Header list of 2sxl.pdb file
Complete list - 3 20 Bytes
HEADER RNA-BINDING DOMAIN 16-JUL-97 2SXL TITLE SEX-LETHAL RBD1, NMR, MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: SEX-LETHAL PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA-BINDING DOMAIN 1 (RBD1), RESIDUES 122 - 209; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER; SOURCE 3 ORGANISM_COMMON: FRUIT FLY; SOURCE 4 ORGANISM_TAXID: 7227; SOURCE 5 CELL_LINE: BL21; SOURCE 6 ORGAN: FRUIT; SOURCE 7 GENE: SEX-LETHAL; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PK7 KEYWDS RNA-BINDING DOMAIN, ALTERNATIVE SPLICING, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS EXPDTA SOLUTION NMR AUTHOR M.INOUE,Y.MUTO,H.SAKAMOTO,T.KIGAWA,K.TAKIO,Y.SHIMURA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 03-NOV-21 2SXL 1 REMARK SEQADV REVDAT 2 24-FEB-09 2SXL 1 VERSN REVDAT 1 22-JUL-98 2SXL 0 JRNL AUTH M.INOUE,Y.MUTO,H.SAKAMOTO,T.KIGAWA,K.TAKIO,Y.SHIMURA, JRNL AUTH 2 S.YOKOYAMA JRNL TITL A CHARACTERISTIC ARRANGEMENT OF AROMATIC AMINO ACID RESIDUES JRNL TITL 2 IN THE SOLUTION STRUCTURE OF THE AMINO-TERMINAL RNA-BINDING JRNL TITL 3 DOMAIN OF DROSOPHILA SEX-LETHAL. JRNL REF J.MOL.BIOL. V. 272 82 1997 JRNL REFN ISSN 0022-2836 JRNL PMID 9299339 JRNL DOI 10.1006/JMBI.1997.1213 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.OUBRIDGE,N.ITO,P.R.EVANS,C.H.TEO,K.NAGAI REMARK 1 TITL CRYSTAL STRUCTURE AT 1.92 A RESOLUTION OF THE RNA-BINDING REMARK 1 TITL 2 DOMAIN OF THE U1A SPLICEOSOMAL PROTEIN COMPLEXED WITH AN RNA REMARK 1 TITL 3 HAIRPIN REMARK 1 REF NATURE V. 372 432 1994 REMARK 1 REFN ISSN 0028-0836 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.L.LEE,R.KANAAR,D.C.RIO,D.E.WEMMER REMARK 1 TITL RESONANCE ASSIGNMENTS AND SOLUTION STRUCTURE OF THE SECOND REMARK 1 TITL 2 RNA-BINDING DOMAIN OF SEX-LETHAL DETERMINED BY REMARK 1 TITL 3 MULTIDIMENSIONAL HETERONUCLEAR MAGNETIC RESONANCE REMARK 1 REF BIOCHEMISTRY V. 33 13775 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 3 REMARK 1 AUTH D.S.GARRETT,P.J.LODI,Y.SHAMOO,K.R.WILLIAMS,G.M.CLORE, REMARK 1 AUTH 2 A.M.GRONENBORN REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE AND FOLDING REMARK 1 TITL 2 TOPOLOGY OF AN RNA BINDING DOMAIN OF MAMMALIAN HNRNP A1 REMARK 1 TITL 3 PROTEIN USING THREE-DIMENSIONAL HETERONUCLEAR MAGNETIC REMARK 1 TITL 4 RESONANCE SPECTROSCOPY REMARK 1 REF BIOCHEMISTRY V. 33 2852 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH M.WITTEKIND,M.GORLACH,M.FRIEDRICHS,G.DREYFUSS,L.MUELLER REMARK 1 TITL 1H, 13C, AND 15N NMR ASSIGNMENTS AND GLOBAL FOLDING PATTERN REMARK 1 TITL 2 OF THE RNA-BINDING DOMAIN OF THE HUMAN HNRNP C PROTEINS REMARK 1 REF BIOCHEMISTRY V. 31 6254 1992 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 5 REMARK 1 AUTH K.NAGAI,C.OUBRIDGE,T.H.JESSEN,J.LI,P.R.EVANS REMARK 1 TITL CRYSTAL STRUCTURE OF THE RNA-BINDING DOMAIN OF THE U1 SMALL REMARK 1 TITL 2 NUCLEAR RIBONUCLEOPROTEIN A REMARK 1 REF NATURE V. 348 515 1990 