Header list of 1fhr.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 02-AUG-00 1FHR
TITLE SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A
TITLE 2 PHOSPHOTYROSYL PEPTIDE
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T;
SOURCE 9 OTHER_DETAILS: YEAST;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THIS PEPTIDE WAS SYNTHESIZED.
KEYWDS FHA DOMAIN, RAD53, RAD9, PHOSPHOTYROSINE, PHOSPHOPROTEIN, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR I.-J.L.BYEON,H.LIAO,S.YONGKIETTRAKUL,M.-D.TSAI
REVDAT 4 23-FEB-22 1FHR 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1FHR 1 VERSN
REVDAT 2 01-APR-03 1FHR 1 JRNL
REVDAT 1 18-OCT-00 1FHR 0
JRNL AUTH P.WANG,I.J.BYEON,H.LIAO,K.D.BEEBE,S.YONGKIETTRAKUL,D.PEI,
JRNL AUTH 2 M.D.TSAI
JRNL TITL II. STRUCTURE AND SPECIFICITY OF THE INTERACTION BETWEEN THE
JRNL TITL 2 FHA2 DOMAIN OF RAD53 AND PHOSPHOTYROSYL PEPTIDES.
JRNL REF J.MOL.BIOL. V. 302 927 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10993733
JRNL DOI 10.1006/JMBI.2000.4095
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.LIAO,I.-J.L.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 STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3346 RESTRAINTS, 3158 DISTANCE CONSTRAINTS, AND 188 TALOS-
REMARK 3 DERIVED DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1FHR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011599.
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 BUFFER
REMARK 210 (PH 6.5), 1 MM DTT,AND 1 MM EDTA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM FHA2 U-15N,13C; 1 MM
REMARK 210 PHOSPHOTYROSYL PEPTIDE OF RAD9;
REMARK 210 10 MM SODIUM PHOSPHATE BUFFER
REMARK 210 (PH 6.5), 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 : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
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 H TYR A 649 O PHE A 670 1.46
REMARK 500 H ILE A 603 O CYS A 623 1.48
REMARK 500 H TYR A 658 O LYS A 679 1.51
REMARK 500 O ILE A 665 HG1 THR A 668 1.52
REMARK 500 O LYS A 628 H ASP A 646 1.54
REMARK 500 O PHE A 626 H TRP A 648 1.55
REMARK 500 O THR A 579 H GLU A 695 1.57
REMARK 500 O TYR A 658 H LYS A 679 1.57
REMARK 500 HD2 PRO A 582 O GLU A 590 1.58
REMARK 500 O PHE A 624 H CYS A 650 1.58
REMARK 500 H LEU A 580 O LEU A 592 1.59
REMARK 500 O PHE A 602 H CYS A 611 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 GLN A 589 58.41 -155.53
REMARK 500 1 ASN A 610 -36.77 -35.86
REMARK 500 1 ASN A 616 -34.98 -36.00
REMARK 500 1 ARG A 620 -73.17 -51.68
REMARK 500 1 LYS A 634 172.98 58.45
REMARK 500 1 SER A 635 113.93 -167.64
REMARK 500 1 MET A 636 44.49 -94.32
REMARK 500 1 TYR A 637 -153.54 -174.30
REMARK 500 1 PRO A 640 -153.89 -71.35
REMARK 500 1 ALA A 641 -71.01 80.02
REMARK 500 1 GLN A 642 -161.31 42.14
REMARK 500 1 LEU A 644 -151.16 -146.53
REMARK 500 1 VAL A 656 155.74 49.85
REMARK 500 1 ASN A 660 -76.29 63.92
REMARK 500 1 ASN A 661 22.20 -152.26
REMARK 500 1 GLN A 666 104.95 -50.62
