Header list of 1qu5.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 06-JUL-99 1QU5 TITLE NMR STRUCTURE OF A NEW PHOSPHOTYROSINE BINDING DOMAIN CONTAINING THE TITLE 2 FHA2 DOMAIN OF RAD 53 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN KINASE SPK1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PHOSPHOTYROSINE-BINDING FHA2 DOMAIN; COMPND 5 EC: 2.7.1.-; COMPND 6 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T KEYWDS FHA, RAD53, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 16 MDLTYP MINIMIZED AVERAGE AUTHOR I.-J.L.BYEON,H.LIAO,M.-D.TSAI REVDAT 6 02-MAR-22 1QU5 1 REMARK REVDAT 5 24-FEB-09 1QU5 1 VERSN REVDAT 4 01-APR-03 1QU5 1 JRNL REVDAT 3 17-JAN-01 1QU5 1 JRNL REVDAT 2 13-DEC-00 1QU5 1 AUTHOR JRNL SOURCE REVDAT 1 17-DEC-99 1QU5 0 JRNL AUTH H.LIAO,I.J.BYEON,M.D.TSAI JRNL TITL STRUCTURE AND FUNCTION OF A NEW PHOSPHOPEPTIDE-BINDING JRNL TITL 2 DOMAIN CONTAINING THE FHA2 OF RAD53. JRNL REF J.MOL.BIOL. V. 294 1041 1999 JRNL REFN ISSN 0022-2836 JRNL PMID 10588905 JRNL DOI 10.1006/JMBI.1999.3313 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER, A. T. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 IN THE FIRST STAGE, THE SIMULATED ANNEALING STRUCTURES WERE REMARK 3 DETERMINED BASED REMARK 3 ON THE EXPERIMENTAL INTER PROTON DISTANCE RESTRAINTS (2651 IN REMARK 3 TOTAL). THE REMARK 3 RESULTING STRUCTURES WERE THEN USED AS INITIAL STRCUTURES FOR THE REMARK 3 SECOND STAGE REMARK 3 OF SIMULATED ANNEALING CALCULATIONS WHERE, IN ADDITION TO THE REMARK 3 DISTANCE REMARK 3 RESTRAINTS, THE STRUCTURES WERE REFINED AGAINST SECONDARY REMARK 3 13C(ALPHA)/13C(BETA) REMARK 3 CHEMICAL SHIFT RESTRAINTS. REMARK 4 REMARK 4 1QU5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000009296. 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 : 0.2 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.2~0.5 MM FHA2, U-15N, 13C; 100 REMARK 210 MM SODIUM PHOSPHATE, 1MM DTT, REMARK 210 1MM EDTA; 0.2~0.5 MM FHA2, U-15N, REMARK 210 13C, 2H (~70%) TRIPLE LABELED; REMARK 210 100 MM PHOSPHATE, 1MM DTT, 1MM REMARK 210 EDTA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; 4D_13C- REMARK 210 SEPARATED_NOESY; HCCH-TOCSY; 15N- REMARK 210 1H-TROSY-HN(CO)CACB; 15N-1H- REMARK 210 TROSY-HNCACB REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.1, FELIX 98 REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 32 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 THE STRUCTURAL DETERMINATION WAS BENEFITED BY THE TROSY TYPE REMARK 210 EXPERIMENTS ON REMARK 210 THE TRIPLE-LABLED (13C, 15N, 2H) SAMPLE. 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: 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 LEU A 580 H LEU A 592 1.50 REMARK 500 O SER A 560 H THR A 563 1.53 REMARK 500 O ASN A 562 H ASN A 565 1.58 REMARK 500 O LYS A 634 HG SER A 635 1.60 REMARK 500 H LYS A 669 O LEU A 717 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 1 ALA A 550 -37.62 -169.74 REMARK 500 1 ARG A 553 108.78 109.84 REMARK 500 1 GLU A 554 97.65 65.46 REMARK 500 1 GLN A 555 -78.06 -170.47 REMARK 500 1 LEU A 557 -72.42 -121.13 REMARK 