Header list of 1vyn.pdb file
Complete list - n 17 2 Bytes
HEADER NUCLEIC ACID BINDING 03-MAY-04 1VYN TITLE STRUCTURE AND NUCLEIC ACID BINDING OF THE DROSOPHILA ARGONAUTE2 PAZ TITLE 2 DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARGONAUTE2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PAZ DOMAIN, RESIDUES 605-743; 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETM60 KEYWDS NUCLEIC ACID BINDING, RNA INTERFERENCE EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER REVDAT 3 17-JAN-18 1VYN 1 JRNL REVDAT 2 24-FEB-09 1VYN 1 VERSN REVDAT 1 11-MAY-04 1VYN 0 SPRSDE 11-MAY-04 1VYN 1UPO JRNL AUTH A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER JRNL TITL STRUCTURE AND NUCLEIC-ACID BINDING OF THE DROSOPHILA JRNL TITL 2 ARGONAUTE 2 PAZ DOMAIN. JRNL REF NATURE V. 426 465 2003 JRNL REFN ESSN 1476-4687 JRNL PMID 14615801 JRNL DOI 10.1038/NATURE02123 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : ARIA1.2, CNS1.1 CNS1.1 CNS1.1 REMARK 3 AUTHORS : NILGES, BRUNGER ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE NMR ENSEMBLE HAS BEEN REFINED IN A REMARK 3 SHELL OF WATER MOLECULES.REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE. REMARK 4 REMARK 4 1VYN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAY-04. REMARK 100 THE DEPOSITION ID IS D_1290015156. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 6.8 REMARK 210 IONIC STRENGTH : 150 MM NACL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.0-1.5 MM 15N OR 15N,13C REMARK 210 -LABELED PROTEIN, 50 MM REMARK 210 NA.PHOSPHATE BUFFER, 150 MM NACL, REMARK 210 0.2 MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE; NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 700 MHZ; 900 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW, ARIA/CNS REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8 REMARK 210 REMARK 210 REMARK: STRUCTURAL RESTRAINTS WERE DERIVED FROM 13C AND 15N-EDITED REMARK 210 NOESY EXPERIMENTS, J-COUPLINGS, AND H-N RESIDUAL DIPOLAR REMARK 210 COUPLINGS. 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 1-10 REMARK 465 RES C SSSEQI REMARK 465 GLY A 1 REMARK 465 ALA A 2 REMARK 465 MET A 3 REMARK 465 GLY A 121 REMARK 465 GLN A 122 REMARK 465 ALA A 123 REMARK 465 LEU A 124 REMARK 465 ASN A 125 REMARK 465 ARG A 126 REMARK 465 LYS A 127 REMARK 465 ASP A 128 REMARK 465 GLY A 129 REMARK 465 ALA A 130 REMARK 465 THR A 131 REMARK 465 GLN A 132 REMARK 465 VAL A 133 REMARK 465 ALA A 134 REMARK 465 ASN A 135 REMARK 465 MET A 136 REMARK 465 ILE A 137 REMARK 465 LYS A 138 REMARK 465 TYR A 139 REMARK 465 ALA A 140 REMARK 465 ALA A 141 REMARK 465 THR A 142 REMARK 465 SER A 143 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: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 2 TYR A 84 CE1 TYR A 84 CZ 0.090 REMARK 500 2 TYR A 84 CZ TYR A 84 CE2 -0.082 REMARK 500 5 TYR A 84 CE1 TYR A 84 CZ 0.083 REMARK 500 5 TYR A 84 CZ TYR A 84 CE2 -0.078 REMARK 500 9 TYR A 84 CE1 TYR A 84 CZ 0.097 REMARK 500 9 TYR A 84 CZ TYR A 84 