Header list of 1k3j.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 03-OCT-01 1K3J
TITLE REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE SPK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL FHA DOMAIN (FHA1);
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 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
KEYWDS FHA DOMAIN, RAD53, RAD9, PHOSPHOTHREONINE, PHOSPHOPROTEIN,
KEYWDS 2 TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.YUAN,S.YONGKIETTRAKUL,I.-J.L.BYEON,S.ZHOU,M.-D.TSAI
REVDAT 4 23-FEB-22 1K3J 1 REMARK
REVDAT 3 24-FEB-09 1K3J 1 VERSN
REVDAT 2 01-APR-03 1K3J 1 JRNL
REVDAT 1 05-DEC-01 1K3J 0
JRNL AUTH C.YUAN,S.YONGKIETTRAKUL,I.J.BYEON,S.ZHOU,M.D.TSAI
JRNL TITL SOLUTION STRUCTURES OF TWO FHA1-PHOSPHOTHREONINE PEPTIDE
JRNL TITL 2 COMPLEXES PROVIDE INSIGHT INTO THE STRUCTURAL BASIS OF THE
JRNL TITL 3 LIGAND SPECIFICITY OF FHA1 FROM YEAST RAD53.
JRNL REF J.MOL.BIOL. V. 314 563 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11846567
JRNL DOI 10.1006/JMBI.2001.5140
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K3J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014515.
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, 1MM DTT,
REMARK 210 AND 1 MM EDTA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM PROTEIN U-15N,13C; 10 MM
REMARK 210 SODIUM PHOSPHATE BUFFER (PH 6.5),
REMARK 210 1 MM DTT, AND 1 MM EDTA; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY
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 2.6, CNS 1.0
REMARK 210 METHOD USED : THE STRUCTURES ARE BASED ON A
REMARK 210 TOTAL OF 2377 RESTRAINTS. AMONG
REMARK 210 THEM, 2107 ARE NOE-DERIVED
REMARK 210 DISTANCE CONSTRAINTS, 192 TALOS-
REMARK 210 DERIVED DIHEDRAL ANGLE
REMARK 210 RESTRAINTS, AND 78 RESTRAINTS
REMARK 210 FROM HYDROGEN BONDS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS REFINED BY ADDING 221 NOE-DERIVED
REMARK 210 DISTANCE CONSTRAINTS AND BY REVISING A FEW PREVIOUS NOE
REMARK 210 ASSIGNMENTS.
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 H PHE A 68 O PHE A 89 1.54
REMARK 500 H TRP A 66 O ILE A 91 1.56
REMARK 500 O ARG A 35 H PHE A 146 1.58
REMARK 500 H GLN A 90 O ASN A 102 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 THR A 15 -60.51 -125.85
REMARK 500 1 ASN A 31 35.23 -171.98
REMARK 500 1 VAL A 33 -61.21 -91.70
REMARK 500 1 GLN A 42 -42.82 -146.01
REMARK 500 1 LYS A 59 31.18 -98.99
REMARK 500 1 LYS A 63 -66.18 -122.46
REMARK 500 1 CYS A 74 139.62 -39.77
REMARK 500 1 LEU A 78 -77.34 -71.97
REMARK 500 1 ASN A 80 64.95 -156.24
REMARK 500 1 GLU A 95 172.07 -47.97
REMARK 500 1 ASP A 96 68.74 -69.08
REMARK 500 1 ASN A 119 35.45 35.82
REMARK 500 1 ASP A 128 171.77 -53.62
REMARK 500 1 ASN A 158 71.74 42.77
REMARK 500 1 ARG A 162 31.08 -147.24
REMARK 500 2 THR A 15 -47.04 -138.93
REMARK 500 2 ASN A 31 38.56 178.84
REMARK 500 2 GLN A 42 -47.56 -144.23
REMARK 500 2 LYS A 63 -65.83 -120.50
