Header list of 1ojg.pdb file
Complete list - n 17 2 Bytes
HEADER TRANSFERASE 10-JUL-03 1OJG TITLE SENSORY DOMAIN OF THE MEMBRANEOUS TWO-COMPONENT FUMARATE SENSOR DCUS TITLE 2 OF E. COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: SENSOR PROTEIN DCUS; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FUMARATE SENSORY DOMAIN, RESIDUES 45-180; COMPND 5 SYNONYM: DCUS; COMPND 6 EC: 2.7.3.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 469008; SOURCE 4 STRAIN: BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMW145 KEYWDS TRANSFERASE, FUMARATE, DCUS, HISTIDINE KINASE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR L.PAPPALARDO,I.G.JANAUSCH,V.VIJAYAN,E.ZIENTZ,J.JUNKER,W.PETI, AUTHOR 2 M.ZWECKSTETTER,G.UNDEN,C.GRIESINGER REVDAT 4 17-JAN-18 1OJG 1 TITLE SOURCE JRNL REVDAT 3 24-FEB-09 1OJG 1 VERSN REVDAT 2 02-OCT-03 1OJG 1 JRNL REVDAT 1 15-AUG-03 1OJG 0 JRNL AUTH L.PAPPALARDO,I.G.JANAUSCH,V.VIJAYAN,E.ZIENTZ,J.JUNKER, JRNL AUTH 2 W.PETI,M.ZWECKSTETTER,G.UNDEN,C.GRIESINGER JRNL TITL THE NMR STRUCTURE OF THE SENSORY DOMAIN OF THE MEMBRANOUS JRNL TITL 2 TWO-COMPONENT FUMARATE SENSOR (HISTIDINE PROTEIN KINASE) JRNL TITL 3 DCUS OF ESCHERICHIA COLI. JRNL REF J. BIOL. CHEM. V. 278 39185 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12907689 JRNL DOI 10.1074/JBC.C300344200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR-NIH REMARK 3 AUTHORS : BRUNGER, CLORE, TJ REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OJG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1290012986. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-HSQC; NOESY-HSQC; TOCSY REMARK 210 -HSQC; HSQC-NOESY-HSQC; HNCO; REMARK 210 CBCA(CO)NH; HNCACB; CC(CO)NH; REMARK 210 HBHACONH; HCCH-COSY; HCCH- REMARK 210 ADIABATIC TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 700 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, XEASY, X-PLOR REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME; REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 470 MODELS 1-10 REMARK 470 RES CSSEQI ATOMS REMARK 470 ARG A 180 O 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 ALA A 84 H GLU A 87 1.15 REMARK 500 O ILE A 85 H ALA A 88 1.19 REMARK 500 O ILE A 69 H GLY A 72 1.32 REMARK 500 HD1 HIS A 110 H GLU A 112 1.33 REMARK 500 O GLY A 72 H LYS A 75 1.38 REMARK 500 O ALA A 128 H GLY A 131 1.46 REMARK 500 O ALA A 84 N GLU A 87 2.04 REMARK 500 O ILE A 85 N ALA A 88 2.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 5 VAL A 100 N - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 10 TYR A 153 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES 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 66 -152.83 -66.38 REMARK 500 1 ILE A 69 -78.46 -56.44 REMARK 500 1 LYS A 75 -158.15 -122.73 REMARK 500 1 PRO A 77 -73.53 -38.59 REMARK 500 1 SER A 80 -154.78 -66.97 REMARK 500 1 ARG A 92 -81.67 -57.80 REMARK 500 1 ASN A 93 27.40 -148.33 REMARK 500 1 ASP A 94 -1.34 