HEADER PROTEIN BINDING 30-MAR-07 2EQU
TITLE SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN 20-LIKE 1
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: CELL-FREE PROTEIN SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P060911-17
KEYWDS TUDOR DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.FUTAMI,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2EQU 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2EQU 1 VERSN
REVDAT 1 02-OCT-07 2EQU 0
JRNL AUTH K.FUTAMI,S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,
JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE TUDOR DOMAIN OF PHD FINGER PROTEIN
JRNL TITL 2 20-LIKE 1
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, AMBER 9
REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID,A,CASE. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EQU 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_1000026994.
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 : 1.17MM 13C-15N PROTEIN; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20060702, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9820, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
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 SER A 79 26.90 47.78
REMARK 500 1 SER A 80 10.37 -148.58
REMARK 500 1 SER A 82 30.25 -155.90
REMARK 500 1 PHE A 85 8.65 -152.22
REMARK 500 1 TRP A 97 -162.98 -121.71
REMARK 500 1 ASN A 111 5.31 53.75
REMARK 500 1 GLU A 113 43.02 -140.02
REMARK 500 1 LYS A 141 -40.37 -131.24
REMARK 500 2 TRP A 97 -150.09 -136.91
REMARK 500 2 THR A 115 -169.19 -162.36
REMARK 500 3 TRP A 97 -36.13 -144.92
REMARK 500 3 LYS A 112 89.22 -29.62
REMARK 500 3 GLU A 113 40.33 38.39
REMARK 500 3 ALA A 140 153.86 -49.28
REMARK 500 3 ASP A 144 36.47 -148.95
REMARK 500 3 TRP A 145 46.67 -69.23
REMARK 500 3 LEU A 148 32.39 -79.90
REMARK 500 4 TRP A 145 13.81 -141.59
REMARK 500 5 TRP A 97 -44.13 -140.23
REMARK 500 5 GLU A 113 35.43 -142.91
REMARK 500 5 TRP A 145 31.77 -69.95
REMARK 500 5 LEU A 148 0.75 -67.60
REMARK 500 6 TRP A 97 -48.02 -138.89
REMARK 500 6 THR A 98 -14.55 -140.27
REMARK 500 6 LYS A 112 -175.86 -67.24
REMARK 500 6 TRP A 145 36.06 -78.13
REMARK 500 7 THR A 98 -29.17 -155.25
REMARK 500 7 GLU A 113 24.33 -140.63
REMARK 500 7 GLN A 143 1.21 -59.61
REMARK 500 7 TRP A 145 7.84 44.86
REMARK 500 8 TRP A 97 -39.77 -151.42
REMARK 500 8 THR A 98 -32.68 -132.73
REMARK 500 8 ASN A 111 11.32 53.35
REMARK 500 8 GLU A 113 49.77 -142.09
REMARK 500 8 TRP A 145 -12.14 -142.51
REMARK 500 9 CYS A 100 34.78 -74.04
REMARK 500 9 MET A 131 2.61 -69.16
REMARK 500 9 LEU A 148 2.84 -65.53
REMARK 500 10 SER A 80 42.60 -80.61
REMARK 500 10 TRP A 97 -42.51 -142.74
REMARK 500 10 ASN A 111 18.51 51.51
REMARK 500 10 MET A 131 -7.33 -59.31
REMARK 500 10 LEU A 148 23.24 -152.24
REMARK 500 11 TRP A 97 -159.70 -93.75
REMARK 500 11 ALA A 140 89.79 -46.84
REMARK 500 11 LYS A 141 27.24 45.81
REMARK 500 11 TRP A 145 38.92 -81.78
REMARK 500 11 ILE A 146 -149.06 -85.93
REMARK 500 11 ALA A 147 48.32 -72.02
REMARK 500 12 THR A 98 -56.50 -142.41
REMARK 500
REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003013074.2 RELATED DB: TARGETDB
DBREF 2EQU A 85 151 UNP Q96BT0 Q96BT0_HUMAN 85 151
SEQADV 2EQU GLY A 78 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU SER A 79 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU SER A 80 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU GLY A 81 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU SER A 82 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU SER A 83 UNP Q96BT0 EXPRESSION TAG
SEQADV 2EQU GLY A 84 UNP Q96BT0 EXPRESSION TAG
SEQRES 1 A 74 GLY SER SER GLY SER SER GLY PHE ASP PHE LYS ALA GLY
SEQRES 2 A 74 GLU GLU VAL LEU ALA ARG TRP THR ASP CYS ARG TYR TYR
SEQRES 3 A 74 PRO ALA LYS ILE GLU ALA ILE ASN LYS GLU GLY THR PHE
SEQRES 4 A 74 THR VAL GLN PHE TYR ASP GLY VAL ILE ARG CYS LEU LYS
SEQRES 5 A 74 ARG MET HIS ILE LYS ALA MET PRO GLU ASP ALA LYS GLY
SEQRES 6 A 74 GLN ASP TRP ILE ALA LEU VAL LYS ALA
HELIX 1 1 LYS A 129 MET A 131 5 3
HELIX 2 2 PRO A 137 LYS A 141 5 5
SHEET 1 A 5 ILE A 125 LEU A 128 0
SHEET 2 A 5 PHE A 116 PHE A 120 -1 N PHE A 116 O LEU A 128
SHEET 3 A 5 TYR A 102 ILE A 110 -1 N GLU A 108 O THR A 117
SHEET 4 A 5 GLU A 92 ARG A 96 -1 N VAL A 93 O ALA A 105
SHEET 5 A 5 ILE A 133 LYS A 134 -1 O LYS A 134 N LEU A 94
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