Header list of 1q27.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 23-JUL-03 1Q27
TITLE NMR SOLUTION STRUCTURE OF DR0079: AN HYPOTHETICAL NUDIX PROTEIN FROM
TITLE 2 D. RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE NUDIX HYDROLASE DR0079;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MUTT/NUDIX FAMILY PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DR0079;
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: PET30B
KEYWDS NUDIX HYDROLASE, RADIATION RESISTANCE, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.W.BUCHKO,S.NI,S.R.HOLBROOK,M.A.KENNEDY
REVDAT 5 02-MAR-22 1Q27 1 REMARK
REVDAT 4 24-FEB-09 1Q27 1 VERSN
REVDAT 3 15-JUN-04 1Q27 1 JRNL
REVDAT 2 08-JUN-04 1Q27 1 JRNL
REVDAT 1 12-AUG-03 1Q27 0
JRNL AUTH G.W.BUCHKO,S.NI,S.R.HOLBROOK,M.A.KENNEDY
JRNL TITL SOLUTION STRUCTURE OF HYPOTHETICAL NUDIX HYDROLASE DR0079
JRNL TITL 2 FROM EXTREMELY RADIATION-RESISTANT DEINOCOCCUS RADIODURANS
JRNL TITL 3 BACTERIUM
JRNL REF PROTEINS V. 56 28 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 15162484
JRNL DOI 10.1002/PROT.20082
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.W.BUCHKO,S.NI,S.A.HOLBROOK,M.A.KENNEDY
REMARK 1 TITL 1H, 13C AND 15N NMR ASSIGNMENTS OF THE HYPOTHETICAL NUDIX
REMARK 1 TITL 2 PROTEIN DR0079 FROM THE EXTREMELY RADIATION-RESISTANT
REMARK 1 TITL 3 BACTERIUM DEINOCOCCUS RADIODURANS
REMARK 1 REF J.BIOMOL.NMR V. 25 169 2003
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1022243724501
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, CNS 1.1
REMARK 3 AUTHORS : GUENTERT (DYANA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DYANA USED FOR INITIAL REFINEMENTS.
REMARK 3 CNS USED FOR FINAL STRUCTURE CALCULATIONS WITH RDCS.
REMARK 4
REMARK 4 1Q27 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019822.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 7.1; 7.1
REMARK 210 IONIC STRENGTH : 100 MM KCL; 20 MM POTASSIUM
REMARK 210 PHOSPHATE; 100 MM KCL; 20 MM
REMARK 210 POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : ~2 MM DR0079; U-15N, 13C; 100 MM
REMARK 210 KCL, 20 MM POTASSIUM PHOSPHATE,
REMARK 210 2 MM DTT, PH 7.1; ~2 MM DR0079;
REMARK 210 U-15N, 13C; 100 MM KCL, 20 MM
REMARK 210 POTASSIUM PHOSPHATE, 2 MM DTT,
REMARK 210 PH 7.1, PF1 FILAMENTOUS PHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; IPAP-HSQC
REMARK 210 EXPERIEMENTS FOR RDCS
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, FELIX 97
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 225
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TEN BEST STRUCTURES, IN TERMS OF
REMARK 210 TOTAL AND NOE ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 6
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: 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 VAL A 4 174.20 -51.26
REMARK 500 1 SER A 5 -174.77 -177.75
REMARK 500 1 GLU A 7 123.42 62.95
REMARK 500 1 GLU A 14 -43.67 -162.54
REMARK 500 1 ARG A 15 -77.22 -88.31
REMARK 500 1 ASP A 16 33.35 -158.71
REMARK 500 1 GLU A 32 -46.44 -167.81
REMARK 500 1 SER A 44 18.13 58.00
REMARK 500 1 PHE A 60 113.25 -167.09
REMARK 500 1 VAL A 66 -172.33 -58.39