70.74 REMARK 500 1 LEU A 96 170.69 152.91 REMARK 500 1 ASP A 102 -168.07 -74.18 REMARK 500 1 GLN A 104 107.93 -170.89 REMARK 500 1 LEU A 106 142.27 153.50 REMARK 500 1 HIS A 110 140.12 169.86 REMARK 500 1 ILE A 116 -82.79 -51.69 REMARK 500 1 GLN A 118 -70.50 -80.79 REMARK 500 1 PRO A 119 117.60 -29.91 REMARK 500 1 PHE A 120 149.86 -175.37 REMARK 500 1 LYS A 121 11.32 48.95 REMARK 500 1 ASP A 123 -11.88 62.71 REMARK 500 1 LEU A 126 -32.62 -38.50 REMARK 500 1 GLU A 132 140.47 167.75 REMARK 500 1 LEU A 142 -11.17 62.70 REMARK 500 1 ASP A 154 -2.41 -58.87 REMARK 500 1 GLU A 155 21.52 98.25 REMARK 500 1 ASN A 156 19.13 -140.78 REMARK 500 1 LEU A 169 152.18 73.66 REMARK 500 1 SER A 170 -104.81 151.30 REMARK 500 1 ARG A 171 79.34 -53.04 REMARK 500 1 VAL A 172 -25.83 -175.12 REMARK 500 2 SER A 66 -161.10 -76.61 REMARK 500 2 ILE A 69 -73.39 -58.71 REMARK 500 2 LYS A 75 -150.58 -134.97 REMARK 500 2 PRO A 77 -16.10 -29.00 REMARK 500 2 SER A 80 -156.75 -68.57 REMARK 500 2 ILE A 82 -7.97 -49.55 REMARK 500 2 ARG A 92 -93.63 -76.33 REMARK 500 2 ASN A 93 31.12 -144.44 REMARK 500 2 LEU A 96 176.77 164.62 REMARK 500 2 MET A 103 72.35 -66.89 REMARK 500 2 GLN A 104 -52.24 -140.70 REMARK 500 2 SER A 105 137.29 97.38 REMARK 500 2 LEU A 106 95.80 157.44 REMARK 500 2 ARG A 107 94.01 -39.43 REMARK 500 2 HIS A 110 149.68 -174.44 REMARK 500 2 ILE A 116 -88.05 -56.00 REMARK 500 2 GLN A 118 -72.42 -69.64 REMARK 500 2 PRO A 119 120.07 -24.95 REMARK 500 2 PHE A 120 138.12 -178.11 REMARK 500 2 LYS A 121 4.98 50.47 REMARK 500 2 ASP A 123 -17.98 71.04 REMARK 500 REMARK 500 THIS ENTRY HAS 321 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. DBREF 1OJG A 45 180 UNP P39272 DCUS_ECOLI 45 180 SEQRES 1 A 136 SER ASP MET THR ARG ASP GLY LEU ALA ASN LYS ALA LEU SEQRES 2 A 136 ALA VAL ALA ARG THR LEU ALA ASP SER PRO GLU ILE ARG SEQRES 3 A 136 GLN GLY LEU GLN LYS LYS PRO GLN GLU SER GLY ILE GLN SEQRES 4 A 136 ALA ILE ALA GLU ALA VAL ARG LYS ARG ASN ASP LEU LEU SEQRES 5 A 136 PHE ILE VAL VAL THR ASP MET GLN SER LEU ARG TYR SER SEQRES 6 A 136 HIS PRO GLU ALA GLN ARG ILE GLY GLN PRO PHE LYS GLY SEQRES 7 A 136 ASP ASP ILE LEU LYS ALA LEU ASN GLY GLU GLU ASN VAL SEQRES 8 A 136 ALA ILE ASN ARG GLY PHE LEU ALA GLN ALA LEU ARG VAL SEQRES 9 A 136 PHE THR PRO ILE TYR ASP GLU ASN HIS LYS GLN ILE GLY SEQRES 10 A 136 VAL VAL ALA ILE GLY LEU GLU LEU SER ARG VAL THR GLN SEQRES 11 A 136 GLN ILE ASN ASP SER ARG HELIX 1 1 SER A 45 ALA A 64 1 20 HELIX 2 2 PRO A 67 GLN A 74 1 8 HELIX 3 3 LYS A 76 SER A 80 5 5 HELIX 4 4 ALA A 84 ASP A 94 1 11 HELIX 5 5 ALA A 113 GLY A 117 5 5 HELIX 6 6 ASP A 124 LEU A 129 1 6 HELIX 7 7 VAL A 172 SER A 179 1 8 SHEET 1 AA 4 PHE A 97 THR A 101 0 SHEET 2 AA 4 GLN A 159 LEU A 167 -1 O VAL A 162 N THR A 101 SHEET 3 AA 4 ALA A 145 TYR A 153 -1 O LEU A 146 N LEU A 167 SHEET 4 AA 4 ASN A 134 ASN A 138 -1 O ASN A 134 N PHE A 149 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 - n 17 2 Bytes