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS DONE USING THE HYBRID REMARK 3 DISTANCE GEOMETRY/SIMULATED ANNEALING METHOD (NILGES, M., CLORE, REMARK 3 G.M., & GRONENBORN, A.M. (1988) FEBS LETT 229, 317-324) AS REMARK 3 CONTAINED IN X-PLOR PROGRAM VERSION 3.1 (BRUNGER, 1992). THE REMARK 3 RMSD FOR THE BACKBONE COORDINATES OF THE 20 STRUCTURES ACCEPTED REMARK 3 AFTER THE LAST ROUND OF REFINEMENT COMPARED TO THE AVERAGE REMARK 3 COORDINATES WAS 0.86 (FOR RESIDUES INVOLVED IN SECONDARY REMARK 3 STRUCTURE). REMARK 4 REMARK 4 2SXL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178658. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 4.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; ROESY; DQF-COSY; REMARK 210 1H-15N 2D HSQC; 1H-15N 2D HMQC-J; REMARK 210 15N-EDITED NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX500; AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY/ REMARK 210 SIMULATED ANNEALING METHOD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : SMALLEST RESIDUAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 ASN A 3 114.51 136.03 REMARK 500 GLN A 13 -2.23 75.73 REMARK 500 LEU A 23 -64.02 -98.31 REMARK 500 LYS A 40 -67.69 -99.75 REMARK 500 TYR A 47 129.21 161.03 REMARK 500 THR A 53 23.15 47.82 REMARK 500 MET A 56 -77.57 -148.72 REMARK 500 VAL A 64 -73.19 -92.34 REMARK 500 ASN A 66 102.37 -47.44 REMARK 500 ILE A 68 -119.96 -92.33 REMARK 500 VAL A 70 54.76 -101.61 REMARK 500 ARG A 71 18.71 52.28 REMARK 500 ASN A 72 -29.30 -179.33 REMARK 500 LYS A 73 -154.40 -135.21 REMARK 500 TYR A 79 45.13 -83.35 REMARK 500 ARG A 81 55.81 -154.26 REMARK 500 GLU A 85 95.48 45.35 REMARK 500 ILE A 87 141.98 77.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 18 0.13 SIDE CHAIN REMARK 500 ARG A 25 0.28 SIDE CHAIN REMARK 500 ARG A 34 0.21 SIDE CHAIN REMARK 500 ARG A 37 0.25 SIDE CHAIN REMARK 500 ARG A 60 0.31 SIDE CHAIN REMARK 500 ARG A 71 0.08 SIDE CHAIN REMARK 500 ARG A 74 0.23 SIDE CHAIN REMARK 500 ARG A 81 0.31 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MY_001000017.1 RELATED DB: TARGETDB DBREF 2SXL A 1 88 UNP P19339 SXL_DROME 122 209 SEQADV 2SXL TYR A 45 UNP P19339 PHE 166 ENGINEERED MUTATION SEQRES 1 A 88 ALA SER ASN THR ASN LEU ILE VAL ASN TYR LEU PRO GLN SEQRES 2 A 88 ASP MET THR ASP ARG GLU LEU TYR ALA LEU PHE ARG ALA SEQRES 3 A 88 ILE GLY PRO ILE ASN THR CYS ARG ILE MET ARG ASP TYR SEQRES 4 A 88 LYS THR GLY TYR SER TYR GLY TYR ALA PHE VAL ASP PHE SEQRES 5 A 88 THR SER GLU MET ASP SER GLN ARG ALA ILE LYS VAL LEU SEQRES 6 A 88 ASN GLY ILE THR VAL ARG ASN LYS ARG LEU LYS VAL SER SEQRES 7 A 88 TYR ALA ARG PRO GLY GLY GLU SER ILE LYS HELIX 1 H1 THR A 16 GLY A 28 1 13 HELIX 2 H2 GLU A 55 ASN A 66 1 12 SHEET 1 S1 4 ILE A 30 MET A 36 0 SHEET 2 S1 4 TYR A 47 PHE A 52 -1 O PHE A 49 N ARG A 34 SHEET 3 S1 4 ASN A 5 ASN A 9 -1 N LEU A 6 O VAL A 50 SHEET 4 S1 4 LYS A 76 TYR A 79 -1 N LYS A 76 O ASN A 9 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
Complete list - 3 20 Bytes