Header list of 1xoy.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 07-OCT-04 1XOY TITLE SOLUTION STRUCTURE OF AT3G04780.1, AN ARABIDOPSIS ORTHOLOG OF THE C- TITLE 2 TERMINAL DOMAIN OF HUMAN THIOREDOXIN-LIKE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN AT3G04780.1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA; SOURCE 3 ORGANISM_COMMON: THALE CRESS; SOURCE 4 ORGANISM_TAXID: 3702; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, CENTER FOR KEYWDS 2 EUKARYOTIC STRUCTURAL GENOMICS, PSI, CESG, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.SONG,C.T.ROBERT,M.S.LEE,J.L.MARKLEY,CENTER FOR EUKARYOTIC AUTHOR 2 STRUCTURAL GENOMICS (CESG) REVDAT 6 02-MAR-22 1XOY 1 REMARK SEQADV REVDAT 5 24-FEB-09 1XOY 1 VERSN REVDAT 4 12-FEB-08 1XOY 1 REMARK REVDAT 3 17-JAN-06 1XOY 1 JRNL REVDAT 2 01-FEB-05 1XOY 1 AUTHOR KEYWDS REMARK REVDAT 1 12-OCT-04 1XOY 0 JRNL AUTH J.SONG,R.C.TYLER,R.L.WROBEL,R.O.FREDERICK,F.C.VOJTEK, JRNL AUTH 2 W.B.JEON,M.S.LEE,J.L.MARKLEY JRNL TITL SOLUTION STRUCTURE OF AT3G04780.1-DES15, AN ARABIDOPSIS JRNL TITL 2 THALIANA ORTHOLOG OF THE C-TERMINAL DOMAIN OF HUMAN JRNL TITL 3 THIOREDOXIN-LIKE PROTEIN. JRNL REF PROTEIN SCI. V. 14 1059 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15741346 JRNL DOI 10.1110/PS.041246805 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1, XPLOR-NIH 2.9.3 REMARK 3 AUTHORS : VARIAN (VNMR), SCHWIETERS, ET AL. (XPLOR-NIH) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1XOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-04. REMARK 100 THE DEPOSITION ID IS D_1000030596. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.2 REMARK 210 PH : 7.2 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C AT3G04780.1, 50 REMARK 210 MM KH2PO4, 10 MM DTT, 90%H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 3D HNCACB; 3D REMARK 210 CBCA(CO)NH; 3D HCCH-TOCSY; 3D REMARK 210 C(CO)NH REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; DMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE REMARK 210 97.027.12.56, SPARKY 3.72, CYANA REMARK 210 1.06 REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 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 SER A 5 -73.12 -176.49 REMARK 500 1 TRP A 22 -33.97 72.44 REMARK 500 1 ASN A 29 -67.42 -151.64 REMARK 500 1 SER A 31 112.91 78.89 REMARK 500 1 ARG A 45 20.72 -61.36 REMARK 500 1 GLU A 48 -49.57 -167.78 REMARK 500 1 ALA A 56 -41.87 -136.10 REMARK 500 1 HIS A 96 107.60 71.01 REMARK 500 1 GLU A 148 -45.83 69.85 REMARK 500 2 LYS A 11 106.25 68.44 REMARK 500 2 ASN A 29 -88.80 -95.11 REMARK 500 2 GLN A 30 17.88 55.47 REMARK 500 2 SER A 32 -4.75 -55.37 REMARK 500 2 SER A 33 -17.16 80.11 REMARK 500 2 ARG A 45 -91.83 -75.07 REMARK 500 2 GLU A 46 84.73 39.39 REMARK 500 2 ASP A 47 85.68 -67.24 REMARK 500 2 GLU A 48 103.12 169.91 REMARK 500 2 ASP A 55 -64.28 -170.70 REMARK 500 2 ASN A 93 -4.29 76.37 REMARK 