REMARK 500 2 ARG A 70 36.05 -86.19
REMARK 500 2 ASP A 96 176.08 54.94
REMARK 500 2 ILE A 104 28.28 -147.62
REMARK 500 2 ASN A 119 34.89 35.15
REMARK 500 2 ASP A 128 167.15 -49.02
REMARK 500 2 ASN A 158 -90.83 42.89
REMARK 500 2 ARG A 162 153.43 61.66
REMARK 500 3 THR A 15 -69.92 -129.92
REMARK 500 3 GLN A 25 -73.22 67.17
REMARK 500 3 ASN A 31 36.21 -170.08
REMARK 500 3 GLN A 42 -39.08 -145.98
REMARK 500 3 LYS A 59 29.84 -147.04
REMARK 500 3 ARG A 60 -55.81 -125.28
REMARK 500 3 LYS A 63 -74.17 -89.42
REMARK 500 3 ASN A 80 84.73 -163.30
REMARK 500 3 GLU A 95 -171.08 59.42
REMARK 500 3 ASN A 98 152.73 61.66
REMARK 500 3 ASN A 119 35.60 34.23
REMARK 500 3 ASP A 128 174.81 -59.31
REMARK 500 3 ASN A 158 88.73 42.33
REMARK 500 3 ASP A 161 78.13 -100.47
REMARK 500 4 THR A 15 78.39 44.23
REMARK 500 4 ASN A 31 39.82 175.71
REMARK 500 4 GLN A 42 -45.25 -147.71
REMARK 500 4 ARG A 60 -68.14 -107.32
REMARK 500 4 SER A 61 -59.47 -173.69
REMARK 500 4 LEU A 78 -72.17 -109.00
REMARK 500 4 ASN A 80 67.20 -163.81
REMARK 500 4 ASP A 96 -45.16 -155.45
REMARK 500 4 ILE A 104 35.97 -150.30
REMARK 500 4 ASN A 119 33.97 34.67
REMARK 500
REMARK 500 THIS ENTRY HAS 241 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G3G RELATED DB: PDB
REMARK 900 1G3G IS THE NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53.
DBREF 1K3J A 14 164 UNP P22216 RAD53_YEAST 14 164
SEQRES 1 A 151 ALA THR GLN ARG PHE LEU ILE GLU LYS PHE SER GLN GLU
SEQRES 2 A 151 GLN ILE GLY GLU ASN ILE VAL CYS ARG VAL ILE CYS THR
SEQRES 3 A 151 THR GLY GLN ILE PRO ILE ARG ASP LEU SER ALA ASP ILE
SEQRES 4 A 151 SER GLN VAL LEU LYS GLU LYS ARG SER ILE LYS LYS VAL
SEQRES 5 A 151 TRP THR PHE GLY ARG ASN PRO ALA CYS ASP TYR HIS LEU
SEQRES 6 A 151 GLY ASN ILE SER ARG LEU SER ASN LYS HIS PHE GLN ILE
SEQRES 7 A 151 LEU LEU GLY GLU ASP GLY ASN LEU LEU LEU ASN ASP ILE
SEQRES 8 A 151 SER THR ASN GLY THR TRP LEU ASN GLY GLN LYS VAL GLU
SEQRES 9 A 151 LYS ASN SER ASN GLN LEU LEU SER GLN GLY ASP GLU ILE
SEQRES 10 A 151 THR VAL GLY VAL GLY VAL GLU SER ASP ILE LEU SER LEU
SEQRES 11 A 151 VAL ILE PHE ILE ASN ASP LYS PHE LYS GLN CYS LEU GLU
SEQRES 12 A 151 GLN ASN LYS VAL ASP ARG ILE ARG
HELIX 1 1 THR A 15 GLN A 25 1 11
HELIX 2 2 ASP A 51 GLU A 58 1 8
HELIX 3 3 ASN A 148 ASN A 158 1 11
SHEET 1 A 6 ARG A 46 SER A 49 0
SHEET 2 A 6 ILE A 32 ILE A 37 -1 N CYS A 34 O LEU A 48
SHEET 3 A 6 LEU A 141 ILE A 147 -1 O PHE A 146 N ARG A 35
SHEET 4 A 6 GLU A 129 VAL A 132 -1 N VAL A 132 O LEU A 141
SHEET 5 A 6 THR A 109 LEU A 111 -1 N TRP A 110 O THR A 131
SHEET 6 A 6 GLN A 114 LYS A 115 -1 O GLN A 114 N LEU A 111
SHEET 1 B 5 TYR A 76 HIS A 77 0
SHEET 2 B 5 LYS A 64 GLY A 69 1 N GLY A 69 O TYR A 76
SHEET 3 B 5 PHE A 89 LEU A 93 -1 O PHE A 89 N PHE A 68
SHEET 4 B 5 LEU A 99 ASP A 103 -1 O ASN A 102 N GLN A 90
SHEET 5 B 5 ASN A 121 LEU A 123 -1 O GLN A 122 N LEU A 101
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