Header list of 1j4l.pdb file
Complete list - 23 20 Bytes
HEADER TRANSFERASE 03-OCT-01 1J4L
TITLE SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A
TITLE 2 PHOSPHOTHREONYL PEPTIDE DERIVED FROM RAD9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE SPK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FHA DOMAIN (FHA2);
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA REPAIR PROTEIN RAD9;
COMPND 9 CHAIN: P;
COMPND 10 FRAGMENT: RESIDUES 599-607;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: SPK1 OR RAD53;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-4T;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THIS PHOSPHOTHREONYL PEPTIDE WAS CHEMICALLY
SOURCE 14 SYNTHESIZED.
KEYWDS FHA DOMAIN, RAD53, RAD9, PHOSPHOTHREONINE, PHOSPHOPROTEIN,
KEYWDS 2 TRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR I.-J.L.BYEON,S.YONGKIETTRAKUL,M.-D.TSAI
REVDAT 4 23-FEB-22 1J4L 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1J4L 1 VERSN
REVDAT 2 01-APR-03 1J4L 1 JRNL
REVDAT 1 05-DEC-01 1J4L 0
JRNL AUTH I.J.BYEON,S.YONGKIETTRAKUL,M.D.TSAI
JRNL TITL SOLUTION STRUCTURE OF THE YEAST RAD53 FHA2 COMPLEXED WITH A
JRNL TITL 2 PHOSPHOTHREONINE PEPTIDE PTXXL: COMPARISON WITH THE
JRNL TITL 3 STRUCTURES OF FHA2-PYXL AND FHA1-PTXXD COMPLEXES.
JRNL REF J.MOL.BIOL. V. 314 577 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11846568
JRNL DOI 10.1006/JMBI.2001.5141
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.WANG,I.J.BYEON,H.LIAO,K.D.BEEBE,S.YONGKIETTRAKUL,D.PEI,
REMARK 1 AUTH 2 M.D.TSAI
REMARK 1 TITL II. STRUCTURE AND SPECIFICITY OF THE INTERACTION BETWEEN THE
REMARK 1 TITL 2 FHA2 DOMAIN OF RAD53 AND PHOSPHOTYROSYL PEPTIDES.
REMARK 1 REF J.MOL.BIOL. V. 302 927 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.4095
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.LIAO,I.J.BYEON,M.D.TSAI
REMARK 1 TITL STRUCTURE AND FUNCTION OF A NEW PHOSPHOPEPTIDE-BINDING
REMARK 1 TITL 2 DOMAIN CONTAINING THE FHA2 OF RAD53.
REMARK 1 REF J.MOL.BIOL. V. 294 1041 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1999.3313
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J4L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000001605.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293.00
REMARK 210 PH : 6.50
REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE, 1 MM
REMARK 210 DTT, AND 1 MM EDTA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM FHA2 U-15N,13C 1.5 MM
REMARK 210 PHOSPHOTHREONYL PEPTIDE OF RAD9;
REMARK 210 10 MM SODIUM PHOSPHATE(PH 6.5),
REMARK 210 1 MM DTT, AND 1 MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D_13C/15N-
REMARK 210 FILTERED_NOESY; 3D_13C -EDITED_
REMARK 210 13C/15N-FILTERED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : THE COMPLEX STRUCTURES ARE
REMARK 210 GENERATED USING A TOTAL OF 3369
REMARK 210 RESTRAINTS, 3181 DISTANCE
REMARK 210 RESTRAINTS, AND 188 TALOS-
REMARK 210 DERIVED DIHEDRAL ANGLE
REMARK 210 RESTRAINTS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE- RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, P
