Header list of 1f3y.pdb file
Complete list - v 10 2 Bytes
HEADER HYDROLASE 06-JUN-00 1F3Y
TITLE SOLUTION STRUCTURE OF THE NUDIX ENZYME DIADENOSINE TETRAPHOSPHATE
TITLE 2 HYDROLASE FROM LUPINUS ANGUSTIFOLIUS L.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIADENOSINE 5',5'''-P1,P4-TETRAPHOSPHATE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 35-199;
COMPND 5 EC: 3.6.1.17;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-3
KEYWDS ENZYME, MIXED 4-STRANDED BETA SHEET, 2-STRANDED ANTIPARALLEL SHEET,
KEYWDS 2 ALPHA-BETA-ALPHA SANDWICH, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR J.D.SWARBRICK,T.BASHTANNYK,D.MAKSEL,X.R.ZHANG,G.M.BLACKBURN,
AUTHOR 2 K.R.GAYLER,P.R.GOOLEY
REVDAT 4 10-NOV-21 1F3Y 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1F3Y 1 VERSN
REVDAT 2 07-JAN-03 1F3Y 1 REMARK
REVDAT 1 06-JUN-01 1F3Y 0
JRNL AUTH J.D.SWARBRICK,T.BASHTANNYK,D.MAKSEL,X.R.ZHANG,G.M.BLACKBURN,
JRNL AUTH 2 K.R.GAYLER,P.R.GOOLEY
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF THE NUDIX ENZYME
JRNL TITL 2 DIADENOSINE TETRAPHOSPHATE HYDROLASE FROM LUPINUS
JRNL TITL 3 ANGUSTIFOLIUS L.
JRNL REF J.MOL.BIOL. V. 302 1165 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11183782
JRNL DOI 10.1006/JMBI.2000.4085
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, DYANA 1.5,1.4, CNS 0.9
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), GUENTERT (DYANA), BRUNGER
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F3Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011213.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298
REMARK 210 PH : 6.5; 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 50MM; 50MM; 50MM; 40MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9MM U-15N, 13C; HYDROLASE 50MM
REMARK 210 PHOSPHATE BUFFER, 1.5MM EDTA,
REMARK 210 3MM DTT; 0.9MM U-15N,13C;
REMARK 210 HYDROLASE 50MM PHOSPHATE BUFFER,
REMARK 210 1.3MM EDTA, 1.5MM EDTA,3MM DTT;
REMARK 210 1.2MM U-15N; HYDROLASE 50MM
REMARK 210 PHOSPHATE BUFFER, 1.5MM EDTA,
REMARK 210 3MM DTT; 1.2MM U-15N; HYDROLASE
REMARK 210 20MM IMIDAZOLE BUFFER, 20MM MGCL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED :
REMARK 210 CBCANH,CBCA(CO)NH,C(CO)NH_TOCSY,HNCO,(HCA)CO(CA)NH; HCACO,HCCH-
REMARK 210 TOCSY,13C-NOESY-HSQC,(HB)CB(CGCD)HD,(HB)CB(CGCDCE)HE,HACAHB,13C_
REMARK 210 CT_HEQC,; HNHB,HNHA,15N-TOCSY-HSQC,15N-NOESY-HSQC,15N-IPAP-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 : XEASY 1.3.13, VNMR 6.1 B
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVORABLE NON
REMARK 210 -BOND ENERGY,STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS,
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3
REMARK 210
REMARK 210 REMARK: NULL
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 ARG A 33 H ASP A 35 1.40
REMARK 500 H ILE A 28 O VAL A 137 1.46
REMARK 500 O ARG A 62 H GLY A 66 1.56
REMARK 500 O GLU A 71 H LYS A 111 1.58
