Header list of 2a2p.pdb file
Complete list - t 20 2 Bytes
HEADER OXIDOREDUCTASE 22-JUN-05 2A2P TITLE SOLUTION STRUCTURE OF SELM FROM MUS MUSCULUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: SELENOPROTEIN M; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SELM PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: SEPM, SELM; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A KEYWDS SELENOPROTEIN, REDOX ENZYME, 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 5 20-OCT-21 2A2P 1 SEQADV REVDAT 4 09-APR-14 2A2P 1 REMARK SEQADV VERSN REVDAT 3 24-FEB-09 2A2P 1 VERSN REVDAT 2 21-FEB-06 2A2P 1 JRNL REVDAT 1 06-DEC-05 2A2P 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, M. (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2A2P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033416. 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 15N,13C-LABELED SELM 50 MM REMARK 210 PHOSPHATE BUFFER (PH 6) REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N REMARK 210 -SEPARATED_NOESY; 3D_13C- REMARK 210 SEPARATED_NOESY 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 1.0, NMRVIEW 5.2.2, ARIA REMARK 210 2.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED REMARK 210 ANNEALING MOLECULAR DYNAMICS REMARK 210 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 : 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: 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 THR A 25 -83.98 62.13 REMARK 500 1 ASP A 30 69.33 -102.37 REMARK 500 1 ARG A 35 118.62 -34.87 REMARK 500 1 LEU A 50 41.16 -106.15 REMARK 500 1 LEU A 53 47.08 -99.08 REMARK 500 1 VAL A 60 50.83 -99.52 REMARK 500 1 THR A 61 -39.13 -164.77 REMARK 500 1 GLU A 62 -66.32 -109.60 REMARK 500 1 ASN A 69 20.73 46.89 REMARK 500 1 ARG A 87 -75.53 53.83 REMARK 500 1 ASN A 88 27.01 -68.66 REMARK 500 1 GLU A 91 109.63 -36.10 REMARK 500 1 GLU A 138 80.99 -69.43 REMARK 500 1 ALA A 139 -41.67 -167.96 REMARK 500 1 ASP A 143 -22.50 -145.17 REMARK 500 1 ASP A 144 42.99 -100.97 REMARK 500 1 HIS A 147 -8.97 66.37 REMARK 500 1 HIS A 148 80.32 48.94 REMARK 500 1 HIS A 149 -74.47 -142.66 REMARK 500 2 THR A 25 95.18 60.01 REMARK 500 2 TYR A 27 149.32 64.60 REMARK 500 2 ASP A 30 68.76 -108.33 REMARK 500 2 ARG A 35 130.63 -39.35 REMARK 500 2 GLN A 49 -19.02 70.21 REMARK 500 2 LEU A 53 59.90 -101.72 REMARK 500 2 GLU A 55 -70.19 -59.48 REMARK 500 2 VAL A 60 54.68 -100.01 REMARK 500 2 THR A 61 -43.08 -160.90 REMARK 500 2 ARG A 87 147.77 58.50 REMARK 500 2 ASN A 88 -78.34 63.68 REMARK 500 2 TYR A 89 29.08 -176.39 REMARK 500 2 GLU A 91 111.18 -36.60 REMARK 500 2 SER A 98 21.08 -79.78 REMARK 500 2 PRO A 136 176.62 -56.78 REMARK 500 2 GLU A 137 -76.88 -59.89 REMARK 500 2 GLU A 138 96.90 -61.81 REMARK 500 2 SER A 140 -83.05 61.81 REMARK 500 2 GLU A 141 96.27 59.60 REMARK 500 2 HIS A 148 -172.01 58.01 REMARK 500 2 HIS A 150 80.36 -156.20 REMARK 500 3 THR A 25 124.11 64.97 REMARK 500 3 ARG A 35 112.47 -34.35 REMARK 500 3 LEU A 53 52.07 -109.04 REMARK 500 3 VAL A 60 52.10 -100.27 REMARK 500 3 THR A 61 -44.04 -158.66 REMARK 500 3 HIS A 74 60.74 -111.11 REMARK 500 3 PRO A 76 94.92 -52.39 REMARK 500 3 ARG A 87 148.16 58.08 REMARK 500 3 ASN A 88 -77.38 63.44 REMARK 500 3 TYR A 89 30.99 -178.64 REMARK 500 REMARK 500 THIS ENTRY HAS 399 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUE 48 IN THE SWISS-PROT ENTRY IS SE_CYS, REMARK 999 FOR SELENOCYSTEINE. IN THIS ENTRY, THE REMARK 999 SELENOCYSTEINE (SEC) HAS BEEN MUTATED TO CYS. DBREF 2A2P A 25 145 UNP Q8VHC3 SELM_MOUSE 25 145 SEQADV 2A2P MET A 24 UNP Q8VHC3 INITIATING METHIONINE SEQADV 2A2P CYS A 48 UNP Q8VHC3 SEC 48 ENGINEERED MUTATION SEQADV 2A2P GLU A 146 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 147 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 148 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 149 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 150 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 151 UNP Q8VHC3 CLONING ARTIFACT SEQADV 2A2P HIS A 152 UNP Q8VHC3 CLONING ARTIFACT SEQRES 1 A 129 MET THR ASN TYR ARG PRO ASP TRP ASN ARG LEU ARG GLY SEQRES 2 A 129 LEU ALA ARG GLY ARG VAL GLU THR CYS GLY GLY CYS GLN SEQRES 3 A 129 LEU ASN ARG LEU LYS GLU VAL LYS ALA PHE VAL THR GLU SEQRES 4 A 129 ASP ILE GLN LEU TYR HIS ASN LEU VAL MET LYS HIS LEU SEQRES 5 A 129 PRO GLY ALA ASP PRO GLU LEU VAL LEU LEU SER ARG ASN SEQRES 6 A 129 TYR GLN GLU LEU GLU ARG ILE PRO LEU SER GLN MET THR SEQRES 7 A 129 ARG ASP GLU ILE ASN ALA LEU VAL GLN GLU LEU GLY PHE SEQRES 8 A 129 TYR ARG LYS SER ALA PRO GLU ALA GLN VAL PRO PRO GLU SEQRES 9 A 129 TYR LEU TRP ALA PRO ALA LYS PRO PRO GLU GLU ALA SER SEQRES 10 A 129 GLU HIS ASP ASP LEU GLU HIS HIS HIS HIS HIS HIS HELIX 1 1 ASP A 30 ARG A 35 1 6 HELIX 2 2 LEU A 53 VAL A 60 1 8 HELIX 3 3 GLU A 62 TYR A 67 1 6 HELIX 4 4 THR A 101 GLY A 113 1 13 HELIX 5 5 PRO A 125 LEU A 129 5 5 SHEET 1 A 4 LEU A 70 LEU A 75 0 SHEET 2 A 4 ARG A 39 CYS A 45 1 N VAL A 42 O VAL A 71 SHEET 3 A 4 GLU A 81 LEU A 85 -1 O GLU A 81 N GLU A 43 SHEET 4 A 4 GLU A 93 PRO A 96 -1 O ILE A 95 N LEU A 82 SSBOND 1 CYS A 45 CYS A 48 1555 1555 2.03 CISPEP 1 ALA A 131 PRO A 132 1 0.46 CISPEP 2 ALA A 131 PRO A 132 2 -0.16 CISPEP 3 ALA A 131 PRO A 132 3 0.49 CISPEP 4 ALA A 131 PRO A 132 4 0.36 CISPEP 5 ALA A 131 PRO A 132 5 0.41 CISPEP 6 ALA A 131 PRO A 132 6 -0.02 CISPEP 7 ALA A 131 PRO A 132 7 0.07 CISPEP 8 ALA A 131 PRO A 132 8 0.15 CISPEP 9 ALA A 131 PRO A 132 9 0.28 CISPEP 10 ALA A 131 PRO A 132 10 0.16 CISPEP 11 ALA A 131 PRO A 132 11 0.46 CISPEP 12 ALA A 131 PRO A 132 12 -0.09 CISPEP 13 ALA A 131 PRO A 132 13 -0.11 CISPEP 14 ALA A 131 PRO A 132 14 -0.04 CISPEP 15 ALA A 131 PRO A 132 15 -0.09 CISPEP 16 ALA A 131 PRO A 132 16 0.51 CISPEP 17 ALA A 131 PRO A 132 17 -0.18 CISPEP 18 ALA A 131 PRO A 132 18 0.28 CISPEP 19 ALA A 131 PRO A 132 19 0.14 CISPEP 20 ALA A 131 PRO A 132 20 -0.14 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 - t 20 2 Bytes