HEADER TRANSCRIPTION 06-APR-07 2YUM
TITLE SOLUTION STRUCTURE OF THE MYB-LIKE DNA-BINDING DOMAIN OF
TITLE 2 HUMAN ZZZ3 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER ZZ-TYPE-CONTAINING PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MYB-LIKE DNA-BINDING DOMAIN, UNP RESIDUES 652-
COMPND 5 713;
COMPND 6 SYNONYM: ZZZ3 PROTEIN;
COMPND 7 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: ZZZ3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050613-19;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TRANSCRIPTION, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.ABE,N.TOCHIO,K.MIYAMOTO,K.SAITO,S.KOSHIBA,M.INOUE,
AUTHOR 2 T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 3 INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2YUM 1 VERSN
REVDAT 1 09-OCT-07 2YUM 0
JRNL AUTH H.ABE,N.TOCHIO,K.MIYAMOTO,K.SAITO,S.KOSHIBA,
JRNL AUTH 2 M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE MYB-LIKE DNA-BINDING
JRNL TITL 2 DOMAIN OF HUMAN ZZZ3 PROTEIN
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 2YUM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-07.
REMARK 100 THE RCSB ID CODE IS RCSB027154.
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 : 1.14MM PROTEIN; 20MM D-TRIS-
REMARK 210 HCL; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 90% 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 20031121, NMNMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9747, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, TARGET
REMARK 210 FUNCTION
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 TRP A 11 172.44 -49.03
REMARK 500 1 LYS A 61 39.45 -82.38
REMARK 500 1 LEU A 62 -33.06 -132.16
REMARK 500 1 THR A 63 72.22 -66.70
REMARK 500 1 LYS A 64 36.16 34.40
REMARK 500 1 PRO A 72 97.71 -69.83
REMARK 500 2 SER A 5 -60.85 -94.52
REMARK 500 2 LYS A 61 -35.22 -34.37
REMARK 500 3 LYS A 49 -70.04 -58.85
REMARK 500 3 LYS A 64 129.99 -173.33
REMARK 500 3 ILE A 67 137.84 -34.96
REMARK 500 3 PRO A 72 94.78 -69.77
REMARK 500 4 GLN A 9 42.29 -100.62
REMARK 500 4 GLU A 32 39.31 -82.31
REMARK 500 4 SER A 33 -55.11 -128.36
REMARK 500 4 LYS A 49 -70.00 -56.97
REMARK 500 4 GLN A 50 -38.18 -37.04
REMARK 500 4 THR A 63 40.13 -81.78
REMARK 500 4 ALA A 65 43.51 34.52
REMARK 500 4 VAL A 69 -60.53 -92.39
REMARK 500 4 PRO A 72 92.03 -69.73
REMARK 500 5 SER A 2 42.09 -85.15
REMARK 500 5 PHE A 59 -52.48 -132.28
REMARK 500 5 LEU A 62 48.65 -101.21
REMARK 500 5 LYS A 64 -63.52 -129.46
REMARK 500 5 SER A 74 100.51 -54.14
REMARK 500 6 SER A 2 150.99 -41.60
REMARK 500 6 GLN A 9 36.83 -85.78
REMARK 500 6 TRP A 11 116.26 -37.10
REMARK 500 6 GLN A 50 -39.88 -39.22
REMARK 500 6 LYS A 64 49.59 34.64
REMARK 500 6 ALA A 65 150.21 -34.42
REMARK 500 6 PRO A 72 86.47 -69.78
REMARK 500 7 GLN A 9 42.15 -89.44
REMARK 500 7 TRP A 11 155.19 -38.35
REMARK 500 7 LYS A 49 -71.28 -61.08
REMARK 500 7 GLN A 50 -29.42 -38.46
REMARK 500 7 THR A 63 159.27 -45.83
REMARK 500 7 PRO A 72 89.54 -69.71
REMARK 500 8 SER A 3 42.19 -90.86
REMARK 500 8 SER A 5 41.79 39.34
REMARK 500 8 ALA A 48 -26.68 -38.18
REMARK 500 8 PRO A 68 -173.29 -69.76
REMARK 500 8 SER A 70 139.91 -172.20
REMARK 500 9 SER A 3 -62.29 -104.08
REMARK 500 9 ASN A 8 -47.78 -133.16
REMARK 500 9 GLN A 16 -70.20 -45.47
REMARK 500 9 THR A 63 144.27 -39.60
REMARK 500 9 LYS A 64 134.55 -39.33
