Header list of 1yx3.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-FEB-05 1YX3 TITLE NMR STRUCTURE OF ALLOCHROMATIUM VINOSUM DSRC: NORTHEAST STRUCTURAL TITLE 2 GENOMICS CONSORTIUM TARGET OP4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN DSRC; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALLOCHROMATIUM VINOSUM; SOURCE 3 ORGANISM_TAXID: 1049; SOURCE 4 GENE: DSRC; 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: PET15B KEYWDS STRUCTURAL GENOMICS, DSRC, DISSIMILATORY SULFITE REDUCTASE, GAMMA KEYWDS 2 SUBUNIT, DSVC, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.R.CORT,C.DAHL,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL AUTHOR 2 GENOMICS CONSORTIUM (NESG) REVDAT 5 02-MAR-22 1YX3 1 REMARK SEQADV REVDAT 4 24-FEB-09 1YX3 1 VERSN REVDAT 3 30-SEP-08 1YX3 1 JRNL REVDAT 2 26-APR-05 1YX3 1 JRNL AUTHOR REVDAT 1 19-APR-05 1YX3 0 JRNL AUTH J.R.CORT,U.SELAN,A.SCHULTE,F.GRIMM,M.A.KENNEDY,C.DAHL JRNL TITL ALLOCHROMATIUM VINOSUM DSRC: SOLUTION-STATE NMR STRUCTURE, JRNL TITL 2 REDOX PROPERTIES, AND INTERACTION WITH DSREFH, A PROTEIN JRNL TITL 3 ESSENTIAL FOR PURPLE SULFUR BACTERIAL SULFUR OXIDATION. JRNL REF J.MOL.BIOL. V. 382 692 2008 JRNL REFN ISSN 0022-2836 JRNL PMID 18656485 JRNL DOI 10.1016/J.JMB.2008.07.022 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.DAHL,S.ENGELS,A.S.POTT-SPERLING,A.SCHULTE,J.SANDER, REMARK 1 AUTH 2 Y.LUBBE,O.DEUSTER,D.C.BRUNE REMARK 1 TITL NOVEL GENES OF THE DSR GENE CLUSTER AND EVIDENCE FOR CLOSE REMARK 1 TITL 2 INTERACTION OF DSR PROTEINS DURING SULFUR OXIDATION IN THE REMARK 1 TITL 3 PHOTOTROPHIC SULFUR BACTERIUM ALLOCHROMATIUM VINOSUM. REMARK 1 REF J.BACTERIOL. V. 187 1392 2005 REMARK 1 REFN ISSN 0021-9193 REMARK 1 PMID 15687204 REMARK 1 DOI 10.1128/JB.187.4.1392-1404.2005 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.S.POTT,C.DAHL REMARK 1 TITL SIROHAEM SULFITE REDUCTASE AND OTHER PROTEINS ENCODED BY REMARK 1 TITL 2 GENES AT THE DSR LOCUS OF CHROMATIUM VINOSUM ARE INVOLVED IN REMARK 1 TITL 3 THE OXIDATION OF INTRACELLULAR SULFUR. REMARK 1 REF MICROBIOLOGY V. 144 1881 1998 REMARK 1 REFN ISSN 0026-2617 REMARK 1 PMID 9695921 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR NIH-XPLOR REMARK 3 AUTHORS : BRUNGER,CLORE,KUSZEWSKI,SCHWIETERS,TJANDRA REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1YX3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-05. REMARK 100 THE DEPOSITION ID IS D_1000032021. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 500 MM NACL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1 MM U-13C, 15N DSRC, 500 MM REMARK 210 NACL, 50 MM SODIUM PHOSPHATE, 5 REMARK 210 MM DTT; 1 MM U-13C, 15N DSRC, REMARK 210 500 MM NACL, 50 MM SODIUM REMARK 210 PHOSPHATE, 5 MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; REMARK 210 3D_13N,15N-SEPARATED_SIMULTANEOUS_NOESY; 4D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.106, AUTOSTRUCTURE REMARK 210 2.1.0, TALOS 2003 REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 25 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGY STRUCTURES WITH REMARK 210 FEWEST RESTRAINT VIOLATIONS 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 MET A -19 REMARK 465 GLY A -18 REMARK 465 SER A -17 REMARK 465 SER A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 HIS A -10 REMARK 465 SER A -9 REMARK 465 SER A -8 REMARK 465 GLY A -7 REMARK 465 LEU A -6 REMARK 465 VAL A -5 REMARK 465 PRO A -4 REMARK 465 ARG A -3 REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 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 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 ALA A 2 131.40 72.09 REMARK 500 1 LEU A 23 38.29 -85.76 REMARK 500 1 ASP A 25 -86.32 -159.37 REMARK 500 1 TRP A 26 109.75 67.53 REMARK 500 1 GLU A 80 35.65 -148.08 REMARK 500 1 PRO A 95 -70.21 -41.55 REMARK 500 2 LEU A 23 35.87 -97.51 REMARK 500 2 ASP A 25 -64.32 -138.50 REMARK 500 2 TRP A 26 124.36 71.91 