Header list of 1l4s.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSLATION 05-MAR-02 1L4S TITLE SOLUTION STRUCTURE OF RIBOSOME ASSOCIATED FACTOR Y COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN YFIA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: RIBOSOME ASSOCIATED FACTOR Y; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 GENE: YFIA; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29B KEYWDS RIBOSOME BINDING PROTEIN, TRANSLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.YE,A.SERGANOV,W.HU,D.J.PATEL REVDAT 3 23-FEB-22 1L4S 1 REMARK REVDAT 2 24-FEB-09 1L4S 1 VERSN REVDAT 1 04-DEC-02 1L4S 0 JRNL AUTH K.YE,A.SERGANOV,W.HU,M.GARBER,D.J.PATEL JRNL TITL RIBOSOME-ASSOCIATED FACTOR Y ADOPTS A FOLD RESEMBLING A JRNL TITL 2 DOUBLE-STRANDED RNA BINDING DOMAIN SCAFFOLD. JRNL REF EUR.J.BIOCHEM. V. 269 5182 2002 JRNL REFN ISSN 0014-2956 JRNL PMID 12392550 JRNL DOI 10.1046/J.1432-1033.2002.03222.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.0 REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR), BRUNGER, A.T. ET REMARK 3 AL. (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON A TOTAL OF REMARK 3 2207 RESTRAINTS, 1507 UNAMBIGUOUS AND 408 AMBIGUOUS NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 72 DISTANCE CONSTRAINTS FROM HYDROGEN REMARK 3 BONDS, 75 DIHEDRAL ANGLE CONSTRAINTS, 65 JHNHA COUPLING REMARK 3 CONSTRAINTS, 80 DIPOLAR COUPLING CONSTRAINTS. REMARK 4 REMARK 4 1L4S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-02. REMARK 100 THE DEPOSITION ID IS D_1000015644. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 304.5; 313 REMARK 210 PH : 5.7; 6.6 REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE NA; 50 MM NACL; REMARK 210 20 MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2 MM PY, U-15N; 10MM SODIUM REMARK 210 PHOSPHATE; 50 MM NACL;PH 5.7; 93% REMARK 210 H2O, 7% D2O; 1.5 MM PY, U-15N, REMARK 210 13C; 10MM SODIUM PHOSPHATE; 50 REMARK 210 MM NACL;PH 5.7; 93% H2O, 7% D2O; REMARK 210 2 MM PY, U-15N; 10MM SODIUM REMARK 210 PHOSPHATE; 50 MM NACL;PH 5.7; REMARK 210 100% D2O; 1.5 MM PY, U-15N,13C; REMARK 210 10MM SODIUM PHOSPHATE; 50 MM REMARK 210 NACL;PH 5.7; 100% D2O; 1 MM PY, REMARK 210 U-15N,13C; 20MM POTASSIUM REMARK 210 PHOSPHATE;PH 6.6; 3.2% (W/V) REMARK 210 BICELLE (DMPC:DHPC:CTAB=30:10:2, REMARK 210 MOLAR RATIO); 93% H2O, 7% D2O; 1 REMARK 210 MM PY, U-10% 13C;10MM SODIUM REMARK 210 PHOSPHATE; 50 MM NACL;PH 5.7; REMARK 210 100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY; REMARK 210 HNHA; J-MODULATED-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98, NMRVIEW 5.0 REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION REMARK 210 ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 MET A 2 102.90 -170.36 REMARK 500 1 GLN A 8 -48.00 -140.95 