REMARK 500 9 SER A 70 -46.68 -134.77
REMARK 500 10 ASN A 8 79.78 -104.45
REMARK 500 10 TRP A 11 171.87 -51.70
REMARK 500 10 GLN A 50 -39.29 -39.01
REMARK 500 10 THR A 63 172.63 -51.32
REMARK 500 10 ILE A 67 132.84 -33.72
REMARK 500 11 ASN A 8 45.43 -91.59
REMARK 500 11 PHE A 59 -56.14 -131.67
REMARK 500 11 LEU A 62 45.99 -107.84
REMARK 500 11 THR A 63 -62.38 -91.19
REMARK 500 12 GLN A 9 66.90 -108.69
REMARK 500 12 ALA A 48 -28.34 -37.15
REMARK 500 12 LYS A 49 -71.00 -74.76
REMARK 500 12 VAL A 69 140.06 -35.17
REMARK 500 13 SER A 5 42.63 38.63
REMARK 500 13 LYS A 18 -36.90 -39.40
REMARK 500 13 GLU A 32 -29.93 -36.39
REMARK 500 13 SER A 33 -70.65 -50.47
REMARK 500 13 LYS A 49 -70.10 -54.66
REMARK 500 13 GLN A 50 -36.63 -38.16
REMARK 500 14 SER A 3 -53.70 -122.56
REMARK 500 14 SER A 6 -53.51 -131.99
REMARK 500 14 LYS A 49 -70.23 -58.28
REMARK 500 14 ILE A 67 132.82 -33.61
REMARK 500 15 SER A 2 42.09 -100.61
REMARK 500 15 VAL A 13 -72.57 -33.73
REMARK 500 15 LEU A 62 -33.39 -36.43
REMARK 500 15 ALA A 65 41.97 -80.56
REMARK 500 15 SER A 74 147.58 -172.22
REMARK 500 16 ASN A 8 44.71 -81.99
REMARK 500 16 VAL A 69 39.93 29.57
REMARK 500 16 SER A 70 150.79 -34.45
REMARK 500 16 PRO A 72 -177.32 -69.81
REMARK 500 17 LEU A 62 33.35 -88.19
REMARK 500 17 LYS A 64 161.56 -41.88
REMARK 500 17 ALA A 65 155.39 -43.70
REMARK 500 17 SER A 70 47.16 39.61
REMARK 500 17 SER A 74 -59.43 -129.95
REMARK 500 18 VAL A 13 -37.10 -36.65
REMARK 500 18 VAL A 69 143.22 -37.37
REMARK 500 19 TRP A 11 134.49 -34.05
REMARK 500 19 GLU A 20 -39.17 -34.67
REMARK 500 19 LYS A 49 -71.28 -60.91
REMARK 500 19 THR A 63 149.81 -34.85
REMARK 500 19 SER A 73 -71.97 -73.92
REMARK 500 20 GLN A 9 41.75 -87.90
REMARK 500 20 TRP A 11 137.64 -39.28
REMARK 500 20 LYS A 49 -70.37 -69.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002027679.2 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS BASED ON REFERENCE 2 IN THE
REMARK 999 DATABASE, ZZZ3_HUMAN.
DBREF 2YUM A 8 69 UNP Q8IYH5 ZZZ3_HUMAN 652 713
SEQADV 2YUM GLY A 1 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 2 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 3 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM GLY A 4 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 5 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 6 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM GLY A 7 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 70 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM GLY A 71 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM PRO A 72 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 73 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM SER A 74 UNP Q8IYH5 EXPRESSION TAG
SEQADV 2YUM GLY A 75 UNP Q8IYH5 EXPRESSION TAG
SEQRES 1 A 75 GLY SER SER GLY SER SER GLY ASN GLN LEU TRP THR VAL
SEQRES 2 A 75 GLU GLU GLN LYS LYS LEU GLU GLN LEU LEU ILE LYS TYR
SEQRES 3 A 75 PRO PRO GLU GLU VAL GLU SER ARG ARG TRP GLN LYS ILE
SEQRES 4 A 75 ALA ASP GLU LEU GLY ASN ARG THR ALA LYS GLN VAL ALA
SEQRES 5 A 75 SER GLN VAL GLN LYS TYR PHE ILE LYS LEU THR LYS ALA
SEQRES 6 A 75 GLY ILE PRO VAL SER GLY PRO SER SER GLY
HELIX 1 1 THR A 12 TYR A 26 1 15
HELIX 2 2 VAL A 31 GLY A 44 1 14
HELIX 3 3 THR A 47 ILE A 60 1 14
HELIX 4 4 LYS A 61 THR A 63 5 3
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
