Header list of 1jqr.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 08-AUG-01 1JQR TITLE NMR STRUCTURE OF THE AFRICAN SWINE FEVER VIRUS DNA POLYMERASE X COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA POLYMERASE BETA-LIKE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: DNA POLYMERASE X; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AFRICAN SWINE FEVER VIRUS; SOURCE 3 ORGANISM_TAXID: 10497; SOURCE 4 GENE: O174L; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-17B KEYWDS DNA POLYMERASE, VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR I.-J.L.BYEON,M.-I.SU,A.K.SHOWALTER,M.-D.TSAI REVDAT 4 23-FEB-22 1JQR 1 REMARK REVDAT 3 24-FEB-09 1JQR 1 VERSN REVDAT 2 01-APR-03 1JQR 1 JRNL REVDAT 1 26-OCT-01 1JQR 0 JRNL AUTH A.K.SHOWALTER,I.J.BYEON,M.I.SU,M.D.TSAI JRNL TITL SOLUTION STRUCTURE OF A VIRAL DNA POLYMERASE X AND EVIDENCE JRNL TITL 2 FOR A MUTAGENIC FUNCTION. JRNL REF NAT.STRUCT.BIOL. V. 8 942 2001 JRNL REFN ISSN 1072-8368 JRNL PMID 11685239 JRNL DOI 10.1038/NSB1101-942 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: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2597 RESTRAINTS, 2241 ARE REMARK 3 NOE-DERIVED DISTANCE RESTRAINTS, 244 TALOS-DERIVED DIHEDRAL ANGLE REMARK 3 RESTRAINTS, AND 112 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. REMARK 4 REMARK 4 1JQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-SEP-01. REMARK 100 THE DEPOSITION ID IS D_1000014079. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : 50 MM BORATE, 50 MM KCL, 1 MM REMARK 210 DTT, 1 MM EDTA REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM OR 1 MM PROTEIN U REMARK 210 -15N,13C; 50 MM BORATE, 50 MM REMARK 210 KCL, 1 MM DTT, 1 MM EDTA; 1 MM REMARK 210 PROTEIN U-15N,13C; 50 MM BORATE, REMARK 210 50 MM KCL, 1 MM DTT, 1 MM EDTA; REMARK 210 UNLABELED 0.5 MM PROTEIN; 50 MM REMARK 210 BORATE, 50 MM KCL, 1 MM DTT, 1 REMARK 210 MM EDTA; UNLABELED 0.5 MM REMARK 210 PROTEIN; 50 MM BORATE, 50 MM KCL, REMARK 210 1 MM DTT, 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; 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, X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 GLU A 21 O ASN A 68 1.50 REMARK 500 O LEU A 61 H VAL A 65 1.56 REMARK 500 O LYS A 136 H PHE A 143 1.57 REMARK 500 O ILE A 90 H TYR A 97 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 ARG A 17 26.40 -152.91 REMARK 500 1 LYS A 45 -70.29 -60.97 REMARK 500 1 PRO A 57 -78.80 -58.27 REMARK 500 1 ASN A 68 58.74 -115.05 REMARK 500 1 PRO A 119 -149.96 -78.34 REMARK 500 1 ASN A 134 51.62 78.22 REMARK 500 1 ASN A 138 135.34 172.00 REMARK 500 1 GLN A 139 75.88 -3.73 REMARK 500 1 TYR A 140 -31.74 166.63 REMARK 500 1 ASN A 145 -80.78 73.08 REMARK 500 1 GLN A 146 15.49 -154.70 REMARK 500 1 THR A 155 -87.53 70.61 REMARK 500 1 GLU A 156 -49.14 -172.29 REMARK 500 1 LYS A 172 36.61 -97.94 REMARK 500 1 ARG A 173 76.48 -111.48 REMARK 500 2 ARG A 17 26.88 -148.07 REMARK 500 2 ASN A 23 -84.59 73.83 REMARK 500 2 GLU A 43 38.72 32.28 REMARK 500 2 GLU A 44 170.19 -59.27 REMARK 500 2 PRO A 57 -80.23 -64.61 REMARK 500 2 ARG A 84 -31.12 89.76 REMARK 500 2 PRO A 119 -152.87 -75.69 REMARK 500 2 ASN A 134 40.44 83.15 REMARK 500 2 ASN A 138 137.86 170.41 REMARK 500 2 GLN A 139 75.32 -3.84 REMARK 500 2 TYR A 140 -32.82 168.20 REMARK 500 2 ASN A 145 -81.85 66.71 REMARK 500 2 GLN A 146 16.86 -155.67 REMARK 500 2 THR A 155 -91.07 73.11 REMARK 500 2 GLU A 156 -50.13 -166.08 REMARK 500 3 ARG A 17 27.65 -160.00 REMARK 500 3 GLU A 43 65.28 