Header list of 1qkl.pdb file
Complete list - r 19 2 Bytes
HEADER RNA POLYMERASE 26-JUL-99 1QKL TITLE HRPABC14.4, ESSENTIAL SUBUNIT OF HUMAN RNA POLYMERASES I, II AND III COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 14.4 KD POLYPEPTIDE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RPB6; COMPND 5 EC: 2.7.7.6; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 ORGAN: HUMAN FETAL BRAIN; SOURCE 6 CELLULAR_LOCATION: NUCLEUS; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-6H2 KEYWDS RNA POLYMERASE, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR F.DEL RIO-PORTILLA,A.G.GASKELL,D.GILBERT,J.A.A.LADIAS,G.WAGNER REVDAT 6 19-APR-17 1QKL 1 REMARK ATOM REVDAT 5 24-FEB-09 1QKL 1 VERSN REVDAT 4 26-MAY-04 1QKL 1 AUTHOR JRNL ATOM MODEL REVDAT 3 20-SEP-00 1QKL 1 ENDMDL REVDAT 2 14-NOV-99 1QKL 1 ATOM REVDAT 1 07-NOV-99 1QKL 0 JRNL AUTH F.DEL RIO-PORTILLA,A.G.GASKELL,D.GILBERT,J.A.A.LADIAS, JRNL AUTH 2 G.WAGNER JRNL TITL SOLUTION STRUCTURE OF THE HRPABC14.4 SUBUNIT OF HUMAN RNA JRNL TITL 2 POLYMERASES JRNL REF NAT.STRUCT.BIOL. V. 6 1039 1999 JRNL REFN ISSN 1072-8368 JRNL PMID 10542096 JRNL DOI 10.1038/14923 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES 801-832 ARE DISORDERED REMARK 4 REMARK 4 1QKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-99. REMARK 100 THE PDBE ID CODE IS EBI-2977. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS TRIPLE RESONANCE & NOES REMARK 210 EXPERIMENTS REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITY; INOVA; AMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX, XEASY, X-PLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 75 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE REMARK 210 EXPERIMENTS ON 13C AND 15N-LABELED HRPABC14.4 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 MET A 894 H LYS A 898 1.44 REMARK 500 O LEU A 891 H LYS A 895 1.49 REMARK 500 O THR A 854 H TYR A 856 1.50 REMARK 500 O VAL A 865 H ARG A 869 1.50 REMARK 500 O ASN A 835 H TYR A 909 1.51 REMARK 500 O ARG A 864 H THR A 868 1.56 REMARK 500 O ARG A 869 H ILE A 873 1.57 REMARK 500 O ILE A 906 O TRP A 918 2.17 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 802 61.63 -116.05 REMARK 500 1 ASN A 807 -144.53 -150.14 REMARK 500 1 PHE A 808 31.74 -143.78 REMARK 500 1 ASP A 809 79.36 -156.55 REMARK 500 1 ASP A 812 41.09 -104.54 REMARK 500 1 PHE A 813 38.96 -143.73 REMARK 500 1 GLU A 817 23.84 -149.06 REMARK 500 1 LEU A 822 -81.87 -166.72 REMARK 500 1 ASP A 824 29.19 -164.21 REMARK 500 1 LEU A 825 66.86 -117.35 REMARK 500 1 ASN A 827 40.15 35.46 REMARK 500 1 ALA A 828 -79.16 -69.38 REMARK 500 1 GLU A 829 -81.52 -120.18 REMARK 500 1 GLU A 830 17.10 55.39 REMARK 500 1 GLN A 833 87.39 -177.51 REMARK 500 1 GLU A 834 115.82 -160.11 REMARK 500 1 SER A 841 142.07 -32.86 REMARK 500 1 PRO A 845 62.91 -67.61 REMARK 500 1 GLN A 846 -35.15 -170.02 REMARK 500 1 ASN A 848 97.36 -52.01 REMARK 500 1 LYS A 850 153.52 176.96 REMARK 500 1 ARG A 851 -66.21 178.06 REMARK 500 1 ILE A 852 -18.10 -150.09 REMARK 500 1 THR A 853 104.61 -55.77 REMARK 500 1 PRO A 855 68.93 -56.60 REMARK 500 1 TYR A 856 105.14 169.23 REMARK 500 1 LYS A 859 -36.13 -22.60 REMARK 500 1 CYS A 876 -89.02 -133.56 REMARK 500 1 ALA A 877 85.40 166.22 REMARK 500 1 PRO A 878 -8.99 -56.73 REMARK 500 1 VAL A 879 -177.80 -52.05 REMARK 500 1 VAL A 881 -75.87 -118.78 REMARK 500 1 GLU A 882 69.02 -105.03 REMARK 500 1 THR A 887 20.01 -157.06 REMARK 500 1 PRO A 889 -9.46 -54.20 REMARK 500 1 LEU A 890 1.96 179.58 REMARK 500 1 ILE A 902 55.97 28.70 REMARK 500 1 SER A 914 -168.94 -169.49 REMARK 500 1 TYR