HEADER DNA BINDING PROTEIN 24-APR-06 2DMQ
TITLE SOLUTION STRUCTURE OF THE HOMEOBOX DOMAIN OF LIM/HOMEOBOX
TITLE 2 PROTEIN LHX9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIM/HOMEOBOX PROTEIN LHX9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HOMEOBOX DOMAIN;
COMPND 5 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: LHX9;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050613-31;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS HOMEOBOX DOMAIN, THREE HELICES WITH THE DNA BINDING HELIX-
KEYWDS 2 TURN-HELIX MOTIF, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA
KEYWDS 5 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.OHNISHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2DMQ 1 VERSN
REVDAT 1 24-OCT-06 2DMQ 0
JRNL AUTH S.OHNISHI,N.TOCHIO,S.KOSHIBA,M.INOUE,T.KIGAWA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE HOMEOBOX DOMAIN OF
JRNL TITL 2 LIM/HOMEOBOX PROTEIN LHX9
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DMQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-APR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025597.
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 : 1.2MM PROTEIN U-15N,13C; 20MM
REMARK 210 D-TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE
REMARK 210 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.965, CYANA 2.0.17
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 : TARGET FUNCTION, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 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 3 41.66 -87.30
REMARK 500 1 LEU A 46 -176.71 -64.03
REMARK 500 1 GLU A 70 131.48 -39.79
REMARK 500 1 SER A 78 121.78 -36.66
REMARK 500 1 SER A 79 113.27 -38.92
REMARK 500 2 PRO A 77 -177.04 -69.84
REMARK 500 2 SER A 78 52.77 39.54
REMARK 500 3 SER A 3 -60.82 -106.61
REMARK 500 3 ARG A 49 -70.46 -47.32
REMARK 500 3 GLN A 69 47.96 37.87
REMARK 500 4 SER A 13 157.23 -43.75
REMARK 500 4 ALA A 41 -29.60 -38.35
REMARK 500 4 LEU A 46 172.75 -56.15
REMARK 500 4 GLN A 69 41.49 -91.04
REMARK 500 5 ARG A 11 140.16 -35.71
REMARK 500 5 LEU A 46 -176.05 -64.03
REMARK 500 5 GLN A 69 109.91 -53.73
REMARK 500 5 SER A 75 130.25 -173.82
REMARK 500 5 SER A 79 118.71 -163.73
REMARK 500 6 GLN A 69 38.10 -98.74
REMARK 500 6 SER A 75 149.75 -34.61
REMARK 500 6 SER A 79 107.25 -46.89
REMARK 500 7 LYS A 8 -48.60 -130.36
REMARK 500 7 GLN A 69 109.22 -42.88
REMARK 500 8 SER A 6 124.17 -36.89
REMARK 500 8 ALA A 41 -30.13 -38.16
REMARK 500 8 GLN A 69 39.47 -89.46
REMARK 500 9 LYS A 8 -45.33 -131.66
REMARK 500 9 ARG A 68 42.68 34.21
REMARK 500 9 GLU A 70 81.61 -68.15
REMARK 500 10 SER A 6 50.23 -92.49
REMARK 500 10 THR A 12 72.47 -66.21
REMARK 500 11 SER A 5 126.55 -174.98
REMARK 500 11 LEU A 46 -179.71 -63.39
REMARK 500 11 VAL A 74 142.49 -172.08
REMARK 500 12 SER A 3 107.68 -54.74
REMARK 500 12 SER A 5 142.45 -172.01
REMARK 500 12 LYS A 8 146.05 -37.25
REMARK 500 12 ASN A 31 70.96 -117.86
REMARK 500 12 SER A 78 -58.09 -120.18
REMARK 500 13 ARG A 20 -34.45 -40.00
REMARK 500 13 GLN A 69 98.02 -64.90
REMARK 500 13 ASN A 71 50.03 37.37
REMARK 500 14 ASN A 71 151.09 -46.64
REMARK 500 14 VAL A 74 128.71 -174.73
REMARK 500 15 GLN A 69 50.98 70.34
REMARK 500 16 GLN A 69 102.21 -39.18
REMARK 500 17 ARG A 9 45.07 39.10
REMARK 500 17 GLU A 70 45.42 -95.73
REMARK 500 17 VAL A 74 35.60 34.24
REMARK 500 18 SER A 3 42.46 70.92
REMARK 500 18 ARG A 68 143.30 -38.57
REMARK 500 18 GLU A 70 26.74 48.96
REMARK 500 18 ASN A 71 115.37 -35.40
REMARK 500 18 VAL A 74 144.95 -34.99
REMARK 500 19 SER A 2 42.23 -108.03
REMARK 500 19 SER A 5 176.25 -49.01
REMARK 500 19 MET A 10 131.38 -174.07
REMARK 500 19 THR A 12 146.24 -173.59
REMARK 500 19 SER A 13 178.06 -54.12
REMARK 500 19 ARG A 68 143.83 -39.14
REMARK 500 20 PRO A 77 97.76 -69.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002002111.1 RELATED DB: TARGETDB
DBREF 2DMQ A 8 74 UNP Q9NQ69 LHX9_HUMAN 259 325
SEQADV 2DMQ GLY A 1 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 2 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 3 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ GLY A 4 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 5 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 6 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ GLY A 7 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 75 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ GLY A 76 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ PRO A 77 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 78 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ SER A 79 UNP Q9NQ69 CLONING ARTIFACT
SEQADV 2DMQ GLY A 80 UNP Q9NQ69 CLONING ARTIFACT
SEQRES 1 A 80 GLY SER SER GLY SER SER GLY LYS ARG MET ARG THR SER
SEQRES 2 A 80 PHE LYS HIS HIS GLN LEU ARG THR MET LYS SER TYR PHE
SEQRES 3 A 80 ALA ILE ASN HIS ASN PRO ASP ALA LYS ASP LEU LYS GLN
SEQRES 4 A 80 LEU ALA GLN LYS THR GLY LEU THR LYS ARG VAL LEU GLN
SEQRES 5 A 80 VAL TRP PHE GLN ASN ALA ARG ALA LYS PHE ARG ARG ASN
SEQRES 6 A 80 LEU LEU ARG GLN GLU ASN GLY GLY VAL SER GLY PRO SER
SEQRES 7 A 80 SER GLY
HELIX 1 1 LYS A 15 ASN A 29 1 15
HELIX 2 2 ASP A 33 THR A 44 1 12
HELIX 3 3 THR A 47 ARG A 68 1 22
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