HEADER TRANSCRIPTION 30-MAR-07 2EQM
TITLE SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN 20-LIKE 1
TITLE 2 [HOMO SAPIENS]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHD FINGER PROTEIN 20-LIKE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TUDOR 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: PHF20L1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060911-19;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TUDOR DOMAIN, PHD FINGER PROTEIN 20-LIKE 1, HOMO SAPIENS, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TARADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2EQM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EQM 1 VERSN
REVDAT 1 02-OCT-07 2EQM 0
JRNL AUTH W.DANG,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TARADA,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN
JRNL TITL 2 20-LIKE 1 [HOMO SAPIENS]
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EQM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000026986.
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 : 1.0MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3;90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -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 : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9820, 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, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, 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 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 LYS A 10 -74.71 -34.60
REMARK 500 1 ASN A 14 99.48 -49.16
REMARK 500 1 PRO A 16 80.16 -69.76
REMARK 500 1 TRP A 57 100.70 -48.92
REMARK 500 1 ARG A 60 94.43 -34.51
REMARK 500 1 PRO A 74 97.77 -69.80
REMARK 500 1 PRO A 78 -172.28 -69.75
REMARK 500 1 ARG A 81 53.84 33.44
REMARK 500 2 SER A 2 119.72 -169.27
REMARK 500 2 LYS A 10 -72.28 -33.86
REMARK 500 2 PRO A 13 -169.99 -69.72
REMARK 500 2 PRO A 16 80.08 -69.76
REMARK 500 2 SER A 58 -57.40 -122.42
REMARK 500 2 TYR A 66 121.45 -39.27
REMARK 500 2 ASN A 70 32.40 73.78
REMARK 500 2 PRO A 74 95.68 -69.73
REMARK 500 2 ARG A 81 38.88 -91.49
REMARK 500 2 LEU A 85 140.60 -35.46
REMARK 500 3 SER A 3 104.03 -35.24
REMARK 500 3 SER A 5 121.32 -37.94
REMARK 500 3 LYS A 10 -74.25 -36.65
REMARK 500 3 ASN A 14 99.63 -48.80
REMARK 500 3 PRO A 16 79.69 -69.72
REMARK 500 3 GLN A 33 29.31 47.97
REMARK 500 3 SER A 58 143.49 -38.00
REMARK 500 3 TYR A 61 101.65 -38.94
REMARK 500 3 TRP A 67 -9.46 -60.00
REMARK 500 3 PRO A 74 92.22 -69.76
REMARK 500 3 LEU A 85 105.89 -55.73
REMARK 500 4 SER A 3 163.86 -45.53
REMARK 500 4 LYS A 10 -73.13 -41.65
REMARK 500 4 ASN A 14 100.37 -49.58
REMARK 500 4 PRO A 16 80.10 -69.85
REMARK 500 4 GLN A 33 25.48 48.24
REMARK 500 4 ARG A 60 77.15 -113.12
REMARK 500 4 ASN A 70 30.26 70.08
REMARK 500 4 PRO A 74 98.08 -69.72
REMARK 500 4 ARG A 81 57.24 -101.34
REMARK 500 4 LEU A 85 -68.51 -92.77
REMARK 500 5 SER A 2 86.96 -65.52
REMARK 500 5 SER A 9 -50.05 -120.01
REMARK 500 5 LYS A 10 -73.06 -38.75
REMARK 500 5 ASN A 14 102.06 -54.53
REMARK 500 5 PRO A 16 79.96 -69.72
REMARK 500 5 TRP A 67 -9.24 -59.49
REMARK 500 5 ASN A 70 31.89 74.93
REMARK 500 5 PRO A 74 93.37 -69.75
REMARK 500 5 GLU A 76 104.97 -55.54
REMARK 500 5 PRO A 78 -171.76 -69.77
REMARK 500 5 LEU A 85 113.55 -172.39
REMARK 500
REMARK 500 THIS ENTRY HAS 160 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003013074.1 RELATED DB: TARGETDB
DBREF 2EQM A 8 88 UNP Q96BT0 Q96BT0_HUMAN 1 81
SEQADV 2EQM GLY A 1 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM SER A 2 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM SER A 3 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM GLY A 4 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM SER A 5 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM SER A 6 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQM GLY A 7 UNP Q96BT0 EXPRESSION TAG
SEQRES 1 A 88 GLY SER SER GLY SER SER GLY MET SER LYS LYS PRO PRO
SEQRES 2 A 88 ASN ARG PRO GLY ILE THR PHE GLU ILE GLY ALA ARG LEU
SEQRES 3 A 88 GLU ALA LEU ASP TYR LEU GLN LYS TRP TYR PRO SER ARG
SEQRES 4 A 88 ILE GLU LYS ILE ASP TYR GLU GLU GLY LYS MET LEU VAL
SEQRES 5 A 88 HIS PHE GLU ARG TRP SER HIS ARG TYR ASP GLU TRP ILE
SEQRES 6 A 88 TYR TRP ASP SER ASN ARG LEU ARG PRO LEU GLU ARG PRO
SEQRES 7 A 88 ALA LEU ARG LYS GLU GLY LEU LYS ASP GLU
SHEET 1 A 5 TYR A 61 TYR A 66 0
SHEET 2 A 5 LYS A 49 PHE A 54 -1 N VAL A 52 O GLU A 63
SHEET 3 A 5 TRP A 35 ASP A 44 -1 N GLU A 41 O LEU A 51
SHEET 4 A 5 ARG A 25 LEU A 29 -1 N LEU A 26 O SER A 38
SHEET 5 A 5 LEU A 72 ARG A 73 -1 O ARG A 73 N GLU A 27
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