Header list of 1jkn.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 12-JUL-01 1JKN
TITLE SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE
TITLE 2 HYDROLASE FROM LUPINUS ANGUSTIFOLIUS COMPLEXED WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUPINUS ANGUSTIFOLIUS;
SOURCE 3 ORGANISM_COMMON: NARROW-LEAVED BLUE LUPINE;
SOURCE 4 ORGANISM_TAXID: 3871;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3
KEYWDS ALPHA-BETA-ALPHA SANDWICH, ENZYME-SUBSTRATE COMPLEX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR J.I.FLETCHER,J.D.SWARBRICK,D.MAKSEL,K.R.GAYLER,P.R.GOOLEY
REVDAT 4 23-FEB-22 1JKN 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JKN 1 VERSN
REVDAT 2 01-APR-03 1JKN 1 JRNL
REVDAT 1 27-FEB-02 1JKN 0
JRNL AUTH J.I.FLETCHER,J.D.SWARBRICK,D.MAKSEL,K.R.GAYLER,P.R.GOOLEY
JRNL TITL THE STRUCTURE OF AP(4)A HYDROLASE COMPLEXED WITH ATP-MGF(X)
JRNL TITL 2 REVEALS THE BASIS OF SUBSTRATE BINDING.
JRNL REF STRUCTURE V. 10 205 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 11839306
JRNL DOI 10.1016/S0969-2126(02)00696-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.D.SWARBRICK,T.BASHTANNYK,D.MAKSEL,X.-R.ZHANG,
REMARK 1 AUTH 2 G.M.BLACKBURN,K.R.GAYLER,P.R.GOOLEY
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF THE NUDIX ENZYME
REMARK 1 TITL 2 DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS
REMARK 1 TITL 3 ANGUSTIFOLIUS L
REMARK 1 REF J.MOL.BIOL. V. 302 1165 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.4085
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.2, DYANA 1.5, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, ET AL. (DYANA), BRUNGER
REMARK 3 ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2948 RESTRAINTS. 2649 ARE NOE-BASED DISTANCE RESTRAINTS, 299 ARE
REMARK 3 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1JKN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013881.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 120 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.6 MM U-15N, U-13C AP4A
REMARK 210 HYDROLASE 1.6 MM ATP 20 MM U-100%
REMARK 210 2H IMIDAZOLE 32 MM NAF 20 MM
REMARK 210 MGCL2; 1.6 MM U-15N, U-13C AP4A
REMARK 210 HYDROLASE 1.6 MM ATP 20 MM U-100%
REMARK 210 2H IMIDAZOLE 32 MM NAF 20 MM
REMARK 210 MGCL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_13C-SEPARATED_NOESY; 2D_DOUBLY-TUNED_13C_15N-FILTERED_NOESY;
REMARK 210 13C-EDITED_13C-FILTERED_NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.1, XEASY 1.4
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY, STRUCTURES WITH
REMARK 210 THE LEAST RESTRAINT VIOLATIONS,
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: DETERMINED USING STANDARD HETERONUCLEAR TECHNIQUES
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 CYS A 20 H PHE A 110 1.55
REMARK 500 O VAL A 88 H LEU A 92 1.58
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 MET A 6 111.97 -174.88
REMARK 500 1 SER A 8 137.50 -177.61
REMARK 500 1 LYS A 26 24.86 80.99
REMARK 500 1 PHE A 29 107.97 -59.75
REMARK 500 1 ILE A 47 159.63 51.95
REMARK 500 1 GLU A 49 99.28 -55.59
REMARK 500 1 ASP A 99 75.45 -112.89
REMARK 500 1 ASP A 124 38.74 -92.88
REMARK 500 2 SER A 5 121.71 -171.06
REMARK 500 2 SER A 8 130.73 174.64
REMARK 500 2 LYS A 26 24.77 81.74
REMARK 500 2 PHE A 29 109.58 -57.79
REMARK 500 2 ASP A 99 64.22 -109.75
REMARK 500 2 ASP A 124 38.72 -91.76
REMARK 500 3 SER A 5 -155.59 -108.08
REMARK 500 3 MET A 6 -40.33 -148.07
REMARK 500 3 SER A 8 131.70 171.88
REMARK 500 3 PHE A 29 108.61 -53.71
REMARK 500 3 GLU A 49 98.07 -55.19
REMARK 500 3 ASP A 116 -17.49 -48.97
REMARK 500 3 ASP A 124 38.83 -93.92