REMARK 500 1 SER A 74 -66.94 69.66
REMARK 500 1 GLU A 76 -37.29 -178.74
REMARK 500 1 LEU A 90 22.35 -151.79
REMARK 500 1 ILE A 94 27.97 42.65
REMARK 500 1 ASP A 95 20.86 -144.47
REMARK 500 1 LEU A 97 -87.47 -99.53
REMARK 500 1 SER A 98 125.31 171.85
REMARK 500 1 ALA A 103 -164.46 173.98
REMARK 500 1 SER A 106 -56.84 178.11
REMARK 500 1 PRO A 107 -72.33 -29.30
REMARK 500 1 PHE A 108 -38.32 -178.66
REMARK 500 1 THR A 111 99.32 63.89
REMARK 500 1 PRO A 127 -168.54 -76.30
REMARK 500 1 PHE A 129 98.00 -55.88
REMARK 500 1 ASN A 130 74.80 -158.43
REMARK 500 1 ILE A 134 99.76 -175.92
REMARK 500 1 LYS A 156 -158.16 -101.78
REMARK 500 1 ARG A 168 -70.65 -62.31
REMARK 500 1 GLU A 170 51.61 -116.86
REMARK 500 2 ASP A 6 88.18 60.73
REMARK 500 2 GLU A 14 -51.78 -127.68
REMARK 500 2 ARG A 15 -70.70 177.31
REMARK 500 2 THR A 25 44.24 -90.86
REMARK 500 2 PRO A 27 42.10 -84.76
REMARK 500 2 ARG A 30 97.78 54.55
REMARK 500 2 ARG A 33 30.29 -174.78
REMARK 500 2 SER A 54 138.82 -172.33
REMARK 500 2 SER A 56 -55.70 77.51
REMARK 500 2 LYS A 57 125.26 63.42
REMARK 500 2 ASN A 62 -65.18 66.78
REMARK 500 2 ALA A 63 156.24 75.48
REMARK 500 2 LEU A 64 177.86 -58.22
REMARK 500 2 GLU A 89 -75.09 -74.03
REMARK 500 2 ILE A 94 28.03 43.70
REMARK 500 2 SER A 98 105.91 65.58
REMARK 500 2 ARG A 100 99.55 -162.80
REMARK 500 2 ALA A 103 -168.96 166.73
REMARK 500 2 PRO A 107 100.59 -56.67
REMARK 500 2 PHE A 108 -43.47 -177.93
REMARK 500 2 GLN A 109 64.01 -166.59
REMARK 500
REMARK 500 THIS ENTRY HAS 310 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Q27 A 1 171 UNP Q9RY71 Y079_DEIRA 1 171
SEQRES 1 A 171 MET GLY GLY VAL SER ASP GLU ARG LEU ASP LEU VAL ASN
SEQRES 2 A 171 GLU ARG ASP GLU VAL VAL GLY GLN ILE LEU ARG THR ASP
SEQRES 3 A 171 PRO ALA LEU ARG TRP GLU ARG VAL ARG VAL VAL ASN ALA
SEQRES 4 A 171 PHE LEU ARG ASN SER GLN GLY GLN LEU TRP ILE PRO ARG
SEQRES 5 A 171 ARG SER PRO SER LYS SER LEU PHE PRO ASN ALA LEU ASP
SEQRES 6 A 171 VAL SER VAL GLY GLY ALA VAL GLN SER GLY GLU THR TYR
SEQRES 7 A 171 GLU GLU ALA PHE ARG ARG GLU ALA ARG GLU GLU LEU ASN
SEQRES 8 A 171 VAL GLU ILE ASP ALA LEU SER TRP ARG PRO LEU ALA SER
SEQRES 9 A 171 PHE SER PRO PHE GLN THR THR LEU SER SER PHE MET CYS
SEQRES 10 A 171 VAL TYR GLU LEU ARG SER ASP ALA THR PRO ILE PHE ASN
SEQRES 11 A 171 PRO ASN ASP ILE SER GLY GLY GLU TRP LEU THR PRO GLU
SEQRES 12 A 171 HIS LEU LEU ALA ARG ILE ALA ALA GLY GLU ALA ALA LYS
SEQRES 13 A 171 GLY ASP LEU ALA GLU LEU VAL ARG ARG CYS TYR ARG GLU
SEQRES 14 A 171 GLU GLU
HELIX 1 1 THR A 77 ASN A 91 1 15
HELIX 2 2 THR A 141 GLU A 153 1 13
HELIX 3 3 LYS A 156 ARG A 168 1 13
SHEET 1 A 2 ARG A 8 VAL A 12 0
SHEET 2 A 2 VAL A 18 LEU A 23 -1 O GLY A 20 N LEU A 11
SHEET 1 B 4 VAL A 68 ALA A 71 0
SHEET 2 B 4 ARG A 35 ASN A 43 -1 N VAL A 37 O GLY A 70
SHEET 3 B 4 PHE A 115 ARG A 122 1 O TYR A 119 N PHE A 40
SHEET 4 B 4 TRP A 99 PHE A 105 -1 N ARG A 100 O GLU A 120
SHEET 1 C 4 VAL A 68 ALA A 71 0
SHEET 2 C 4 ARG A 35 ASN A 43 -1 N VAL A 37 O GLY A 70
SHEET 3 C 4 GLN A 47 ILE A 50 -1 O GLN A 47 N ASN A 43
SHEET 4 C 4 GLU A 138 LEU A 140 -1 O GLU A 138 N ILE A 50
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