Header list of 2a4h.pdb file
Complete list - r 9 2 Bytes
HEADER OXIDOREDUCTASE 28-JUN-05 2A4H TITLE SOLUTION STRUCTURE OF SEP15 FROM DROSOPHILA MELANOGASTER COMPND MOL_ID: 1; COMPND 2 MOLECULE: SELENOPROTEIN SEP15; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: REDOX DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 GENE: SEP15; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A KEYWDS SELENOPROTEIN, REDOX, OXIDOREDUCTASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.D.FERGUSON,V.M.LABUNSKYY,D.E.FOMENKO,Y.CHELLIAH,C.A.AMEZCUA,J.RIZO, AUTHOR 2 V.N.GLADYSHEV,J.DEISENHOFER REVDAT 4 09-MAR-22 2A4H 1 REMARK SEQADV REVDAT 3 24-FEB-09 2A4H 1 VERSN REVDAT 2 21-FEB-06 2A4H 1 JRNL REVDAT 1 13-DEC-05 2A4H 0 JRNL AUTH A.D.FERGUSON,V.M.LABUNSKYY,D.E.FOMENKO,Y.CHELLIAH, JRNL AUTH 2 C.A.AMEZCUA,J.RIZO,V.N.GLADYSHEV,J.DEISENHOFER JRNL TITL NMR STRUCTURES OF THE SELENOPROTEINS SEP15 AND SELM REVEAL JRNL TITL 2 REDOX ACTIVITY OF A NEW THIOREDOXIN-LIKE FAMILY. JRNL REF J.BIOL.CHEM. V. 281 3536 2006 JRNL REFN ISSN 0021-9258 JRNL PMID 16319061 JRNL DOI 10.1074/JBC.M511386200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, ARIA 2.0 REMARK 3 AUTHORS : VARIAN (VNMR), NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A4H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033476. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 50 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM SEP15 U-15N,13C 50 MM REMARK 210 PHOSPHATE BUFFER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D REMARK 210 TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1, NMRVIEW 5.2.2, ARIA REMARK 210 2.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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: 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 55 -74.48 -120.71 REMARK 500 1 HIS A 56 89.60 -162.67 REMARK 500 1 HIS A 58 -70.26 -70.94 REMARK 500 1 HIS A 60 54.07 -142.93 REMARK 500 1 HIS A 61 -73.55 65.71 REMARK 500 1 LEU A 62 -60.39 -178.39 REMARK 500 1 GLN A 65 131.44 64.75 REMARK 500 1 ALA A 68 -87.36 -142.61 REMARK 500 1 THR A 71 154.96 -43.98 REMARK 500 1 THR A 81 16.68 57.83 REMARK 500 1 TYR A 87 62.96 -112.22 REMARK 500 1 ILE A 90 -81.05 -50.49 REMARK 500 1 ILE A 107 57.92 80.64 REMARK 500 1 TYR A 109 63.61 -111.22 REMARK 500 1 VAL A 110 156.05 -34.04 REMARK 500 1 LEU A 113 -163.80 -119.43 REMARK 500 1 ALA A 122 -42.46 173.46 REMARK 500 1 VAL A 126 90.20 94.13 REMARK 500 1 LYS A 134 -36.43 -177.88 REMARK 500 1 TRP A 135 -64.31 -19.75 REMARK 500 1 ASN A 136 -41.61 -152.01 REMARK 500 1 THR A 137 170.57 51.06 REMARK 500 1 ASP A 138 -79.81 59.58 REMARK 500 1 LYS A 155 132.36 64.19 REMARK 500 1 SER A 159 -77.97 -144.19 REMARK 500 1 ASP A 163 99.29 -52.05 REMARK 500 1 ASP A 168 31.64 -162.63 REMARK 500 1 ASP A 169 88.83 178.19 REMARK 500 1 ASP A 171 85.34 -177.33 REMARK 500 1 TYR A 172 -159.86 48.58 REMARK 500 1 ASN A 176 119.52 59.86 REMARK 500 1 ARG A 177 78.54 -150.52 REMARK 500 2 ALA A 54 -76.50 65.70 REMARK 500 2 SER A 55 -64.58 -176.74 REMARK 500 2 HIS A 58 74.05 -111.45 REMARK 500 2 LEU A 62 -71.04 67.28 REMARK 500 2 GLN A 64 -71.36 -48.30 REMARK 500 2 TYR A 87 61.67 -110.72 REMARK 500 2 ILE A 90 -80.99 -50.96 REMARK 500 2 ILE A 107 81.45 59.99 REMARK 500 2 TYR A 109 62.77 -104.16 REMARK 500 2 VAL A 110 156.14 -33.20 REMARK 500 2 ALA A 122 -69.15 -173.70 REMARK 500 2 VAL A 126 72.76 68.14 REMARK 500 2 LYS A 134 -67.54 -140.52 REMARK 500 2 TRP A 135 -85.87 32.52 REMARK 500 2 ASN A 136 -20.37 -172.06 REMARK 500 2 THR A 137 -167.28 50.25 REMARK 500 2 ASP A 138 -80.02 60.42 REMARK 500 2 LYS A 155 -67.90 68.82 REMARK 500 REMARK 500 THIS ENTRY HAS 606 RAMACHANDRAN OUTLIERS. 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. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2A2P RELATED DB: PDB REMARK 900 SELM DBREF 2A4H A 62 178 UNP Q9VVJ7 Q9VVJ7_DROME 62 178 SEQADV 2A4H MET A 53 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H ALA A 54 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H SER A 55 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 56 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 57 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 58 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 59 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 60 UNP Q9VVJ7 CLONING ARTIFACT SEQADV 2A4H HIS A 61 UNP Q9VVJ7 CLONING ARTIFACT SEQRES 1 A 126 MET ALA SER HIS HIS HIS HIS HIS HIS LEU ASP GLN GLN SEQRES 2 A 126 PRO ALA ALA GLN ARG THR TYR ALA LYS ALA ILE LEU GLU SEQRES 3 A 126 VAL CYS THR CYS LYS PHE ARG ALA TYR PRO GLN ILE GLN SEQRES 4 A 126 ALA PHE ILE GLN SER GLY ARG PRO ALA LYS PHE PRO ASN SEQRES 5 A 126 LEU GLN ILE LYS TYR VAL ARG GLY LEU ASP PRO VAL VAL SEQRES 6 A 126 LYS LEU LEU ASP ALA SER GLY LYS VAL GLN GLU THR LEU SEQRES 7 A 126 SER ILE THR LYS TRP ASN THR ASP THR VAL GLU GLU PHE SEQRES 8 A 126 PHE GLU THR HIS LEU ALA LYS ASP GLY ALA GLY LYS ASN SEQRES 9 A 126 SER TYR SER VAL VAL GLU ASP ALA ASP GLY ASP ASP ASP SEQRES 10 A 126 GLU ASP TYR LEU ARG THR ASN ARG ILE HELIX 1 1 ILE A 90 SER A 96 1 7 HELIX 2 2 PRO A 99 LYS A 101 5 3 HELIX 3 3 THR A 139 HIS A 147 1 9 SHEET 1 A 4 LEU A 105 LYS A 108 0 SHEET 2 A 4 ALA A 75 GLU A 78 1 SHEET 3 A 4 VAL A 116 LEU A 120 -1 SHEET 4 A 4 GLU A 128 SER A 131 -1 SSBOND 1 CYS A 80 CYS A 82 1555 1555 2.04 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 9 2 Bytes