Header list of 1p9c.pdb file
Complete list - 23 20 Bytes
HEADER LIGAND BINDING PROTEIN 10-MAY-03 1P9C TITLE NMR SOLUTION STRUCTURE OF THE C-TERMINAL UBIQUITIN-INTERACTING MOTIF TITLE 2 OF THE PROTEASOME SUBUNIT S5A COMPND MOL_ID: 1; COMPND 2 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL UBIQUITIN-INTERACTING MOTIF; COMPND 5 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT S5A, RPN10, MULTIUBIQUITIN COMPND 6 CHAIN BINDING PROTEIN, ANTISECRETORY FACTOR-1, AF, ASF; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: PSMD4 OR MCB1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ALPHA HELIX, HAIRPIN LOOP, LIGAND BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR T.D.MUELLER,J.FEIGON REVDAT 3 23-FEB-22 1P9C 1 REMARK REVDAT 2 24-FEB-09 1P9C 1 VERSN REVDAT 1 07-OCT-03 1P9C 0 JRNL AUTH T.D.MUELLER,J.FEIGON JRNL TITL STRUCTURAL DETERMINANTS FOR THE BINDING OF UBIQUITIN-LIKE JRNL TITL 2 DOMAINS TO THE PROTEASOME. JRNL REF EMBO J. V. 22 4634 2003 JRNL REFN ISSN 0261-4189 JRNL PMID 12970176 JRNL DOI 10.1093/EMBOJ/CDG467 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.1 REMARK 3 AUTHORS : BRUKER KARLSRUHE (XWINNMR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 474 DISTANCE RESTRAINTS, 452 ARE NOE-DERIVED DISTANCE RESTRAINTS, REMARK 3 22 ARE FROM HYDROGEN BONDS REMARK 4 REMARK 4 1P9C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-03. REMARK 100 THE DEPOSITION ID IS D_1000019170. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 150MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM S5A PEPTIDE, UNLABELED; 2MM REMARK 210 S5A PEPTIDE U-15N,13C REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 2.8.9, X-PLOR 3.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 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 STANDARD TRIPLE REMARK 210 -RESONANCE NMR SPECTROSCOPY TECHNIQUES 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 ILE A 265 -34.52 174.44 REMARK 500 1 SER A 266 -75.12 79.06 REMARK 500 1 GLN A 267 -46.31 85.60 REMARK 500 1 PHE A 270 -65.24 173.85 REMARK 500 1 PRO A 276 -152.81 -56.21 REMARK 500 1 ASP A 277 42.77 -106.30 REMARK 500 1 THR A 282 -84.62 24.65 REMARK 500 1 ALA A 298 -53.46 -179.18 REMARK 500 1 GLU A 304 45.20 -161.97 REMARK 500 1 SER A 305 45.56 -152.38 REMARK 500 2 THR A 264 -85.28 -117.26 REMARK 500 2 ILE A 265 -88.58 -61.86 REMARK 500 2 SER A 266 159.53 55.35 REMARK 500 2 GLU A 269 63.09 173.49 REMARK 500 2 PHE A 270 -32.80 179.22 REMARK 500 2 PRO A 276 -86.56 -87.34 REMARK 500 2 ASP A 277 -74.66 73.84 REMARK 500 2 LEU A 278 -26.09 84.11 REMARK 500 2 SER A 280 25.25 -147.99 REMARK 500 2 THR A 282 -92.22 22.58 REMARK 500 2 ALA A 298 -80.68 168.19 REMARK 500 2 GLU A 299 94.77 164.25 REMARK 500 2 PHE A 300 63.00 67.50 REMARK 500 2 ALA A 306 -54.50 85.26 REMARK 500 3 ILE A 265 34.98 -98.85 REMARK 500 3 GLU A 269 29.76 43.04 REMARK 500 3 ARG A 272 69.95 155.92 REMARK 500 3 LEU A 275 -42.83 115.32 REMARK 500 3 ASP A 277 46.99 36.37 REMARK 500 3 SER A 280 -34.26 -130.52 REMARK 500 3 THR A 282 -91.55 21.48 REMARK 500 3 LEU A 295 32.56 35.30 REMARK 500 3 GLN A 296 29.09 -154.12 REMARK 500 3 GLU A 299 -61.11 84.85 REMARK 500 3 ALA A 306 -167.42 56.85 REMARK 500 4 THR A 264 50.12 -98.37 REMARK 500 4 GLN A 268 48.95 36.81 REMARK 500 4 GLU A 269 67.90 -153.72 REMARK 500 4 PHE A 270 -50.21 -173.97 REMARK 500 4 ARG A 272 -18.99 154.64 REMARK 500 4 THR A 273 -24.65 91.03 REMARK 500 4 LEU A 278 -18.51 71.77 REMARK 500 4 THR A 282 -84.32 24.69 REMARK 500 4 GLU A 299 85.90 58.48 REMARK 500 4 PHE A 300 109.75 57.16 REMARK 500 4 GLN A 302 -81.42 -105.14 REMARK 500 4 GLU A 304 24.75 49.73 REMARK 500 4 ALA A 306 -171.30 -172.37 REMARK 500 5 THR A 264 57.88 -106.02 REMARK 500 5 ILE A 265 -35.13 177.05 REMARK 500 REMARK 500 THIS ENTRY HAS 132 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1P98 RELATED DB: PDB REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE UBIQUITIN-LIKE DOMAIN OF HHR23A REMARK 900 RELATED ID: 1P9D RELATED DB: PDB REMARK 900 HIGH-RESOLUTION STRUCTURE OF THE COMPLEX OF HHR23A UBIQUITIN-LIKE REMARK 900 DOMAIN AND THE C-TERMINAL UBIQUITIN-INTERACTING MOTIF OF PROTEASOME REMARK 900 SUBUNIT S5A DBREF 1P9C A 263 307 UNP P55036 PSD4_HUMAN 263 307 SEQRES 1 A 45 MET THR ILE SER GLN GLN GLU PHE GLY ARG THR GLY LEU SEQRES 2 A 45 PRO ASP LEU SER SER MET THR GLU GLU GLU GLN ILE ALA SEQRES 3 A 45 TYR ALA MET GLN MET SER LEU GLN GLY ALA GLU PHE GLY SEQRES 4 A 45 GLN ALA GLU SER ALA ASP HELIX 1 1 ASP A 277 LEU A 295 1 19 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 - 23 20 Bytes