Header list of 1k2m.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 28-SEP-01 1K2M TITLE SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A TITLE 2 PHOSPHOTYROSYL 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 826-832; 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 PHOSPHOTYROSYL PEPTIDE WAS CHEMICALLY SOURCE 14 SYNTHESIZED. KEYWDS FHA DOMAIN, RAD53, RAD9, PHOSPHOTYROSINE, PHOSPHOPROTEIN, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR I.-J.L.BYEON,S.YONGKIETTRAKUL,M.-D.TSAI REVDAT 4 23-FEB-22 1K2M 1 REMARK SEQADV LINK REVDAT 3 24-FEB-09 1K2M 1 VERSN REVDAT 2 01-APR-03 1K2M 1 JRNL REVDAT 1 05-DEC-01 1K2M 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 : BRUKER (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE COMPLEX STRUCTURES ARE GENERATED REMARK 3 USING A TOTAL OF 3398 RESTRAINTS, 3210 DISTANCE RESTRAINTS, AND REMARK 3 188 TOLOS-DERIVED DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1K2M COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-01. REMARK 100 THE DEPOSITION ID IS D_1000014482. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 10 MM SODIUM PHOSPHATE(PH 6.5), REMARK 210 1 MM DTT, AND 1 MM EDTA REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM FHA2 U-15N,13C; 1MM REMARK 210 PHOSPHOTYROSYL 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 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 : XWINNMR 2.6, X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY 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 THR A 652 HE21 GLN A 666 1.49 REMARK 500 O TYR A 658 H LYS A 679 1.53 REMARK 500 O ILE A 665 HG1 THR A 668 1.53 REMARK 500 O LYS A 628 H ASP A 646 1.55 REMARK 500 H PHE A 626 O TRP A 648 1.57 REMARK 500 H ILE A 587 O VAL A 689 1.58 REMARK 500 O PHE A 602 H CYS A 611 1.58 REMARK 500 O PHE A 626 H TRP A 648 1.59 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 1 PHE A 577 -61.08 -127.12 REMARK 500 1 PRO A 582 100.02 -46.86 REMARK 500 1 ASN A 616 -30.81 -38.80 REMARK 500 1 TYR A 637 -63.78 71.86 REMARK 500 1 GLN A 642 -82.53 62.33 REMARK 500 1 LEU A 644 -157.56 -99.83 REMARK 500 1 VAL A 656 133.02 51.59 REMARK 500 1 ASN A 660 -81.32 60.11 REMARK 500 1 GLN A 666 104.00 -55.81 REMARK 500 1 ASP A 674 120.52 -37.01 REMARK 500 1 LYS A 687 19.29 59.93 REMARK 500 1 PHE A 703 -36.77 -33.84 REMARK 500 1 ASN A 704 30.53 -171.98 REMARK 500 1 GLU A 705 -57.93 68.31 REMARK 500 1 LEU A 710 -161.70 -58.86 REMARK 500 1 GLN A 711 -64.17 77.22 REMARK 500 1 ARG A 714 85.51 19.96 REMARK 500 1 TYR P 830 89.65 -175.82 REMARK 500 2 PHE A 577 -56.23 -128.82 REMARK 500 2 PRO A 582 101.11 -45.96 REMARK 500 2 GLN A 589 57.09 -104.05 REMARK 500 2 VAL A 621 53.05 -105.18 REMARK 500 2 TYR A 637 -70.47 66.85 REMARK 500 2 PRO A 640 -163.36 -70.71 REMARK 500 2 GLN A 642 -67.50 70.55 REMARK 500 2 LEU A 644 -157.56 -101.14 REMARK 500 2 VAL A 656 128.42 54.32 REMARK 500 2 ASN A 660 -83.83 59.43 REMARK 500 2 THR A 700 50.74 -91.08 REMARK 500 2 ASN A 704 -44.69 -147.88 REMARK 500 2 GLU A 705 -34.00 136.10 REMARK 500 2 ARG A 714 86.90 42.43 REMARK 500 2 LYS A 729 -63.20 -102.08 