25.60 REMARK 500 3 LYS A 45 70.36 45.67 REMARK 500 3 MET A 46 -171.66 46.66 REMARK 500 3 ASN A 68 66.12 -117.52 REMARK 500 3 VAL A 80 -81.76 -135.85 REMARK 500 3 CYS A 81 151.47 61.40 REMARK 500 3 GLU A 83 -61.74 -154.92 REMARK 500 3 PRO A 119 -151.48 -77.12 REMARK 500 3 ASN A 134 48.47 80.29 REMARK 500 3 ASN A 138 132.17 179.41 REMARK 500 3 GLN A 139 76.29 -5.45 REMARK 500 3 TYR A 140 -31.75 168.10 REMARK 500 3 ASN A 145 -75.75 75.12 REMARK 500 3 GLN A 146 17.44 -154.02 REMARK 500 3 THR A 155 -87.73 54.91 REMARK 500 3 GLU A 156 -45.59 -172.93 REMARK 500 4 ARG A 17 16.77 -140.52 REMARK 500 4 GLU A 43 65.88 36.67 REMARK 500 4 PRO A 57 -71.12 -63.85 REMARK 500 REMARK 500 THIS ENTRY HAS 336 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1JQR A 1 174 UNP P42494 O174_ASFB7 1 174 SEQRES 1 A 174 MET LEU THR LEU ILE GLN GLY LYS LYS ILE VAL ASN HIS SEQRES 2 A 174 LEU ARG SER ARG LEU ALA PHE GLU TYR ASN GLY GLN LEU SEQRES 3 A 174 ILE LYS ILE LEU SER LYS ASN ILE VAL ALA VAL GLY SER SEQRES 4 A 174 LEU ARG ARG GLU GLU LYS MET LEU ASN ASP VAL ASP LEU SEQRES 5 A 174 LEU ILE ILE VAL PRO GLU LYS LYS LEU LEU LYS HIS VAL SEQRES 6 A 174 LEU PRO ASN ILE ARG ILE LYS GLY LEU SER PHE SER VAL SEQRES 7 A 174 LYS VAL CYS GLY GLU ARG LYS CYS VAL LEU PHE ILE GLU SEQRES 8 A 174 TRP GLU LYS LYS THR TYR GLN LEU ASP LEU PHE THR ALA SEQRES 9 A 174 LEU ALA GLU GLU LYS PRO TYR ALA ILE PHE HIS PHE THR SEQRES 10 A 174 GLY PRO VAL SER TYR LEU ILE ARG ILE ARG ALA ALA LEU SEQRES 11 A 174 LYS LYS LYS ASN TYR LYS LEU ASN GLN TYR GLY LEU PHE SEQRES 12 A 174 LYS ASN GLN THR LEU VAL PRO LEU LYS ILE THR THR GLU SEQRES 13 A 174 LYS GLU LEU ILE LYS GLU LEU GLY PHE THR TYR ARG ILE SEQRES 14 A 174 PRO LYS LYS ARG LEU HELIX 1 1 LEU A 4 ARG A 15 1 12 HELIX 2 2 LEU A 30 LYS A 32 5 3 HELIX 3 3 VAL A 37 ARG A 42 1 6 HELIX 4 4 LEU A 61 LEU A 66 1 6 HELIX 5 5 GLU A 107 GLY A 118 1 12 HELIX 6 6 PRO A 119 LYS A 132 1 14 HELIX 7 7 GLU A 156 GLY A 164 1 9 HELIX 8 8 ILE A 169 ARG A 173 5 5 SHEET 1 A 2 LEU A 2 THR A 3 0 SHEET 2 A 2 MET A 46 LEU A 47 -1 O LEU A 47 N LEU A 2 SHEET 1 B 3 GLN A 25 LYS A 28 0 SHEET 2 B 3 LEU A 18 TYR A 22 -1 N PHE A 20 O ILE A 27 SHEET 3 B 3 ILE A 69 ILE A 71 -1 O ARG A 70 N ALA A 19 SHEET 1 C 5 ILE A 34 ALA A 36 0 SHEET 2 C 5 VAL A 50 VAL A 56 -1 O LEU A 53 N VAL A 35 SHEET 3 C 5 LYS A 95 LEU A 105 1 O PHE A 102 N ILE A 54 SHEET 4 C 5 LYS A 85 TRP A 92 -1 N ILE A 90 O TYR A 97 SHEET 5 C 5 SER A 75 CYS A 81 -1 N VAL A 80 O VAL A 87 SHEET 1 D 3 TYR A 135 ASN A 138 0 SHEET 2 D 3 GLY A 141 LYS A 144 -1 O PHE A 143 N LYS A 136 SHEET 3 D 3 THR A 147 LEU A 148 -1 O THR A 147 N LYS A 144 SSBOND 1 CYS A 81 CYS A 86 1555 1555 2.03 CISPEP 1 GLY A 118 PRO A 119 1 0.15 CISPEP 2 GLY A 118 PRO A 119 2 0.06 CISPEP 3 GLY A 118 PRO A 119 3 0.14 CISPEP 4 GLY A 118 PRO A 119 4 0.18 CISPEP 5 GLY A 118 PRO A 119 5 0.18 CISPEP 6 GLY A 118 PRO A 119 6 -0.03 CISPEP 7 GLY A 118 PRO A 119 7 0.16 CISPEP 8 GLY A 118 PRO A 119 8 0.04 CISPEP 9 GLY A 118 PRO A 119 9 0.09 CISPEP 10 GLY A 118 PRO A 119 10 0.08 CISPEP 11 GLY A 118 PRO A 119 11 0.02 CISPEP 12 GLY A 118 PRO A 119 12 0.10 CISPEP 13 GLY A 118 PRO A 119 13 0.04 CISPEP 14 GLY A 118 PRO A 119 14 0.11 CISPEP 15 GLY A 118 PRO A 119 15 0.14 CISPEP 16 GLY A 118 PRO A 119 16 0.09 CISPEP 17 GLY A 118 PRO A 119 17 0.10 CISPEP 18 GLY A 118 PRO A 119 18 0.13 CISPEP 19 GLY A 118 PRO A 119 19 0.07 CISPEP 20 GLY A 118 PRO A 119 20 -0.06 CISPEP 21 GLY A 118 PRO A 119 21 0.16 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