HEADER TRANSCRIPTION 24-APR-06 2DN0
TITLE SOLUTION STRUCTURE OF THE SECOND HOMEOBOX DOMAIN OF HUMAN ZINC FINGERS
TITLE 2 AND HOMEOBOXES PROTEIN 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGERS AND HOMEOBOXES PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HOMEOBOX;
COMPND 5 SYNONYM: TRIPLE HOMEOBOX 1 PROTEIN;
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: ZHX3;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050404-22;
SOURCE 9 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS TRIPLE HOMEOBOX 1 PROTEIN, KIAA0395, TIX1, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.SEIMIYA,C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DN0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DN0 1 VERSN
REVDAT 1 24-OCT-06 2DN0 0
JRNL AUTH K.SEIMIYA,C.KUROSAKI,F.HAYASHI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND HOMEOBOX DOMAIN OF HUMAN
JRNL TITL 2 ZINC FINGERS AND HOMEOBOXES PROTEIN 3
JRNL REF TO BE PUBLISHED
JRNL REFN
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 2DN0 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 DEPOSITION ID IS D_1000025606.
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 : 1.04MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : ECA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DELTA NMR 4.3.2, NMRPIPE
REMARK 210 20031121, NMRVIEW 5.0.4, KUJIRA
REMARK 210 0.9742, CYANA 2.0.17
REMARK 210 METHOD USED : NULL
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: 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 5 170.07 -56.44
REMARK 500 1 LEU A 47 150.27 -49.46
REMARK 500 1 LEU A 66 66.20 -104.80
REMARK 500 1 PRO A 73 94.28 -69.79
REMARK 500 2 ARG A 29 -63.10 -106.28
REMARK 500 2 THR A 42 -31.01 -35.93
REMARK 500 2 LYS A 67 175.46 -56.43
REMARK 500 3 SER A 3 154.77 -43.08
REMARK 500 3 SER A 9 153.60 -47.33
REMARK 500 3 LYS A 12 87.77 -63.93
REMARK 500 3 GLU A 39 -39.43 -39.37
REMARK 500 3 SER A 74 91.11 -64.46
REMARK 500 4 SER A 16 29.01 48.67
REMARK 500 4 ARG A 29 -74.02 -52.14
REMARK 500 4 GLU A 37 -70.96 -58.81
REMARK 500 4 THR A 42 -36.68 -37.68
REMARK 500 4 ASN A 65 51.54 35.33
REMARK 500 5 SER A 2 42.21 -82.00
REMARK 500 5 LYS A 12 40.83 -93.23
REMARK 500 5 ASN A 13 41.44 -87.89
REMARK 500 5 PRO A 33 -174.52 -69.74
REMARK 500 6 LYS A 14 111.69 -35.46
REMARK 500 6 GLU A 18 -37.86 -35.96
REMARK 500 6 PHE A 27 -37.48 -34.79
REMARK 500 6 ARG A 29 -74.18 -49.06
REMARK 500 6 CYS A 63 58.32 -114.01
REMARK 500 6 SER A 71 75.87 -66.63
REMARK 500 6 SER A 74 93.79 -56.07
REMARK 500 7 ILE A 10 45.88 -99.95
REMARK 500 7 PRO A 33 -177.36 -69.70
REMARK 500 7 THR A 42 -31.88 -37.03
REMARK 500 8 SER A 2 42.15 35.27
REMARK 500 8 SER A 9 34.90 -84.22
REMARK 500 8 TYR A 11 39.66 -86.62
REMARK 500 8 CYS A 28 -71.69 -65.84
REMARK 500 8 THR A 42 -34.06 -34.11
REMARK 500 8 THR A 49 -38.92 -39.56
REMARK 500 8 PRO A 73 94.45 -69.71
REMARK 500 9 SER A 9 141.63 -36.19
REMARK 500 9 GLU A 18 -39.60 -35.34
REMARK 500 9 THR A 42 -33.31 -39.22
REMARK 500 9 SER A 75 126.52 -39.11
REMARK 500 10 ALA A 8 -62.26 -108.36
REMARK 500 10 PRO A 33 -174.28 -69.73
REMARK 500 11 ASN A 13 43.07 35.56
REMARK 500 11 LYS A 15 146.07 -173.24
REMARK 500 11 THR A 42 -31.54 -36.46
REMARK 500 12 ALA A 8 43.55 -86.51
REMARK 500 12 ASN A 13 50.84 -92.37
REMARK 500 12 GLN A 35 -46.36 -131.64
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100384.2 RELATED DB: TARGETDB
DBREF 2DN0 A 8 70 UNP Q9H4I2 ZHX3_HUMAN 494 556
SEQADV 2DN0 GLY A 1 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 2 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 3 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 GLY A 4 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 5 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 6 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 GLY A 7 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 71 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 GLY A 72 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 PRO A 73 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 74 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 SER A 75 UNP Q9H4I2 CLONING ARTIFACT
SEQADV 2DN0 GLY A 76 UNP Q9H4I2 CLONING ARTIFACT
SEQRES 1 A 76 GLY SER SER GLY SER SER GLY ALA SER ILE TYR LYS ASN
SEQRES 2 A 76 LYS LYS SER HIS GLU GLN LEU SER ALA LEU LYS GLY SER
SEQRES 3 A 76 PHE CYS ARG ASN GLN PHE PRO GLY GLN SER GLU VAL GLU
SEQRES 4 A 76 HIS LEU THR LYS VAL THR GLY LEU SER THR ARG GLU VAL
SEQRES 5 A 76 ARG LYS TRP PHE SER ASP ARG ARG TYR HIS CYS ARG ASN
SEQRES 6 A 76 LEU LYS GLY SER ARG SER GLY PRO SER SER GLY
HELIX 1 1 SER A 16 ASN A 30 1 15
HELIX 2 2 GLN A 35 GLY A 46 1 12
HELIX 3 3 SER A 48 CYS A 63 1 16
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