REMARK 500 2 LEU A 77 39.10 -90.59 REMARK 500 2 LYS A 79 -82.80 -141.08 REMARK 500 2 LYS A 81 -53.38 -128.37 REMARK 500 2 SER A 84 -67.50 -159.64 REMARK 500 2 THR A 109 -52.76 66.75 REMARK 500 3 ALA A 2 174.48 64.57 REMARK 500 3 ASN A 24 -49.33 -154.98 REMARK 500 3 ASP A 25 -73.42 -114.20 REMARK 500 3 TRP A 26 118.40 66.41 REMARK 500 3 LYS A 79 -34.80 -146.11 REMARK 500 4 ASP A 8 -70.88 70.36 REMARK 500 4 ASP A 25 -50.49 -137.41 REMARK 500 4 TRP A 26 120.27 68.56 REMARK 500 4 LYS A 79 -169.37 -111.99 REMARK 500 4 LYS A 81 87.31 -151.30 REMARK 500 4 SER A 84 -88.57 55.34 REMARK 500 4 PRO A 106 -166.83 -75.08 REMARK 500 5 ALA A 2 -147.43 -98.44 REMARK 500 5 ASP A 8 72.62 55.52 REMARK 500 5 ASP A 25 -79.94 179.91 REMARK 500 5 TRP A 26 104.97 60.22 REMARK 500 5 GLU A 80 -85.90 68.80 REMARK 500 5 LYS A 81 -61.69 66.14 REMARK 500 5 LYS A 107 108.19 -51.22 REMARK 500 5 THR A 109 -55.60 73.17 REMARK 500 6 ASP A 25 -67.42 -152.67 REMARK 500 6 TRP A 26 123.08 69.92 REMARK 500 6 GLU A 59 -60.43 -93.63 REMARK 500 6 LYS A 81 -72.89 -88.58 REMARK 500 6 SER A 84 -85.68 -165.41 REMARK 500 6 PRO A 108 -61.88 -91.14 REMARK 500 6 THR A 109 -70.45 70.08 REMARK 500 7 ALA A 2 144.82 73.01 REMARK 500 7 ASP A 8 -69.67 69.00 REMARK 500 7 LEU A 20 108.89 -57.10 REMARK 500 7 SER A 21 72.53 -109.41 REMARK 500 7 ASN A 22 -39.25 -167.94 REMARK 500 7 LEU A 23 -118.03 55.69 REMARK 500 7 ASN A 24 -74.61 65.06 REMARK 500 7 TRP A 26 113.61 69.97 REMARK 500 7 ASN A 83 -73.42 65.84 REMARK 500 REMARK 500 THIS ENTRY HAS 143 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: OP4 RELATED DB: TARGETDB DBREF 1YX3 A 1 112 UNP O87899 O87899_CHRVI 1 112 SEQADV 1YX3 MET A -19 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 GLY A -18 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 SER A -17 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 SER A -16 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -15 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -14 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -13 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -12 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -11 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A -10 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 SER A -9 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 SER A -8 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 GLY A -7 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 LEU A -6 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 VAL A -5 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 PRO A -4 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 ARG A -3 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 GLY A -2 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 SER A -1 UNP O87899 CLONING ARTIFACT SEQADV 1YX3 HIS A 0 UNP O87899 CLONING ARTIFACT SEQRES 1 A 132 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY SEQRES 2 A 132 LEU VAL PRO ARG GLY SER HIS MET ALA ASP THR ILE GLU SEQRES 3 A 132 VAL ASP GLY LYS GLN PHE ALA VAL ASP GLU GLU GLY TYR SEQRES 4 A 132 LEU SER ASN LEU ASN ASP TRP VAL PRO GLY VAL ALA ASP SEQRES 5 A 132 VAL MET ALA LYS GLN ASP ASN LEU GLU LEU THR GLU GLU SEQRES 6 A 132 HIS TRP ASP ILE ILE ASN PHE LEU ARG GLU TYR TYR GLU SEQRES 7 A 132 GLU TYR GLN ILE ALA PRO ALA VAL ARG VAL LEU THR LYS SEQRES 8 A 132 ALA VAL GLY LYS LYS LEU GLY LYS GLU LYS GLY ASN SER SEQRES 9 A 132 LYS TYR LEU TYR SER LEU PHE PRO TYR GLY PRO ALA LYS SEQRES 10 A 132 GLN ALA CYS ARG PHE ALA GLY LEU PRO LYS PRO THR GLY SEQRES 11 A 132 CYS VAL HELIX 1 1 VAL A 27 GLN A 37 1 11 HELIX 2 2 THR A 43 GLN A 61 1 19 HELIX 3 3 ALA A 65 GLY A 78 1 14 HELIX 4 4 ASN A 83 PHE A 91 1 9 HELIX 5 5 GLY A 94 GLY A 104 1 11 SHEET 1 A 3 ASP A 3 VAL A 7 0 SHEET 2 A 3 LYS A 10 ASP A 15 -1 O VAL A 14 N ASP A 3 SHEET 3 A 3 TYR A 19 LEU A 20 -1 O TYR A 19 N ASP A 15 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