REMARK 500 3 SER A 126 -62.34 -102.24
REMARK 500 3 PRO A 129 -176.87 -51.69
REMARK 500 3 GLU A 130 -41.97 -150.10
REMARK 500 3 LYS A 150 16.28 -145.99
REMARK 500 4 LEU A 3 -178.53 60.18
REMARK 500 4 SER A 5 124.37 -173.14
REMARK 500 4 MET A 6 -38.31 -133.04
REMARK 500 4 SER A 8 138.98 174.33
REMARK 500 4 PHE A 29 109.58 -56.45
REMARK 500 4 GLU A 49 98.09 -53.60
REMARK 500 4 ASP A 99 65.23 -109.75
REMARK 500 4 ASP A 116 -16.69 -49.85
REMARK 500 4 ASP A 124 38.96 -93.75
REMARK 500 4 SER A 126 -68.28 -121.36
REMARK 500 4 PRO A 129 165.34 -48.44
REMARK 500 4 GLU A 130 -45.68 -150.05
REMARK 500 5 SER A 5 125.66 -179.57
REMARK 500 5 MET A 6 -24.70 -150.89
REMARK 500 5 ASP A 7 43.31 77.57
REMARK 500 5 SER A 8 121.54 -177.85
REMARK 500 5 GLU A 49 98.74 -67.26
REMARK 500 5 ASP A 99 73.82 -108.34
REMARK 500 5 ASP A 124 38.97 -91.98
REMARK 500 5 SER A 126 -69.96 -121.15
REMARK 500 6 PRO A 2 -168.73 -69.89
REMARK 500 6 LEU A 3 124.64 63.41
REMARK 500 6 SER A 5 -156.72 -124.13
REMARK 500 6 MET A 6 -33.65 -142.66
REMARK 500 6 SER A 8 125.64 178.24
REMARK 500
REMARK 500 THIS ENTRY HAS 256 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 166
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F3Y RELATED DB: PDB
REMARK 900 1F3Y CONTAINS THE SAME PROTEIN IN THE FREE FORM
DBREF 1JKN A 6 165 UNP O04841 O04841_LUPAN 40 199
SEQADV 1JKN GLY A 1 UNP O04841 CLONING ARTIFACT
SEQADV 1JKN PRO A 2 UNP O04841 CLONING ARTIFACT
SEQADV 1JKN LEU A 3 UNP O04841 CLONING ARTIFACT
SEQADV 1JKN GLY A 4 UNP O04841 CLONING ARTIFACT
SEQADV 1JKN SER A 5 UNP O04841 CLONING ARTIFACT
SEQRES 1 A 165 GLY PRO LEU GLY SER MET ASP SER PRO PRO GLU GLY TYR
SEQRES 2 A 165 ARG ARG ASN VAL GLY ILE CYS LEU MET ASN ASN ASP LYS
SEQRES 3 A 165 LYS ILE PHE ALA ALA SER ARG LEU ASP ILE PRO ASP ALA
SEQRES 4 A 165 TRP GLN MET PRO GLN GLY GLY ILE ASP GLU GLY GLU ASP
SEQRES 5 A 165 PRO ARG ASN ALA ALA ILE ARG GLU LEU ARG GLU GLU THR
SEQRES 6 A 165 GLY VAL THR SER ALA GLU VAL ILE ALA GLU VAL PRO TYR
SEQRES 7 A 165 TRP LEU THR TYR ASP PHE PRO PRO LYS VAL ARG GLU LYS
SEQRES 8 A 165 LEU ASN ILE GLN TRP GLY SER ASP TRP LYS GLY GLN ALA
SEQRES 9 A 165 GLN LYS TRP PHE LEU PHE LYS PHE THR GLY GLN ASP GLN
SEQRES 10 A 165 GLU ILE ASN LEU LEU GLY ASP GLY SER GLU LYS PRO GLU
SEQRES 11 A 165 PHE GLY GLU TRP SER TRP VAL THR PRO GLU GLN LEU ILE
SEQRES 12 A 165 ASP LEU THR VAL GLU PHE LYS LYS PRO VAL TYR LYS GLU
SEQRES 13 A 165 VAL LEU SER VAL PHE ALA PRO HIS LEU
HET ATP A 166 43
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 2 ATP C10 H16 N5 O13 P3
HELIX 1 1 ASP A 52 THR A 65 1 14
HELIX 2 2 PRO A 85 TRP A 96 1 12
HELIX 3 3 GLU A 140 THR A 146 1 7
HELIX 4 4 VAL A 147 PHE A 149 5 3
HELIX 5 5 LYS A 150 PHE A 161 1 12
HELIX 6 6 ALA A 162 LEU A 165 5 4
SHEET 1 A 4 ALA A 70 GLU A 75 0
SHEET 2 A 4 PHE A 108 PHE A 112 -1 N LEU A 109 O ALA A 74
SHEET 3 A 4 TYR A 13 MET A 22 1 O GLY A 18 N PHE A 108
SHEET 4 A 4 GLN A 44 GLY A 45 -1 O GLY A 45 N VAL A 17
SHEET 1 B 5 ALA A 70 GLU A 75 0
SHEET 2 B 5 PHE A 108 PHE A 112 -1 N LEU A 109 O ALA A 74
SHEET 3 B 5 TYR A 13 MET A 22 1 O GLY A 18 N PHE A 108
SHEET 4 B 5 GLY A 102 GLN A 105 1 O GLY A 102 N ARG A 14
SHEET 5 B 5 LEU A 80 ASP A 83 -1 N LEU A 80 O GLN A 105
SHEET 1 C 3 TRP A 40 GLN A 41 0
SHEET 2 C 3 ILE A 28 ARG A 33 -1 N ALA A 31 O GLN A 41
SHEET 3 C 3 PHE A 131 VAL A 137 -1 N GLY A 132 O SER A 32
SITE 1 AC1 13 ASN A 16 ARG A 33 GLN A 41 GLN A 44
SITE 2 AC1 13 TYR A 82 PHE A 84 VAL A 88 LYS A 91
SITE 3 AC1 13 TRP A 96 GLN A 103 VAL A 147 PHE A 149
SITE 4 AC1 13 LYS A 150
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