A 915 157.68 172.46 REMARK 500 1 TRP A 918 175.29 139.28 REMARK 500 1 LEU A 923 -152.04 -149.32 REMARK 500 1 ILE A 925 -128.63 -95.01 REMARK 500 2 SER A 802 -157.23 -113.65 REMARK 500 2 ASP A 803 102.03 -59.79 REMARK 500 2 ASP A 806 77.20 -110.80 REMARK 500 2 ASN A 807 53.31 -69.79 REMARK 500 2 PHE A 808 -69.33 -137.04 REMARK 500 2 ASP A 809 -76.91 -148.91 REMARK 500 2 ASP A 811 -169.67 -108.34 REMARK 500 2 ASP A 812 41.39 -104.64 REMARK 500 REMARK 500 THIS ENTRY HAS 876 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 1 ARG A 844 0.30 SIDE CHAIN REMARK 500 1 ARG A 851 0.27 SIDE CHAIN REMARK 500 1 ARG A 862 0.19 SIDE CHAIN REMARK 500 1 ARG A 864 0.32 SIDE CHAIN REMARK 500 1 ARG A 869 0.21 SIDE CHAIN REMARK 500 1 ARG A 900 0.32 SIDE CHAIN REMARK 500 1 ARG A 907 0.32 SIDE CHAIN REMARK 500 1 ARG A 908 0.16 SIDE CHAIN REMARK 500 2 ARG A 844 0.26 SIDE CHAIN REMARK 500 2 ARG A 851 0.24 SIDE CHAIN REMARK 500 2 ARG A 862 0.18 SIDE CHAIN REMARK 500 2 ARG A 864 0.32 SIDE CHAIN REMARK 500 2 ARG A 869 0.20 SIDE CHAIN REMARK 500 2 ARG A 900 0.31 SIDE CHAIN REMARK 500 2 ARG A 907 0.30 SIDE CHAIN REMARK 500 2 ARG A 908 0.13 SIDE CHAIN REMARK 500 3 ARG A 844 0.29 SIDE CHAIN REMARK 500 3 ARG A 851 0.21 SIDE CHAIN REMARK 500 3 ARG A 862 0.31 SIDE CHAIN REMARK 500 3 ARG A 864 0.25 SIDE CHAIN REMARK 500 3 ARG A 869 0.26 SIDE CHAIN REMARK 500 3 ARG A 900 0.32 SIDE CHAIN REMARK 500 3 ARG A 907 0.32 SIDE CHAIN REMARK 500 3 ARG A 908 0.26 SIDE CHAIN REMARK 500 4 ARG A 844 0.32 SIDE CHAIN REMARK 500 4 ARG A 851 0.23 SIDE CHAIN REMARK 500 4 ARG A 862 0.30 SIDE CHAIN REMARK 500 4 ARG A 864 0.31 SIDE CHAIN REMARK 500 4 ARG A 869 0.20 SIDE CHAIN REMARK 500 4 ARG A 900 0.27 SIDE CHAIN REMARK 500 4 ARG A 907 0.31 SIDE CHAIN REMARK 500 4 ARG A 908 0.22 SIDE CHAIN REMARK 500 5 ARG A 844 0.24 SIDE CHAIN REMARK 500 5 ARG A 851 0.24 SIDE CHAIN REMARK 500 5 ARG A 862 0.29 SIDE CHAIN REMARK 500 5 ARG A 864 0.28 SIDE CHAIN REMARK 500 5 ARG A 869 0.17 SIDE CHAIN REMARK 500 5 ARG A 900 0.23 SIDE CHAIN REMARK 500 5 ARG A 907 0.30 SIDE CHAIN REMARK 500 5 ARG A 908 0.18 SIDE CHAIN REMARK 500 6 ARG A 844 0.25 SIDE CHAIN REMARK 500 6 ARG A 851 0.32 SIDE CHAIN REMARK 500 6 ARG A 862 0.30 SIDE CHAIN REMARK 500 6 ARG A 864 0.32 SIDE CHAIN REMARK 500 6 ARG A 869 0.21 SIDE CHAIN REMARK 500 6 ARG A 900 0.26 SIDE CHAIN REMARK 500 6 ARG A 907 0.25 SIDE CHAIN REMARK 500 6 ARG A 908 0.24 SIDE CHAIN REMARK 500 7 ARG A 844 0.24 SIDE CHAIN REMARK 500 7 ARG A 851 0.30 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 174 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1QKL A 801 927 UNP P41584 RPB6_HUMAN 1 127 SEQRES 1 A 127 MET SER ASP ASN GLU ASP ASN PHE ASP GLY ASP ASP PHE SEQRES 2 A 127 ASP ASP VAL GLU GLU ASP GLU GLY LEU ASP ASP LEU GLU SEQRES 3 A 127 ASN ALA GLU GLU GLU GLY GLN GLU ASN VAL GLU ILE LEU SEQRES 4 A 127 PRO SER GLY GLU ARG PRO GLN ALA ASN GLN LYS ARG ILE SEQRES 5 A 127 THR THR PRO TYR MET THR LYS TYR GLU ARG ALA ARG VAL SEQRES 6 A 127 LEU GLY THR ARG ALA LEU GLN ILE ALA MET CYS ALA PRO SEQRES 7 A 127 VAL MET VAL GLU LEU GLU GLY GLU THR ASP PRO LEU LEU SEQRES 8 A 127 ILE ALA MET LYS GLU LEU LYS ALA ARG LYS ILE PRO ILE SEQRES 9 A 127 ILE ILE ARG ARG TYR LEU PRO ASP GLY SER TYR GLU ASP SEQRES 10 A 127 TRP GLY VAL ASP GLU LEU ILE ILE THR ASP HELIX 1 1 LYS A 859 MET A 875 1 17 HELIX 2 2 LEU A 890 ARG A 900 1 11 SHEET 1 A 3 ASN A 835 PRO A 840 0 SHEET 2 A 3 ILE A 904 LEU A 910 -1 N ILE A 905 O LEU A 839 SHEET 3 A 3 SER A 914 TRP A 918 -1 N SER A 914 O LEU A 910 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 19 2 Bytes