CE2 -0.094 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 18 -146.08 -145.99 REMARK 500 1 ASN A 21 179.15 178.27 REMARK 500 1 ARG A 38 99.07 -57.23 REMARK 500 1 PRO A 54 107.63 -45.65 REMARK 500 1 ASP A 75 40.72 70.03 REMARK 500 2 ALA A 18 -159.32 -148.98 REMARK 500 2 ARG A 38 98.53 -58.96 REMARK 500 3 ALA A 18 -145.48 -149.42 REMARK 500 3 ASN A 25 72.04 64.45 REMARK 500 3 ARG A 38 107.51 -51.78 REMARK 500 3 ASN A 89 34.34 72.90 REMARK 500 4 ASN A 25 81.76 65.90 REMARK 500 4 ARG A 38 104.89 -54.99 REMARK 500 4 ASN A 89 34.24 72.86 REMARK 500 5 ALA A 18 -138.94 -155.60 REMARK 500 5 ARG A 38 99.49 -55.62 REMARK 500 6 ASN A 89 37.89 73.34 REMARK 500 7 ALA A 18 -126.84 -152.89 REMARK 500 7 ARG A 38 98.01 -55.69 REMARK 500 7 PRO A 54 119.48 -33.08 REMARK 500 7 ASN A 89 45.64 71.04 REMARK 500 7 TYR A 90 88.85 -152.12 REMARK 500 8 ALA A 18 -152.53 -154.44 REMARK 500 8 ASN A 25 49.57 -78.79 REMARK 500 8 ARG A 38 93.87 -54.98 REMARK 500 8 PRO A 54 109.61 -40.52 REMARK 500 8 ASN A 89 35.44 70.18 REMARK 500 9 ALA A 18 -132.42 -149.01 REMARK 500 9 ASN A 21 -162.93 -170.16 REMARK 500 9 THR A 24 50.05 -99.89 REMARK 500 9 ARG A 38 102.47 -51.61 REMARK 500 9 ASN A 89 35.27 75.06 REMARK 500 10 GLN A 51 9.76 59.58 REMARK 500 10 ASN A 89 37.95 71.28 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1R6Z RELATED DB: PDB REMARK 900 THE CRYSTAL STRUCTURE OF THE ARGONAUTE2 PAZ DOMAIN (AS AMBP FUSION) REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES 1-4 IN THE CONSTRUCT USED FOR THE STRUCTURE REMARK 999 DETERMINATION ARE FROM THE EXPRESSION VECTOR. DBREF 1VYN A 1 4 PDB 1VYN 1VYN 1 4 DBREF 1VYN A 5 143 UNP Q9VUQ5 Q9VUQ5 605 743 SEQRES 1 A 143 GLY ALA MET ALA MET PRO MET ILE GLU TYR LEU GLU ARG SEQRES 2 A 143 PHE SER LEU LYS ALA LYS ILE ASN ASN THR THR ASN LEU SEQRES 3 A 143 ASP TYR SER ARG ARG PHE LEU GLU PRO PHE LEU ARG GLY SEQRES 4 A 143 ILE ASN VAL VAL TYR THR PRO PRO GLN SER PHE GLN SER SEQRES 5 A 143 ALA PRO ARG VAL TYR ARG VAL ASN GLY LEU SER ARG ALA SEQRES 6 A 143 PRO ALA SER SER GLU THR PHE GLU HIS ASP GLY LYS LYS SEQRES 7 A 143 VAL THR ILE ALA SER TYR PHE HIS SER ARG ASN TYR PRO SEQRES 8 A 143 LEU LYS PHE PRO GLN LEU HIS CYS LEU ASN VAL GLY SER SEQRES 9 A 143 SER ILE LYS SER ILE LEU LEU PRO ILE GLU LEU CYS SER SEQRES 10 A 143 ILE GLU GLU GLY GLN ALA LEU ASN ARG LYS ASP GLY ALA SEQRES 11 A 143 THR GLN VAL ALA ASN MET ILE LYS TYR ALA ALA THR SER HELIX 1 1 MET A 7 PHE A 14 1 8 HELIX 2 2 ASN A 25 ARG A 38 1 14 HELIX 3 3 ILE A 81 ARG A 88 1 8 HELIX 4 4 PRO A 112 GLU A 114 5 3 SHEET 1 AA 6 MET A 5 PRO A 6 0 SHEET 2 AA 6 CYS A 116 ILE A 118 -1 O ILE A 118 N MET A 5 SHEET 3 AA 6 ILE A 40 TYR A 44 -1 O VAL A 43 N SER A 117 SHEET 4 AA 6 ARG A 55 LEU A 62 -1 O ARG A 55 N TYR A 44 SHEET 5 AA 6 LEU A 100 SER A 104 -1 O ASN A 101 N GLY A 61 SHEET 6 AA 6 LYS A 107 LEU A 110 -1 O LYS A 107 N SER A 104 SHEET 1 AB 2 THR A 71 HIS A 74 0 SHEET 2 AB 2 LYS A 77 THR A 80 -1 O LYS A 77 N HIS A 74 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