500 2 HIS A 96 99.63 72.10 REMARK 500 2 GLU A 148 -32.05 78.51 REMARK 500 2 LYS A 154 130.45 -170.15 REMARK 500 3 TRP A 22 -4.37 76.45 REMARK 500 3 ASN A 29 -17.29 152.47 REMARK 500 3 SER A 33 -90.03 -154.75 REMARK 500 3 GLU A 48 -52.12 175.91 REMARK 500 3 ASN A 93 96.90 38.04 REMARK 500 3 HIS A 96 84.41 51.99 REMARK 500 3 PHE A 130 78.62 -101.03 REMARK 500 3 GLU A 148 -36.16 67.76 REMARK 500 3 LYS A 154 134.33 -172.34 REMARK 500 4 ALA A 6 71.38 55.08 REMARK 500 4 LYS A 11 99.51 61.85 REMARK 500 4 LEU A 16 6.04 -68.65 REMARK 500 4 VAL A 25 84.85 39.16 REMARK 500 4 LEU A 28 -72.01 -59.25 REMARK 500 4 SER A 31 130.53 71.06 REMARK 500 4 ASP A 47 84.54 -64.03 REMARK 500 4 GLU A 48 99.71 160.42 REMARK 500 4 LYS A 86 -71.04 -87.06 REMARK 500 4 ASN A 93 -42.12 73.96 REMARK 500 4 HIS A 96 96.08 58.40 REMARK 500 4 LYS A 126 105.36 -56.58 REMARK 500 4 SER A 135 163.67 171.98 REMARK 500 4 GLU A 148 -23.50 63.30 REMARK 500 5 SER A 2 -63.05 -151.74 REMARK 500 5 ALA A 3 -55.82 -141.02 REMARK 500 5 GLU A 4 77.44 40.19 REMARK 500 5 ALA A 6 91.87 63.05 REMARK 500 REMARK 500 THIS ENTRY HAS 292 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6341 RELATED DB: BMRB REMARK 900 RELATED ID: GO.11624 RELATED DB: TARGETDB DBREF 1XOY A 2 161 UNP Q9SQZ9 Y3478_ARATH 2 161 SEQADV 1XOY SER A 1 UNP Q9SQZ9 CLONING ARTIFACT SEQRES 1 A 161 SER SER ALA GLU SER ALA SER GLN ILE PRO LYS GLY GLN SEQRES 2 A 161 VAL ASP LEU LEU ASP PHE ILE ASP TRP SER GLY VAL GLU SEQRES 3 A 161 CYS LEU ASN GLN SER SER SER HIS SER LEU PRO ASN ALA SEQRES 4 A 161 LEU LYS GLN GLY TYR ARG GLU ASP GLU GLY LEU ASN LEU SEQRES 5 A 161 GLU SER ASP ALA ASP GLU GLN LEU LEU ILE TYR ILE PRO SEQRES 6 A 161 PHE ASN GLN VAL ILE LYS LEU HIS SER PHE ALA ILE LYS SEQRES 7 A 161 GLY PRO GLU GLU GLU GLY PRO LYS THR VAL LYS PHE PHE SEQRES 8 A 161 SER ASN LYS GLU HIS MET CYS PHE SER ASN VAL ASN ASP SEQRES 9 A 161 PHE PRO PRO SER ASP THR ALA GLU LEU THR GLU GLU ASN SEQRES 10 A 161 LEU LYS GLY LYS PRO VAL VAL LEU LYS TYR VAL LYS PHE SEQRES 11 A 161 GLN ASN VAL ARG SER LEU THR ILE PHE ILE GLU ALA ASN SEQRES 12 A 161 GLN SER GLY SER GLU VAL THR LYS VAL GLN LYS ILE ALA SEQRES 13 A 161 LEU TYR GLY SER THR HELIX 1 1 LEU A 36 LYS A 41 1 6 HELIX 2 2 CYS A 98 ASN A 103 1 6 HELIX 3 3 GLU A 116 GLY A 120 5 5 SHEET 1 A 4 VAL A 14 ASP A 15 0 SHEET 2 A 4 LYS A 154 GLY A 159 -1 O GLY A 159 N VAL A 14 SHEET 3 A 4 LEU A 72 LYS A 78 -1 N SER A 74 O TYR A 158 SHEET 4 A 4 VAL A 123 VAL A 124 -1 O VAL A 123 N PHE A 75 SHEET 1 B 5 GLU A 26 CYS A 27 0 SHEET 2 B 5 LEU A 60 ILE A 70 -1 O TYR A 63 N GLU A 26 SHEET 3 B 5 VAL A 133 ASN A 143 -1 O ILE A 138 N ILE A 62 SHEET 4 B 5 PRO A 85 SER A 92 -1 N LYS A 89 O PHE A 139 SHEET 5 B 5 ASP A 109 ALA A 111 -1 O ALA A 111 N VAL A 88 SHEET 1 C 2 LEU A 52 GLU A 53 0 SHEET 2 C 2 LYS A 151 VAL A 152 -1 O VAL A 152 N LEU A 52 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