
REMARK 210 HN(CO)CA; 3D H(CCO)NH; 3D HCCH-
REMARK 210 TOCSY; 3D HNHA; 3D HN(COCA)CB;
REMARK 210 3D HBHANH; 3D HN(CA)CO; 3D 1H-
REMARK 210 15N NOESY; 3D 1H-13C NOESY; 1D
REMARK 210 1H PROTON SPECTRUM WATER
REMARK 210 SUPPRESION WITH EXITATION
REMARK 210 SCULPTIN
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TALOS, SPARKY, TOPSPIN
REMARK 210 METHOD USED : TORSION ANGLE 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: 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 6 -179.54 -174.13
REMARK 500 1 VAL A 16 23.75 -145.90
REMARK 500 1 ASP A 20 23.21 -157.03
REMARK 500 1 SER A 21 80.68 -178.68
REMARK 500 1 SER A 23 -176.20 55.74
REMARK 500 1 THR A 24 -74.08 -98.91
REMARK 500 1 GLU A 25 -75.10 -87.64
REMARK 500 1 ASP A 32 35.19 -95.60
REMARK 500 1 ASP A 33 -43.18 -142.10
REMARK 500 1 PHE A 35 67.59 62.74
REMARK 500 1 SER A 47 -40.40 -135.01
REMARK 500 1 ASP A 61 -173.59 -67.52
REMARK 500 1 ALA A 65 68.17 -109.50
REMARK 500 1 ASP A 66 143.01 -176.80
REMARK 500 1 LYS A 69 -175.97 -65.78
REMARK 500 1 ASP A 87 85.91 57.57
REMARK 500 1 ALA A 89 -171.29 54.91
REMARK 500 1 ASP A 95 33.48 -169.17
REMARK 500 1 LYS A 98 -179.72 56.06
REMARK 500 1 ARG A 99 -71.43 -62.53
REMARK 500 2 SER A 2 -178.34 -170.93
REMARK 500 2 SER A 9 -34.68 -179.49
REMARK 500 2 GLU A 10 162.93 62.79
REMARK 500 2 PHE A 11 120.00 -160.88
REMARK 500 2 MET A 12 179.90 58.67
REMARK 500 2 ASP A 15 -170.89 -64.17
REMARK 500 2 SER A 21 103.82 -178.85
REMARK 500 2 SER A 23 -75.80 69.40
REMARK 500 2 THR A 24 -74.16 -177.79
REMARK 500 2 GLU A 25 -75.33 -92.18
REMARK 500 2 ASP A 32 35.40 -97.59
REMARK 500 2 ASP A 33 -42.54 -142.81
REMARK 500 2 PHE A 35 72.46 62.03
REMARK 500 2 SER A 47 -41.07 -135.71
REMARK 500 2 ASP A 61 -169.79 -70.36
REMARK 500 2 LYS A 62 -53.25 -131.11
REMARK 500 2 ALA A 65 69.07 -109.15
REMARK 500 2 ASP A 66 143.25 -176.36
REMARK 500 2 ASP A 87 80.20 57.58
REMARK 500 2 ALA A 89 171.89 63.91
REMARK 500 2 LYS A 98 47.25 -143.39
REMARK 500 3 VAL A 13 -178.71 -62.93
REMARK 500 3 VAL A 16 23.80 -154.59
REMARK 500 3 GLU A 19 113.70 -174.33
REMARK 500 3 TYR A 22 -172.23 57.63
REMARK 500 3 THR A 24 -52.54 -146.27
REMARK 500 3 GLU A 25 -41.05 -139.22
REMARK 500 3 ASP A 32 34.84 -98.99
REMARK 500 3 ASP A 33 -42.46 -142.45
REMARK 500 3 PHE A 35 70.21 60.92
REMARK 500
REMARK 500 THIS ENTRY HAS 406 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 31 SG
REMARK 620 2 CYS A 34 SG 104.2
REMARK 620 3 CYS A 56 SG 105.0 110.8
REMARK 620 4 CYS A 67 SG 104.7 114.2 116.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17365 RELATED DB: BMRB
DBREF 2L7P A 12 100 UNP Q2LAE1 ASHH2_ARATH 849 937
SEQADV 2L7P GLY A 1 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P SER A 2 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P ARG A 3 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P ARG A 4 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P ALA A 5 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P SER A 6 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P VAL A 7 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P GLY A 8 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P SER A 9 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P GLU A 10 UNP Q2LAE1 EXPRESSION TAG
SEQADV 2L7P PHE A 11 UNP Q2LAE1 EXPRESSION TAG
SEQRES 1 A 100 GLY SER ARG ARG ALA SER VAL GLY SER GLU PHE MET VAL
SEQRES 2 A 100 VAL ASP VAL THR ILE GLU ASP SER TYR SER THR GLU SER
SEQRES 3 A 100 ALA TRP VAL ARG CYS ASP ASP CYS PHE LYS TRP ARG ARG
SEQRES 4 A 100 ILE PRO ALA SER VAL VAL GLY SER ILE ASP GLU SER SER
SEQRES 5 A 100 ARG TRP ILE CYS MET ASN ASN SER ASP LYS ARG PHE ALA
SEQRES 6 A 100 ASP CYS SER LYS SER GLN GLU MET SER ASN GLU GLU ILE
SEQRES 7 A 100 ASN GLU GLU LEU GLY ILE GLY GLN ASP GLU ALA ASP ALA
SEQRES 8 A 100 TYR ASP CYS ASP ALA ALA LYS ARG GLY
HET ZN A 201 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 PRO A 41 GLY A 46 1 6
HELIX 2 2 ILE A 55 ASN A 59 5 5
HELIX 3 3 SER A 74 GLY A 83 1 10
SHEET 1 A 2 ALA A 27 ARG A 30 0
SHEET 2 A 2 TRP A 37 ILE A 40 -1 O ILE A 40 N ALA A 27
LINK SG CYS A 31 ZN ZN A 201 1555 1555 2.35
LINK SG CYS A 34 ZN ZN A 201 1555 1555 2.31
LINK SG CYS A 56 ZN ZN A 201 1555 1555 2.26
LINK SG CYS A 67 ZN ZN A 201 1555 1555 2.27
SITE 1 AC1 4 CYS A 31 CYS A 34 CYS A 56 CYS A 67
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