REMARK 500 3 PHE A 577 -47.28 -132.69 REMARK 500 3 PRO A 582 99.22 -47.66 REMARK 500 3 GLN A 589 55.73 -106.03 REMARK 500 3 LYS A 634 105.15 60.07 REMARK 500 3 TYR A 637 -74.66 67.43 REMARK 500 3 PRO A 640 -149.98 -65.01 REMARK 500 3 GLN A 642 -171.92 71.95 REMARK 500 3 LEU A 644 -156.53 -107.67 REMARK 500 3 VAL A 656 136.71 50.14 REMARK 500 3 ASN A 660 -81.51 60.76 REMARK 500 3 GLN A 666 107.10 -42.76 REMARK 500 3 ASP A 674 95.18 -65.61 REMARK 500 3 ASN A 704 -56.06 -148.40 REMARK 500 3 GLU A 705 -28.76 156.14 REMARK 500 3 LEU A 710 -162.85 -55.27 REMARK 500 3 ARG A 714 83.48 40.26 REMARK 500 3 ASP P 827 78.71 62.11 REMARK 500 REMARK 500 THIS ENTRY HAS 393 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FHR RELATED DB: PDB REMARK 900 1FHR CONTAINS THE SAME FHA2-PTYR PEPTIDE COMPLEX. REMARK 900 RELATED ID: 1FHQ RELATED DB: PDB REMARK 900 1FHQ CONTAINS THE SAME PROTEIN IN A PEPTIDE-FREE STATE. REMARK 900 RELATED ID: 1DMZ RELATED DB: PDB REMARK 900 1DMZ CONTAINS THE SAME PROTEIN IN A PEPTIDE-FREE STATE. REMARK 900 RELATED ID: 1QU5 RELATED DB: PDB REMARK 900 1QU5 CONTAINS THE SAME PROTEIN IN A PEPTIDE-FREE STATE. REMARK 900 RELATED ID: 1J4K RELATED DB: PDB REMARK 900 1J4K CONTAINS THE MINIMIZED AVERAGE STRUCTURE FOR THIS ENSEMBLE. REMARK 900 RELATED ID: 1K2N RELATED DB: PDB REMARK 900 1K2N CONTAINS THE SAME PROTEIN COMPLEXED WITH A PHOSPHOTHREONYL REMARK 900 PEPTIDE DERIVED FROM RAD9. REMARK 900 RELATED ID: 1J4L RELATED DB: PDB REMARK 900 1J4L CONTAINS THE MINIMIZED AVERAGE STRUCTURE FOR THE SAME PROTEIN REMARK 900 COMPLEXED WITH A PHOSPHOTHREONYL PEPTIDE DERIVED FROM RAD9. DBREF 1K2M A 573 730 UNP P22216 RAD53_YEAST 573 730 DBREF 1K2M P 826 832 UNP P14737 RAD9_YEAST 826 832 SEQADV 1K2M PTR P 829 UNP P14737 TYR 829 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 7 GLU ASP ILE PTR TYR LEU ASP MODRES 1K2M PTR P 829 TYR O-PHOSPHOTYROSINE HET PTR P 829 24 HETNAM PTR O-PHOSPHOTYROSINE HETSYN PTR PHOSPHONOTYROSINE FORMUL 2 PTR C9 H12 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 672 -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 ILE P 828 N PTR P 829 1555 1555 1.33 LINK C PTR P 829 N TYR P 830 1555 1555 1.33 CISPEP 1 ASN A 599 PRO A 600 1 -0.16 CISPEP 2 ASN A 599 PRO A 600 2 0.22 CISPEP 3 ASN A 599 PRO A 600 3 -0.36 CISPEP 4 ASN A 599 PRO A 600 4 -0.36 CISPEP 5 ASN A 599 PRO A 600 5 -0.34 CISPEP 6 ASN A 599 PRO A 600 6 -0.71 CISPEP 7 ASN A 599 PRO A 600 7 -0.18 CISPEP 8 ASN A 599 PRO A 600 8 0.23 CISPEP 9 ASN A 599 PRO A 600 9 -0.23 CISPEP 10 ASN A 599 PRO A 600 10 -0.02 CISPEP 11 ASN A 599 PRO A 600 11 -0.76 CISPEP 12 ASN A 599 PRO A 600 12 -0.34 CISPEP 13 ASN A 599 PRO A 600 13 -0.27 CISPEP 14 ASN A 599 PRO A 600 14 -0.05 CISPEP 15 ASN A 599 PRO A 600 15 -0.07 CISPEP 16 ASN A 599 PRO A 600 16 -0.35 CISPEP 17 ASN A 599 PRO A 600 17 0.33 CISPEP 18 ASN A 599 PRO A 600 18 0.21 CISPEP 19 ASN A 599 PRO A 600 19 0.21 CISPEP 20 ASN A 599 PRO A 600 20 -0.43 CISPEP 21 ASN A 599 PRO A 600 21 -0.53 CISPEP 22 ASN A 599 PRO A 600 22 0.01 CRYST1 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
Complete list - b 23 2 Bytes