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TYR A 658 H LYS A 679 1.53
REMARK 500 O GLN A 595 H VAL A 598 1.53
REMARK 500 H PHE A 626 O TRP A 648 1.58
REMARK 500 H TYR A 658 O LYS A 679 1.59
REMARK 500 O LYS A 628 H ASP A 646 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 577 -55.52 -122.56
REMARK 500 PRO A 582 99.61 -47.24
REMARK 500 GLN A 589 56.41 -110.38
REMARK 500 TYR A 637 -69.96 68.42
REMARK 500 PRO A 640 -154.85 -61.93
REMARK 500 GLN A 642 -61.34 78.75
REMARK 500 LEU A 644 -162.12 -108.26
REMARK 500 VAL A 656 124.42 54.79
REMARK 500 ASN A 660 -82.76 55.72
REMARK 500 GLN A 666 101.85 -39.40
REMARK 500 ASN A 704 -52.09 -155.43
REMARK 500 GLU A 705 -36.09 146.92
REMARK 500 LEU A 710 -154.68 45.69
REMARK 500 GLN A 711 -76.60 14.08
REMARK 500 GLU A 712 96.84 -65.23
REMARK 500 ARG A 714 87.46 47.15
REMARK 500 GLU P 601 44.52 -166.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1J4L A 573 730 UNP P22216 RAD53_YEAST 573 730
DBREF 1J4L P 599 607 UNP P14737 RAD9_YEAST 599 607
SEQADV 1J4L TPO P 603 UNP P14737 THR 603 MODIFIED RESIDUE
SEQRES 1 A 158 GLY ASN GLY ARG PHE LEU THR LEU LYS PRO LEU PRO ASP
SEQRES 2 A 158 SER ILE ILE GLN GLU SER LEU GLU ILE GLN GLN GLY VAL
SEQRES 3 A 158 ASN PRO PHE PHE ILE GLY ARG SER GLU ASP CYS ASN CYS
SEQRES 4 A 158 LYS ILE GLU ASP ASN ARG LEU SER ARG VAL HIS CYS PHE
SEQRES 5 A 158 ILE PHE LYS LYS ARG HIS ALA VAL GLY LYS SER MET TYR
SEQRES 6 A 158 GLU SER PRO ALA GLN GLY LEU ASP ASP ILE TRP TYR CYS
SEQRES 7 A 158 HIS THR GLY THR ASN VAL SER TYR LEU ASN ASN ASN ARG
SEQRES 8 A 158 MET ILE GLN GLY THR LYS PHE LEU LEU GLN ASP GLY ASP
SEQRES 9 A 158 GLU ILE LYS ILE ILE TRP ASP LYS ASN ASN LYS PHE VAL
SEQRES 10 A 158 ILE GLY PHE LYS VAL GLU ILE ASN ASP THR THR GLY LEU
SEQRES 11 A 158 PHE ASN GLU GLY LEU GLY MET LEU GLN GLU GLN ARG VAL
SEQRES 12 A 158 VAL LEU LYS GLN THR ALA GLU GLU LYS ASP LEU VAL LYS
SEQRES 13 A 158 LYS LEU
SEQRES 1 P 9 GLU VAL GLU LEU TPO GLN GLU LEU PRO
MODRES 1J4L TPO P 603 THR PHOSPHOTHREONINE
HET TPO P 603 17
HETNAM TPO PHOSPHOTHREONINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 2 TPO C4 H10 N O6 P
HELIX 1 1 THR A 720 LYS A 729 1 10
SHEET 1 A 6 LEU A 592 ILE A 594 0
SHEET 2 A 6 LEU A 578 PRO A 582 -1 N LEU A 580 O LEU A 592
SHEET 3 A 6 PHE A 692 ILE A 696 -1 O GLU A 695 N THR A 579
SHEET 4 A 6 ASP A 676 LYS A 679 -1 N ASP A 676 O VAL A 694
SHEET 5 A 6 SER A 657 LEU A 659 -1 N TYR A 658 O LYS A 679
SHEET 6 A 6 ASN A 662 MET A 664 -1 O ASN A 662 N LEU A 659
SHEET 1 B 6 CYS A 611 LYS A 612 0
SHEET 2 B 6 PHE A 601 GLY A 604 1 N GLY A 604 O CYS A 611
SHEET 3 B 6 CYS A 623 HIS A 630 -1 O ILE A 625 N PHE A 601
SHEET 4 B 6 LEU A 644 HIS A 651 -1 O ASP A 646 N LYS A 628
SHEET 5 B 6 THR A 668 LEU A 671 -1 O PHE A 670 N TYR A 649
SHEET 6 B 6 LEU A 717 LYS A 718 -1 O LEU A 717 N LYS A 669
LINK C LEU P 602 N TPO P 603 1555 1555 1.33
LINK C TPO P 603 N GLN P 604 1555 1555 1.33
CISPEP 1 ASN A 599 PRO A 600 0 0.56
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
Complete list - 23 20 Bytes