500 1 LEU A 558 172.85 171.52 REMARK 500 1 HIS A 559 170.98 46.62 REMARK 500 1 SER A 560 144.28 -14.62 REMARK 500 1 ASN A 561 -112.14 2.31 REMARK 500 1 THR A 563 25.82 41.21 REMARK 500 1 GLU A 564 24.90 46.33 REMARK 500 1 ASN A 565 64.84 39.02 REMARK 500 1 SER A 568 110.49 72.07 REMARK 500 1 LYS A 571 -78.39 -163.58 REMARK 500 1 LYS A 572 109.12 44.78 REMARK 500 1 PHE A 577 -39.60 -133.91 REMARK 500 1 GLN A 589 108.30 -165.13 REMARK 500 1 GLU A 590 -121.60 159.67 REMARK 500 1 GLN A 596 47.97 23.45 REMARK 500 1 VAL A 598 -35.48 -35.24 REMARK 500 1 ASN A 599 89.22 46.26 REMARK 500 1 CYS A 611 -138.96 -140.75 REMARK 500 1 LYS A 612 117.51 -176.75 REMARK 500 1 GLU A 614 71.14 10.14 REMARK 500 1 SER A 619 37.88 -92.65 REMARK 500 1 ARG A 620 117.56 66.55 REMARK 500 1 ALA A 631 93.53 60.04 REMARK 500 1 VAL A 632 161.46 -42.25 REMARK 500 1 SER A 635 163.74 105.91 REMARK 500 1 MET A 636 -111.43 44.72 REMARK 500 1 TYR A 637 165.79 49.95 REMARK 500 1 GLU A 638 -61.56 -129.94 REMARK 500 1 PRO A 640 -152.51 -66.26 REMARK 500 1 ALA A 641 50.03 -152.62 REMARK 500 1 LEU A 644 -174.18 54.07 REMARK 500 1 ASN A 655 -141.16 -102.74 REMARK 500 1 ASN A 660 -62.51 66.85 REMARK 500 1 GLN A 666 154.43 55.69 REMARK 500 1 TRP A 682 96.67 -162.52 REMARK 500 1 LYS A 687 75.38 47.96 REMARK 500 1 PHE A 688 88.05 -153.48 REMARK 500 1 ILE A 690 63.19 -109.69 REMARK 500 1 ASP A 698 -71.98 -87.00 REMARK 500 1 THR A 699 18.77 58.52 REMARK 500 1 THR A 700 -75.75 -49.42 REMARK 500 1 ASN A 704 11.44 57.89 REMARK 500 1 GLU A 705 26.51 47.06 REMARK 500 1 LEU A 707 28.47 -169.87 REMARK 500 1 MET A 709 63.08 -69.98 REMARK 500 1 GLU A 712 79.08 -175.43 REMARK 500 REMARK 500 THIS ENTRY HAS 799 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 553 0.28 SIDE CHAIN REMARK 500 1 ARG A 576 0.31 SIDE CHAIN REMARK 500 1 ARG A 605 0.26 SIDE CHAIN REMARK 500 1 ARG A 617 0.30 SIDE CHAIN REMARK 500 1 ARG A 620 0.32 SIDE CHAIN REMARK 500 1 ARG A 629 0.17 SIDE CHAIN REMARK 500 1 ARG A 663 0.32 SIDE CHAIN REMARK 500 1 ARG A 714 0.27 SIDE CHAIN REMARK 500 2 ARG A 553 0.10 SIDE CHAIN REMARK 500 2 ARG A 576 0.26 SIDE CHAIN REMARK 500 2 ARG A 605 0.28 SIDE CHAIN REMARK 500 2 ARG A 617 0.28 SIDE CHAIN REMARK 500 2 ARG A 629 0.31 SIDE CHAIN REMARK 500 2 ARG A 663 0.16 SIDE CHAIN REMARK 500 2 ARG A 714 0.32 SIDE CHAIN REMARK 500 3 ARG A 553 0.31 SIDE CHAIN REMARK 500 3 ARG A 576 0.31 SIDE CHAIN REMARK 500 3 ARG A 605 0.30 SIDE CHAIN REMARK 500 3 ARG A 617 0.29 SIDE CHAIN REMARK 500 3 ARG A 620 0.21 SIDE CHAIN REMARK 500 3 ARG A 629 0.20 SIDE CHAIN REMARK 500 3 ARG A 663 0.29 SIDE CHAIN REMARK 500 3 ARG A 714 0.30 SIDE CHAIN REMARK 500 4 ARG A 553 0.31 SIDE CHAIN REMARK 500 4 ARG A 576 0.32 SIDE CHAIN REMARK 500 4 ARG A 605 0.23 SIDE CHAIN REMARK 500 4 ARG A 617 0.13 SIDE CHAIN REMARK 500 4 ARG A 620 0.31 SIDE CHAIN REMARK 500 4 ARG A 663 0.20 SIDE CHAIN REMARK 500 4 ARG A 714 0.31 SIDE CHAIN REMARK 500 5 ARG A 553 0.24 SIDE CHAIN REMARK 500 5 ARG A 576 0.31 SIDE CHAIN REMARK 500 5 ARG A 605 0.21 SIDE CHAIN REMARK 500 5 ARG A 617 0.32 SIDE CHAIN REMARK 500 5 ARG A 620 0.32 SIDE CHAIN