REMARK 500 1 THR A 31 -39.69 -159.40 REMARK 500 1 HIS A 32 -120.17 -143.41 REMARK 500 1 LEU A 33 116.27 61.06 REMARK 500 1 ASN A 35 74.46 61.26 REMARK 500 1 LYS A 65 42.92 -147.59 REMARK 500 1 HIS A 89 -162.64 55.29 REMARK 500 1 LYS A 90 -42.54 -168.71 REMARK 500 1 ALA A 93 125.87 65.64 REMARK 500 1 ARG A 95 -79.43 -87.72 REMARK 500 1 ALA A 96 -168.73 -179.14 REMARK 500 1 THR A 98 -65.39 -125.10 REMARK 500 1 SER A 99 -43.88 -176.86 REMARK 500 1 VAL A 100 -172.37 45.63 REMARK 500 1 LYS A 101 114.60 -177.32 REMARK 500 1 ALA A 103 131.99 -175.72 REMARK 500 1 GLU A 108 35.60 -166.31 REMARK 500 1 VAL A 109 -46.08 -154.99 REMARK 500 2 MET A 2 86.30 57.25 REMARK 500 2 LEU A 33 135.50 62.44 REMARK 500 2 ASN A 35 75.61 53.87 REMARK 500 2 LYS A 42 145.96 -173.29 REMARK 500 2 GLN A 45 -78.71 -86.01 REMARK 500 2 LYS A 65 43.80 -141.21 REMARK 500 2 LYS A 90 83.83 83.60 REMARK 500 2 ARG A 94 -47.80 -150.26 REMARK 500 2 LYS A 101 176.28 -59.91 REMARK 500 2 ASP A 102 38.53 -157.27 REMARK 500 2 PHE A 105 -178.47 -59.44 REMARK 500 2 VAL A 109 31.13 -98.45 REMARK 500 2 GLU A 111 78.60 -119.84 REMARK 500 3 GLN A 8 -50.39 -140.62 REMARK 500 3 GLU A 27 -75.30 -56.27 REMARK 500 3 TRP A 29 36.05 -90.72 REMARK 500 3 HIS A 32 -85.23 62.81 REMARK 500 3 LEU A 33 143.93 62.71 REMARK 500 3 ASN A 35 77.61 52.76 REMARK 500 3 LYS A 65 44.47 -107.73 REMARK 500 3 ALA A 93 -59.35 -131.74 REMARK 500 3 ARG A 94 124.55 62.78 REMARK 500 3 ARG A 95 -46.30 -159.36 REMARK 500 3 ALA A 96 77.72 59.53 REMARK 500 3 ASP A 102 75.50 -177.88 REMARK 500 3 PHE A 105 94.50 48.08 REMARK 500 3 GLU A 108 91.55 59.22 REMARK 500 3 GLU A 111 113.36 -163.84 REMARK 500 4 GLN A 8 20.61 -141.72 REMARK 500 4 MET A 9 -177.99 177.31 REMARK 500 4 THR A 31 -90.56 38.78 REMARK 500 REMARK 500 THIS ENTRY HAS 314 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1L4S A 1 112 UNP P0AD49 YFIA_ECOLI 2 113 SEQRES 1 A 112 THR MET ASN ILE THR SER LYS GLN MET GLU ILE THR PRO SEQRES 2 A 112 ALA ILE ARG GLN HIS VAL ALA ASP ARG LEU ALA LYS LEU SEQRES 3 A 112 GLU LYS TRP GLN THR HIS LEU ILE ASN PRO HIS ILE ILE SEQRES 4 A 112 LEU SER LYS GLU PRO GLN GLY PHE VAL ALA ASP ALA THR SEQRES 5 A 112 ILE ASN THR PRO ASN GLY VAL LEU VAL ALA SER GLY LYS SEQRES 6 A 112 HIS GLU ASP MET TYR THR ALA ILE ASN GLU LEU ILE ASN SEQRES 7 A 112 LYS LEU GLU ARG GLN LEU ASN LYS LEU GLN HIS LYS GLY SEQRES 8 A 112 GLU ALA ARG ARG ALA ALA THR SER VAL LYS ASP ALA ASN SEQRES 9 A 112 PHE VAL GLU GLU VAL GLU GLU GLU HELIX 1 1 THR A 12 LEU A 26 1 15 HELIX 2 2 ASP A 68 HIS A 89 1 22 SHEET 1 A 4 ASN A 3 SER A 6 0 SHEET 2 A 4 HIS A 37 GLU A 43 1 O ILE A 38 N ASN A 3 SHEET 3 A 4 GLY A 46 THR A 55 -1 O GLY A 46 N GLU A 43 SHEET 4 A 4 GLY A 58 GLY A 64 -1 O GLY A 58 N THR A 55 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 - b 23 2 Bytes