Header list of 1t2s.pdb file
Complete list - r 2 2 Bytes
HEADER NUCLEIC ACID BINDING PROTEIN/DNA 22-APR-04 1T2S
TITLE STRUCTURAL BASIS FOR 3' END RECOGNITION OF NUCLEIC ACIDS BY THE
TITLE 2 DROSOPHILA ARGONAUTE 2 PAZ DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*TP*CP*AP*C)-3';
COMPND 3 CHAIN: B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ARGONAUTE 2;
COMPND 7 CHAIN: A;
COMPND 8 FRAGMENT: PAZ DOMAIN, RESIDUES 605-723;
COMPND 9 SYNONYM: CG7439 PROTEIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 5 ORGANISM_COMMON: FRUIT FLY;
SOURCE 6 ORGANISM_TAXID: 7227;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PETM60
KEYWDS NUCLEIC ACID BINDING PROTEIN, DNA, NUCLEIC ACID BINDING PROTEIN-DNA
KEYWDS 2 COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER
REVDAT 3 02-MAR-22 1T2S 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1T2S 1 VERSN
REVDAT 1 01-JUN-04 1T2S 0
JRNL AUTH A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER
JRNL TITL NUCLEIC ACID 3'-END RECOGNITION BY THE ARGONAUTE2 PAZ
JRNL TITL 2 DOMAIN.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 576 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15156196
JRNL DOI 10.1038/NSMB777
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER
REMARK 1 TITL STRUCTURE AND NUCLEIC-ACID BINDING OF THE DROSOPHILA
REMARK 1 TITL 2 ARGONAUTE 2 PAZ DOMAIN
REMARK 1 REF NATURE V. 426 465 2003
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/NATURE02123
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA1.2, CNS1.1
REMARK 3 AUTHORS : NILGES, BRUNGER ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE EXPERIMENTALLY DETERMINED DISTANCE
REMARK 3 RESTRAINTS WERE APPLIED IN A MIXED TORSION AND CARTESIA DYNAMICS
REMARK 3 SIMULATED ANNEALING PROTOCOL. THE FINAL STRUCTURE ENSEMBLE WAS
REMARK 3 REFINED IN A SHELL OF WATER MOLECULES.
REMARK 4
REMARK 4 1T2S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022239.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.2-1 MM 15N OR 15N,13C-LABELED
REMARK 210 PROTEIN, 0.1-2.5 MM UNLABELED
REMARK 210 DNA, 50 MM SODIUM PHOSPHATE
REMARK 210 BUFFER, 0.2 MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 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 : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURAL RESTRAINTS WERE DERIVED FROM 13C AND 15N-EDITED
REMARK 210 AND EDITED FILTERED NOESY EXPERIMENTS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 DC B 201
REMARK 465 DT B 202
REMARK 465 DC B 203
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 MET A 3 61.12 -113.98
REMARK 500 1 ASN A 21 -154.52 -153.95
REMARK 500 1 ASN A 89 50.21 72.80
REMARK 500 2 ASN A 25 59.21 -106.59
REMARK 500 2 ARG A 38 101.86 -58.95
REMARK 500 2 ASN A 89 56.07 72.35
REMARK 500 2 TYR A 90 99.93 -161.25
REMARK 500 2 PHE A 94 68.72 -151.68
REMARK 500 2 HIS A 98 177.17 69.99
REMARK 500 2 VAL A 102 -168.10 -129.05
REMARK 500 3 PHE A 14 -60.77 -102.49
REMARK 500 3 ASN A 21 -165.63 -119.29
REMARK 500 3 ASN A 25 53.29 -94.17
REMARK 500 3 LEU A 97 35.87 -88.45
REMARK 500 3 HIS A 98 174.17 61.05
REMARK 500 4 PHE A 14 -61.08 -106.33
REMARK 500 5 ARG A 38 98.56 -67.64
REMARK 500 5 ASN A 89 45.91 71.36
REMARK 500 5 PRO A 112 106.64 -57.12
REMARK 500 6 ALA A 2 87.83 61.55
REMARK 500 6 ASN A 25 47.62 -84.94
REMARK 500 6 ASN A 89 45.26 74.41
REMARK 500 7 VAL A 102 -167.52 -127.28
REMARK 500 7 PRO A 112 106.22 -57.23
REMARK 500 8 ALA A 18 -164.61 -126.88
REMARK 500 8 ASN A 89 33.36 71.74
REMARK 500 9 PHE A 14 -60.09 -95.69
REMARK 500 9 ASN A 25 65.25 -103.77
REMARK 500 10 ASN A 21 -158.00 -151.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T2S RELATED DB: PDB
REMARK 900 RELATED ID: 1UPO RELATED DB: PDB
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 1T2S A 5 123 UNP Q9VUQ5 AGO2_DROME 605 723
DBREF 1T2S B 201 205 PDB 1T2S 1T2S 201 205
SEQADV 1T2S GLY A 1 UNP Q9VUQ5 CLONING ARTIFACT
SEQADV 1T2S ALA A 2 UNP Q9VUQ5 CLONING ARTIFACT
SEQADV 1T2S MET A 3 UNP Q9VUQ5 CLONING ARTIFACT
SEQADV 1T2S ALA A 4 UNP Q9VUQ5 CLONING ARTIFACT
SEQRES 1 B 5 DC DT DC DA DC
SEQRES 1 A 123 GLY ALA MET ALA MET PRO MET ILE GLU TYR LEU GLU ARG
SEQRES 2 A 123 PHE SER LEU LYS ALA LYS ILE ASN ASN THR THR ASN LEU
SEQRES 3 A 123 ASP TYR SER ARG ARG PHE LEU GLU PRO PHE LEU ARG GLY
SEQRES 4 A 123 ILE ASN VAL VAL TYR THR PRO PRO GLN SER PHE GLN SER
SEQRES 5 A 123 ALA PRO ARG VAL TYR ARG VAL ASN GLY LEU SER ARG ALA
SEQRES 6 A 123 PRO ALA SER SER GLU THR PHE GLU HIS ASP GLY LYS LYS
SEQRES 7 A 123 VAL THR ILE ALA SER TYR PHE HIS SER ARG ASN TYR PRO
SEQRES 8 A 123 LEU LYS PHE PRO GLN LEU HIS CYS LEU ASN VAL GLY SER
SEQRES 9 A 123 SER ILE LYS SER ILE LEU LEU PRO ILE GLU LEU CYS SER
SEQRES 10 A 123 ILE GLU GLU GLY GLN ALA
HELIX 1 1 MET A 7 SER A 15 1 9
HELIX 2 2 SER A 29 ARG A 38 1 10
HELIX 3 3 ILE A 81 ARG A 88 1 8
HELIX 4 4 PRO A 112 GLU A 114 5 3
SHEET 1 A 4 MET A 5 PRO A 6 0
SHEET 2 A 4 CYS A 116 ILE A 118 -1 O ILE A 118 N MET A 5
SHEET 3 A 4 ILE A 40 TYR A 44 -1 N VAL A 43 O SER A 117
SHEET 4 A 4 ARG A 55 VAL A 59 -1 O VAL A 59 N ILE A 40
SHEET 1 B 3 GLY A 61 PRO A 66 0
SHEET 2 B 3 HIS A 98 GLY A 103 -1 O CYS A 99 N SER A 63
SHEET 3 B 3 SER A 108 LEU A 111 -1 O LEU A 111 N LEU A 100
SHEET 1 C 2 THR A 71 HIS A 74 0
SHEET 2 C 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 - r 2 2 Bytes