HEADER GENE REGULATION 05-MAR-08 2K1J
TITLE PLAN HOMEODOMAIN FINGER OF TUMOUR SUPRESSOR ING4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INHIBITOR OF GROWTH PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PHD-TYPE ZINC-FINGER, UNP RESIDUES 188-249;
COMPND 5 SYNONYM: P29ING4;
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: ING4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET11D
KEYWDS PHD, ZN, GENE REGULATION, ACETYLATION, ALTERNATIVE SPLICING, ANTI-
KEYWDS 2 ONCOGENE, CELL CYCLE, COILED COIL, METAL-BINDING, NUCLEUS, ZINC,
KEYWDS 3 ZINC-FINGER
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR A.PALACIOS,P.GARCIA,D.PADRO,E.LOPEZ-HERNANDEZ,F.J.BLANCO
REVDAT 3 16-MAR-22 2K1J 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2K1J 1 VERSN
REVDAT 1 15-APR-08 2K1J 0
SPRSDE 15-APR-08 2K1J 2JMQ
JRNL AUTH A.PALACIOS,P.GARCIA,D.PADRO,E.LOPEZ-HERNANDEZ,I.MARTIN,
JRNL AUTH 2 F.J.BLANCO
JRNL TITL SOLUTION STRUCTURE AND NMR CHARACTERIZATION OF THE BINDING
JRNL TITL 2 TO METHYLATED HISTONE TAILS OF THE PLANT HOMEODOMAIN FINGER
JRNL TITL 3 OF THE TUMOUR SUPPRESSOR ING4.
JRNL REF FEBS LETT. V. 580 6903 2006
JRNL REFN ISSN 0014-5793
JRNL PMID 17157298
JRNL DOI 10.1016/J.FEBSLET.2006.11.055
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA, AMBER 7.0
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA), CASE,
REMARK 3 DARDEN, CHEATHAM III, SIMMERLING, WANG, DUKE, LUO,
REMARK 3 AND KOLL (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2K1J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000100558.
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 : 1.2 MM [U-95% 13C; U-90% 15N]
REMARK 210 PLANT HOMEODOMAIN OF ING4, 95%
REMARK 210 H2O, 5% D2O; 1.2 MM [U-95% 13C;
REMARK 210 U-90% 15N] PLANT HOMEODOMAIN OF
REMARK 210 ING4, 100% D2O; 0.9 MM [U-90%
REMARK 210 15N] PLANT HOMEODOMAIN OF ING4,
REMARK 210 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 HNCACB; 3D
REMARK 210 H(CCO)NH; 3D HNHA; 3D HNHB; 3D
REMARK 210 1H-15N NOESY; 3D 1H-15N TOCSY;
REMARK 210 3D 1H-13C NOESY; 3D HCCH-TOCSY;
REMARK 210 3D HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, XWINNMR, NMRPIPE,
REMARK 210 NMRDRAW
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 250
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 ASP A 188 -164.03 56.38
REMARK 500 1 TYR A 198 -81.97 -133.56
REMARK 500 1 SER A 205 153.48 -49.04
REMARK 500 1 GLU A 220 -15.70 51.60
REMARK 500 1 SER A 243 -35.18 -152.94
REMARK 500 1 LYS A 247 37.31 -140.36
REMARK 500 2 VAL A 191 148.61 53.43
REMARK 500 2 TYR A 198 -67.34 -136.30
REMARK 500 2 HIS A 202 54.69 71.10
REMARK 500 2 SER A 205 156.71 -47.81
REMARK 500 2 GLU A 220 -10.18 49.80
REMARK 500 2 LYS A 236 108.92 -57.21
REMARK 500 2 CYS A 239 171.87 -58.46
REMARK 500 2 SER A 243 -39.59 -152.79
REMARK 500 2 LYS A 248 80.92 38.79
REMARK 500 3 ASP A 188 46.84 -156.55
REMARK 500 3 TYR A 198 -80.93 -137.51
REMARK 500 3 VAL A 204 -178.89 -67.92
REMARK 500 3 ASP A 216 -10.43 -144.58
REMARK 500 3 GLU A 220 -9.77 46.95
REMARK 500 3 SER A 243 -32.51 -150.24
REMARK 500 3 LYS A 247 56.35 -146.06
REMARK 500 4 MET A 189 -50.33 -156.40
REMARK 500 4 TYR A 198 -55.13 -137.83
REMARK 500 4 HIS A 202 52.01 71.37
REMARK 500 4 SER A 205 155.12 -47.57
REMARK 500 4 GLU A 220 -12.61 50.07
REMARK 500 4 SER A 243 -38.67 -151.17
REMARK 500 5 ASP A 188 -107.52 -140.10
REMARK 500 5 MET A 189 59.51 -140.73
REMARK 500 5 TYR A 198 -81.20 -135.19
REMARK 500 5 SER A 205 151.69 -46.83
REMARK 500 5 GLU A 220 -16.27 50.83
REMARK 500 5 SER A 243 -34.82 -149.17
REMARK 500 6 PRO A 190 45.39 -80.65
REMARK 500 6 TYR A 198 -81.18 -136.38
REMARK 500 6 LEU A 200 -9.72 -59.52
REMARK 500 6 VAL A 204 -179.62 -69.20
REMARK 500 6 SER A 205 150.16 -45.67
REMARK 500 6 GLU A 220 -15.70 50.14
REMARK 500 6 SER A 243 -34.07 -153.71
REMARK 500 6 LYS A 248 72.62 43.78
REMARK 500 7 MET A 189 -49.40 -146.00
REMARK 500 7 TYR A 198 -67.29 -139.46
REMARK 500 7 HIS A 202 52.20 72.45
REMARK 500 7 SER A 205 157.44 -47.94
REMARK 500 7 GLU A 220 -7.75 48.36
REMARK 500 7 CYS A 239 172.51 -59.25
REMARK 500 7 SER A 243 -39.59 -157.08
REMARK 500 7 LYS A 248 50.42 -150.80
REMARK 500
REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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 250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 251
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7210 RELATED DB: BMRB
DBREF 2K1J A 188 249 UNP Q9UNL4 ING4_HUMAN 188 249
SEQADV 2K1J MET A 187 UNP Q9UNL4 INITIATING METHIONINE
SEQRES 1 A 63 MET ASP MET PRO VAL ASP PRO ASN GLU PRO THR TYR CYS
SEQRES 2 A 63 LEU CYS HIS GLN VAL SER TYR GLY GLU MET ILE GLY CYS
SEQRES 3 A 63 ASP ASN PRO ASP CYS SER ILE GLU TRP PHE HIS PHE ALA
SEQRES 4 A 63 CYS VAL GLY LEU THR THR LYS PRO ARG GLY LYS TRP PHE
SEQRES 5 A 63 CYS PRO ARG CYS SER GLN GLU ARG LYS LYS LYS
HET ZN A 250 1
HET ZN A 251 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
SHEET 1 A 2 MET A 209 ILE A 210 0
SHEET 2 A 2 PHE A 222 HIS A 223 -1 O PHE A 222 N ILE A 210
SITE 1 AC1 4 TYR A 198 CYS A 199 GLN A 203 HIS A 223
SITE 1 AC2 5 GLY A 211 CYS A 212 ASN A 214 PHE A 222
SITE 2 AC2 5 CYS A 239
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