REMARK 500 5 ARG A 629 0.24 SIDE CHAIN REMARK 500 5 ARG A 663 0.32 SIDE CHAIN REMARK 500 5 ARG A 714 0.26 SIDE CHAIN REMARK 500 6 ARG A 553 0.28 SIDE CHAIN REMARK 500 6 ARG A 576 0.30 SIDE CHAIN REMARK 500 6 ARG A 617 0.31 SIDE CHAIN REMARK 500 6 ARG A 620 0.31 SIDE CHAIN REMARK 500 6 ARG A 629 0.19 SIDE CHAIN REMARK 500 6 ARG A 663 0.24 SIDE CHAIN REMARK 500 6 ARG A 714 0.31 SIDE CHAIN REMARK 500 7 ARG A 553 0.27 SIDE CHAIN REMARK 500 7 ARG A 576 0.27 SIDE CHAIN REMARK 500 7 ARG A 605 0.16 SIDE CHAIN REMARK 500 7 ARG A 617 0.26 SIDE CHAIN REMARK 500 7 ARG A 620 0.18 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 118 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1QU5 A 549 730 UNP P22216 RAD53_YEAST 549 730 SEQRES 1 A 182 GLU ALA GLU THR ARG GLU GLN LYS LEU LEU HIS SER ASN SEQRES 2 A 182 ASN THR GLU ASN VAL LYS SER SER LYS LYS LYS GLY ASN SEQRES 3 A 182 GLY ARG PHE LEU THR LEU LYS PRO LEU PRO ASP SER ILE SEQRES 4 A 182 ILE GLN GLU SER LEU GLU ILE GLN GLN GLY VAL ASN PRO SEQRES 5 A 182 PHE PHE ILE GLY ARG SER GLU ASP CYS ASN CYS LYS ILE SEQRES 6 A 182 GLU ASP ASN ARG LEU SER ARG VAL HIS CYS PHE ILE PHE SEQRES 7 A 182 LYS LYS ARG HIS ALA VAL GLY LYS SER MET TYR GLU SER SEQRES 8 A 182 PRO ALA GLN GLY LEU ASP ASP ILE TRP TYR CYS HIS THR SEQRES 9 A 182 GLY THR ASN VAL SER TYR LEU ASN ASN ASN ARG MET ILE SEQRES 10 A 182 GLN GLY THR LYS PHE LEU LEU GLN ASP GLY ASP GLU ILE SEQRES 11 A 182 LYS ILE ILE TRP ASP LYS ASN ASN LYS PHE VAL ILE GLY SEQRES 12 A 182 PHE LYS VAL GLU ILE ASN ASP THR THR GLY LEU PHE ASN SEQRES 13 A 182 GLU GLY LEU GLY MET LEU GLN GLU GLN ARG VAL VAL LEU SEQRES 14 A 182 LYS GLN THR ALA GLU GLU LYS ASP LEU VAL LYS LYS LEU HELIX 1 1 ASN A 562 VAL A 566 5 5 HELIX 2 2 LYS A 684 LYS A 687 5 4 HELIX 3 3 LEU A 702 GLY A 706 5 5 HELIX 4 4 THR A 720 VAL A 727 1 8 HELIX 5 5 LYS A 728 LEU A 730 5 3 SHEET 1 A 2 LEU A 578 LEU A 580 0 SHEET 2 A 2 VAL A 694 ILE A 696 -1 O GLU A 695 N THR A 579 SHEET 1 B 5 PHE A 601 ILE A 603 0 SHEET 2 B 5 CYS A 623 LYS A 628 -1 N CYS A 623 O ILE A 603 SHEET 3 B 5 ASP A 646 TYR A 649 -1 O ASP A 646 N LYS A 628 SHEET 4 B 5 THR A 668 LEU A 671 -1 N PHE A 670 O TYR A 649 SHEET 5 B 5 LEU A 717 LYS A 718 -1 O LEU A 717 N LYS A 669 SHEET 1 C 2 TYR A 658 LEU A 659 0 SHEET 2 C 2 ASN A 662 ARG A 663 -1 O ASN A 662 N LEU A 659 SHEET 1 D 2 LYS A 679 ASP A 683 0 SHEET 2 D 2 PHE A 688 GLY A 691 -1 O PHE A 688 N ASP A 683 CISPEP 1 ASN A 599 PRO A 600 1 -1.63 CISPEP 2 ASN A 599 PRO A 600 2 -1.52 CISPEP 3 ASN A 599 PRO A 600 3 -1.64 CISPEP 4 ASN A 599 PRO A 600 4 -2.50 CISPEP 5 ASN A 599 PRO A 600 5 -1.96 CISPEP 6 ASN A 599 PRO A 600 6 -0.46 CISPEP 7 ASN A 599 PRO A 600 7 -1.31 CISPEP 8 ASN A 599 PRO A 600 8 -2.27 CISPEP 9 ASN A 599 PRO A 600 9 -1.37 CISPEP 10 ASN A 599 PRO A 600 10 -1.88 CISPEP 11 ASN A 599 PRO A 600 11 -1.84 CISPEP 12 ASN A 599 PRO A 600 12 -2.38 CISPEP 13 ASN A 599 PRO A 600 13 -2.48 CISPEP 14 ASN A 599 PRO A 600 14 -2.34 CISPEP 15 ASN A 599 PRO A 600 15 -1.47 CISPEP 16 ASN A 599 PRO A 600 16 -1.86 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
Complete list - r 2 2 Bytes