Header list of 1wi8.pdb file
Complete list - v 10 2 Bytes
HEADER BIOSYNTHETIC PROTEIN 28-MAY-04 1WI8 TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF EUKARYOTIC INITIATION TITLE 2 FACTOR 4B COMPND MOL_ID: 1; COMPND 2 MOLECULE: EUKARYOTIC TRANSLATION INITIATION FACTOR 4B; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: EIF-4B; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: RIKEN CDNA ADSE02039; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040301-18; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, STRUCTURAL KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 3 BIOSYNTHETIC PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR S.SUZUKI,Y.MUTO,T.NAGATA,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 10-NOV-21 1WI8 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WI8 1 VERSN REVDAT 1 28-NOV-04 1WI8 0 JRNL AUTH S.SUZUKI,Y.MUTO,T.NAGATA,M.INOUE,T.KIGAWA,T.TERADA, JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN OF EUKARYOTIC JRNL TITL 2 INITIATION FACTOR 4B JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17 REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WI8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023607. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0MM 13C/15N-PROTEIN 20MM D REMARK 210 -TRIS-HCL; 100MM NACL; 1MM D-DTT; REMARK 210 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.901, OLIVIA 1.9.12, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS, REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 PRO A 91 95.30 -69.74 REMARK 500 1 PRO A 104 -179.39 -69.72 REMARK 500 1 VAL A 107 107.97 -52.38 REMARK 500 1 SER A 131 -50.45 -120.38 REMARK 500 1 GLU A 159 120.19 -37.06 REMARK 500 1 GLN A 173 82.64 -67.43 REMARK 500 1 PRO A 181 -177.26 -69.78 REMARK 500 1 SER A 182 129.89 -174.96 REMARK 500 2 SER A 88 117.54 -171.02 REMARK 500 2 PRO A 130 0.97 -69.73 REMARK 500 2 PRO A 133 2.65 -69.80 REMARK 500 3 SER A 179 45.17 34.40 REMARK 500 4 SER A 183 -60.12 -124.55 REMARK 500 5 ASP A 106 32.52 -98.67 REMARK 500 5 SER A 183 162.02 -48.77 REMARK 500 6 SER A 82 141.98 -173.30 REMARK 500 6 LEU A 90 154.96 -36.53 REMARK 500 6 PRO A 104 -165.04 -69.77 REMARK 500 6 GLN A 175 165.73 -43.76 REMARK 500 6 PRO A 181 -177.37 -69.78 REMARK 500 7 SER A 82 42.71 37.99 REMARK 500 7 LYS A 92 35.36 -98.96 REMARK 500 7 GLN A 175 35.07 35.07 REMARK 500 7 ASP A 176 43.62 -89.95 REMARK 500 8 VAL A 107 122.96 -33.24 REMARK 500 8 GLU A 134 35.81 -83.51 REMARK 500 8 ASP A 176 135.87 -171.02 REMARK 500 9 SER A 82 114.87 -174.64 REMARK 500 9 ASP A 106 31.53 -88.53 REMARK 500 9 GLU A 129 138.98 -39.11 REMARK 500 9 PRO A 133 0.92 -69.84 REMARK 500 9 GLU A 159 124.71 -36.62 REMARK 500 9 PRO A 181 -174.90 -69.83 REMARK 500 10 PRO A 91 94.34 -69.75 REMARK 500 10 ARG A 117 146.71 -37.07 REMARK 500 10 GLU A 134 -64.42 -90.25 REMARK 500 11 SER A 82 143.66 -171.87 REMARK 500 11 PRO A 91 99.85 -69.77 REMARK 500 11 ARG A 117 145.05 -34.94 REMARK 500 11 GLU A 134 36.92 -90.75 REMARK 500 12 SER A 82 130.13 -171.26 REMARK 500 12 PRO A 95 -179.86 -69.72 REMARK 500 12 ASN A 102 54.68 38.65 REMARK 500 12 ASP A 106 32.31 -87.28 REMARK 500 12 ARG A 117 146.88 -39.07 REMARK 500 12 PRO A 181 -176.71 -69.76 REMARK 500 13 SER A 86 127.55 -171.31 REMARK 500 13 LYS A 92 37.58 -83.52 REMARK 500 13 LYS A 177 165.42 -46.43 REMARK 500 13 PRO A 181 93.81 -69.80 REMARK 500 REMARK 500 THIS ENTRY HAS 74 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001000201.1 RELATED DB: TARGETDB DBREF 1WI8 A 88 178 UNP P23588 IF4B_HUMAN 88 178 SEQADV 1WI8 GLY A 81 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 82 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 83 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 GLY A 84 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 85 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 86 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 GLY A 87 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 LYS A 164 UNP P23588 ARG 164 ENGINEERED MUTATION SEQADV 1WI8 SER A 179 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 GLY A 180 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 PRO A 181 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 182 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 SER A 183 UNP P23588 CLONING ARTIFACT SEQADV 1WI8 GLY A 184 UNP P23588 CLONING ARTIFACT SEQRES 1 A 104 GLY SER SER GLY SER SER GLY SER ARG LEU PRO LYS SER SEQRES 2 A 104 PRO PRO TYR THR ALA PHE LEU GLY ASN LEU PRO TYR ASP SEQRES 3 A 104 VAL THR GLU GLU SER ILE LYS GLU PHE PHE ARG GLY LEU SEQRES 4 A 104 ASN ILE SER ALA VAL ARG LEU PRO ARG GLU PRO SER ASN SEQRES 5 A 104 PRO GLU ARG LEU LYS GLY PHE GLY TYR ALA GLU PHE GLU SEQRES 6 A 104 ASP LEU ASP SER LEU LEU SER ALA LEU SER LEU ASN GLU SEQRES 7 A 104 GLU SER LEU GLY ASN LYS ARG ILE ARG VAL ASP VAL ALA SEQRES 8 A 104 ASP GLN ALA GLN ASP LYS ASP SER GLY PRO SER SER GLY HELIX 1 1 THR A 108 PHE A 116 1 9 HELIX 2 2 ASP A 146 SER A 155 1 10 HELIX 3 3 LEU A 156 GLU A 158 5 3 SHEET 1 A 4 ILE A 121 ARG A 125 0 SHEET 2 A 4 GLY A 140 PHE A 144 -1 O TYR A 141 N ARG A 125 SHEET 3 A 4 TYR A 96 GLY A 101 -1 N LEU A 100 O GLY A 140 SHEET 4 A 4 ARG A 167 VAL A 170 -1 O ASP A 169 N PHE A 99 SHEET 1 B 2 SER A 160 LEU A 161 0 SHEET 2 B 2 LYS A 164 ARG A 165 -1 O LYS A 164 N LEU A 161 CISPEP 1 PRO A 94 PRO A 95 1 -0.07 CISPEP 2 PRO A 94 PRO A 95 2 -0.10 CISPEP 3 PRO A 94 PRO A 95 3 -0.08 CISPEP 4 PRO A 94 PRO A 95 4 -0.06 CISPEP 5 PRO A 94 PRO A 95 5 -0.10 CISPEP 6 PRO A 94 PRO A 95 6 -0.09 CISPEP 7 PRO A 94 PRO A 95 7 -0.05 CISPEP 8 PRO A 94 PRO A 95 8 -0.07 CISPEP 9 PRO A 94 PRO A 95 9 -0.13 CISPEP 10 PRO A 94 PRO A 95 10 -0.06 CISPEP 11 PRO A 94 PRO A 95 11 -0.02 CISPEP 12 PRO A 94 PRO A 95 12 -0.12 CISPEP 13 PRO A 94 PRO A 95 13 -0.01 CISPEP 14 PRO A 94 PRO A 95 14 -0.06 CISPEP 15 PRO A 94 PRO A 95 15 0.03 CISPEP 16 PRO A 94 PRO A 95 16 -0.03 CISPEP 17 PRO A 94 PRO A 95 17 -0.06 CISPEP 18 PRO A 94 PRO A 95 18 -0.03 CISPEP 19 PRO A 94 PRO A 95 19 -0.02 CISPEP 20 PRO A 94 PRO A 95 20 -0.09 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 - v 10 2 Bytes