REMARK 500 1 THR A 700 66.96 -69.37
REMARK 500 1 ASN A 704 -51.87 -148.70
REMARK 500 1 GLU A 705 -28.09 152.19
REMARK 500 1 LEU A 710 129.61 67.14
REMARK 500 1 GLN A 711 90.41 42.93
REMARK 500 1 ARG A 714 77.47 -106.03
REMARK 500 1 ASP P 827 41.71 -99.10
REMARK 500 2 ASN A 610 -34.73 -38.68
REMARK 500 2 ARG A 620 -73.99 -51.57
REMARK 500 2 VAL A 621 58.14 -91.97
REMARK 500 2 CYS A 623 146.30 177.56
REMARK 500 2 TYR A 637 -157.75 175.23
REMARK 500 2 PRO A 640 -151.99 -69.39
REMARK 500 2 ALA A 641 -68.49 73.84
REMARK 500 2 GLN A 642 -171.85 46.61
REMARK 500 2 LEU A 644 -154.42 -146.95
REMARK 500 2 VAL A 656 148.60 49.30
REMARK 500 2 ASN A 660 -77.27 63.35
REMARK 500 2 ASN A 661 19.50 -148.50
REMARK 500 2 GLN A 666 107.34 -55.96
REMARK 500 2 THR A 700 65.44 -68.74
REMARK 500 2 ASN A 704 -65.41 -154.95
REMARK 500 2 GLU A 705 -30.20 169.98
REMARK 500 2 LEU A 710 -162.60 -166.79
REMARK 500 2 ARG A 714 79.01 44.57
REMARK 500 2 PTR P 829 32.24 -162.76
REMARK 500 3 PRO A 582 109.49 -58.49
REMARK 500 3 GLN A 589 52.78 -153.30
REMARK 500 3 ASN A 610 -33.43 -38.79
REMARK 500 3 ASN A 616 -36.56 -36.47
REMARK 500 3 VAL A 621 52.36 -99.49
REMARK 500 3 CYS A 623 155.30 178.61
REMARK 500 3 MET A 636 49.62 -88.18
REMARK 500 3 TYR A 637 -153.36 -176.05
REMARK 500
REMARK 500 THIS ENTRY HAS 423 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
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.
DBREF 1FHR A 573 730 UNP P22216 RAD53_YEAST 573 730
DBREF 1FHR P 826 832 UNP P14737 RAD9_YEAST 826 832
SEQADV 1FHR 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 1FHR 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 VAL A 727 1 8
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 578 O ILE A 594
SHEET 3 A 6 PHE A 688 ILE A 696 -1 O LYS A 693 N LYS A 581
SHEET 4 A 6 ASP A 676 ASP A 683 -1 O ASP A 676 N 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 O PHE A 602 N CYS A 611
SHEET 3 B 6 CYS A 623 HIS A 630 -1 O CYS A 623 N ILE A 603
SHEET 4 B 6 LEU A 644 HIS A 651 -1 O LEU A 644 N HIS A 630
SHEET 5 B 6 THR A 668 LEU A 671 -1 N THR A 668 O HIS A 651
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 -0.97
CISPEP 2 ASN A 599 PRO A 600 2 -1.55
CISPEP 3 ASN A 599 PRO A 600 3 -1.54
CISPEP 4 ASN A 599 PRO A 600 4 -1.78
CISPEP 5 ASN A 599 PRO A 600 5 -1.87
CISPEP 6 ASN A 599 PRO A 600 6 -1.63
CISPEP 7 ASN A 599 PRO A 600 7 -2.39
CISPEP 8 ASN A 599 PRO A 600 8 -1.24
CISPEP 9 ASN A 599 PRO A 600 9 -2.37
CISPEP 10 ASN A 599 PRO A 600 10 -2.16
CISPEP 11 ASN A 599 PRO A 600 11 -1.82
CISPEP 12 ASN A 599 PRO A 600 12 -2.33
CISPEP 13 ASN A 599 PRO A 600 13 -1.43
CISPEP 14 ASN A 599 PRO A 600 14 -1.39
CISPEP 15 ASN A 599 PRO A 600 15 -1.55
CISPEP 16 ASN A 599 PRO A 600 16 -1.27
CISPEP 17 ASN A 599 PRO A 600 17 -1.59
CISPEP 18 ASN A 599 PRO A 600 18 -1.64
CISPEP 19 ASN A 599 PRO A 600 19 -2.48
CISPEP 20 ASN A 599 PRO A 600 20 -0.85
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 - b 23 2 Bytes