REMARK 500 H SER A 32 O GLU A 133 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 SER A 5 -87.51 56.32
REMARK 500 1 MET A 6 127.39 64.59
REMARK 500 1 ARG A 15 106.44 -51.78
REMARK 500 1 ASN A 24 -5.74 -56.06
REMARK 500 1 LEU A 34 56.44 -55.49
REMARK 500 1 ASP A 35 -37.63 -177.35
REMARK 500 1 PRO A 43 152.73 -49.97
REMARK 500 1 GLN A 44 148.28 -177.80
REMARK 500 1 ASP A 48 -174.88 -69.17
REMARK 500 1 SER A 69 74.18 -61.55
REMARK 500 1 TRP A 79 -155.94 -92.62
REMARK 500 1 LEU A 80 105.31 -162.90
REMARK 500 1 PRO A 85 177.59 -57.94
REMARK 500 1 LEU A 92 -64.74 -120.29
REMARK 500 1 SER A 98 28.52 -171.85
REMARK 500 1 TRP A 100 -164.88 -67.14
REMARK 500 1 LYS A 101 0.90 165.45
REMARK 500 1 THR A 113 52.67 -98.39
REMARK 500 1 GLN A 117 -4.31 -56.70
REMARK 500 1 LEU A 121 26.82 42.91
REMARK 500 1 SER A 126 -13.93 80.86
REMARK 500 1 GLU A 127 -77.32 -91.51
REMARK 500 1 PRO A 129 -179.93 -65.87
REMARK 500 1 GLU A 130 -67.45 -95.06
REMARK 500 2 SER A 5 -98.13 70.08
REMARK 500 2 MET A 6 132.38 65.58
REMARK 500 2 ASN A 24 -5.63 -57.59
REMARK 500 2 GLN A 44 141.62 -170.57
REMARK 500 2 GLU A 49 -76.66 -46.92
REMARK 500 2 SER A 69 73.44 -62.41
REMARK 500 2 TYR A 82 37.07 -78.88
REMARK 500 2 ASP A 83 -110.03 25.30
REMARK 500 2 PHE A 84 -178.58 174.63
REMARK 500 2 PRO A 85 177.30 -55.21
REMARK 500 2 ARG A 89 -76.73 -58.84
REMARK 500 2 LEU A 92 -51.37 -121.88
REMARK 500 2 GLN A 95 -100.81 -79.16
REMARK 500 2 TRP A 96 29.84 40.90
REMARK 500 2 SER A 98 145.00 -175.38
REMARK 500 2 ASP A 99 84.40 58.15
REMARK 500 2 LYS A 101 6.83 167.51
REMARK 500 2 THR A 113 55.27 -95.77
REMARK 500 2 GLN A 117 -5.09 -57.65
REMARK 500 2 LEU A 121 -34.23 73.11
REMARK 500 2 GLU A 127 -47.98 -146.91
REMARK 500 2 GLU A 130 -72.77 -88.89
REMARK 500 2 PHE A 149 0.63 -57.07
REMARK 500 3 LEU A 3 120.91 63.52
REMARK 500 3 SER A 5 98.34 51.85
REMARK 500 3 TYR A 13 48.06 -98.55
REMARK 500
REMARK 500 THIS ENTRY HAS 652 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F3Y A 1 165 UNP O04841 O04841_LUPAN 35 199
SEQADV 1F3Y GLY A 1 UNP O04841 TYR 35 ENGINEERED MUTATION
SEQADV 1F3Y PRO A 2 UNP O04841 CYS 36 ENGINEERED MUTATION
SEQADV 1F3Y LEU A 3 UNP O04841 HIS 37 ENGINEERED MUTATION
SEQADV 1F3Y GLY A 4 UNP O04841 SER 38 ENGINEERED MUTATION
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
HELIX 1 1 ASP A 52 GLY A 66 1 15
HELIX 2 2 PRO A 85 LEU A 92 1 8
HELIX 3 3 ASN A 93 TRP A 96 5 4
HELIX 4 4 GLN A 115 ILE A 119 5 5
HELIX 5 5 THR A 138 THR A 146 1 9
HELIX 6 6 VAL A 147 PHE A 149 5 3
HELIX 7 7 LYS A 150 ALA A 162 1 13
HELIX 8 8 PRO A 163 LEU A 165 5 3
SHEET 1 A 4 GLN A 44 GLY A 46 0
SHEET 2 A 4 ASN A 16 MET A 22 -1 N VAL A 17 O GLY A 45
SHEET 3 A 4 GLN A 105 PHE A 112 1 O LYS A 106 N GLY A 18
SHEET 4 A 4 ALA A 70 GLU A 75 -1 O GLU A 71 N LYS A 111
SHEET 1 B 3 ILE A 36 GLN A 41 0
SHEET 2 B 3 ILE A 28 ARG A 33 -1 N ALA A 31 O GLN A 41
SHEET 3 B 3 PHE A 131 VAL A 137 -1 N GLY A 132 O SER A 32
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 - v 10 2 Bytes