Header list of 1q0w.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSPORT PROTEIN 17-JUL-03 1Q0W TITLE SOLUTION STRUCTURE OF VPS27 AMINO-TERMINAL UIM-UBIQUITIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN VPS27; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: AMINO-TERMINAL UIM, RESIDUES 256 TO 278; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: UBIQUITIN; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE SEQUENCE WAS SYNTHESIZED USING A PEPTIDE SOURCE 4 SYNTHESIZER. THE SEQUENCE CONTAINS A NON-NATIVE TYROSINE RESIDUE AT SOURCE 5 THE AMINO-TERMINUS (RESIDUE NUMBER 255). THE SEQUENCE OCCURS SOURCE 6 NATURALLY IN S. CEREVISIAE.; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 10 ORGANISM_TAXID: 4932; SOURCE 11 GENE: (UBI1 OR RPL40A OR YIL148W) AND (UBI2 OR RPL40B OR YKR094C) SOURCE 12 AND (UBI3 OR RPS31 OR YLR167W OR L9470.14) AND (UBI4 OR SCD2 OR SOURCE 13 YLL039C); SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3-A KEYWDS PROTEIN-PROTEIN COMPLEX, TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.A.SWANSON,R.S.KANG,S.D.STAMENOVA,L.HICKE,I.RADHAKRISHNAN REVDAT 3 27-OCT-21 1Q0W 1 REMARK SEQADV REVDAT 2 24-FEB-09 1Q0W 1 VERSN REVDAT 1 07-OCT-03 1Q0W 0 JRNL AUTH K.A.SWANSON,R.S.KANG,S.D.STAMENOVA,L.HICKE,I.RADHAKRISHNAN JRNL TITL SOLUTION STRUCTURE OF VPS27 UIM-UBIQUITIN COMPLEX IMPORTANT JRNL TITL 2 FOR ENDOSOMAL SORTING AND RECEPTOR DOWNREGULATION JRNL REF EMBO J. V. 22 4597 2003 JRNL REFN ISSN 0261-4189 JRNL PMID 12970172 JRNL DOI 10.1093/EMBOJ/CDG471 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1B, CNS 1.1, ARIA 1.2 REMARK 3 AUTHORS : VARIAN INSTRUMENTS (VNMR), BRUNGER ET AL. (CNS), REMARK 3 LINGE AND NILGES (ARIA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2138 DISTANCE RESTRAINTS, INCLUDING 2062 NOE-DERIVED DISTANCE REMARK 3 RESTRAINTS [1625 UNAMBIGUOUS AND 437 AMBIGUOUS RESTRAINTS], 76 REMARK 3 HYDROGEN BONDING DISTANCE RESTRAINTS, AND 112 TORSION ANGLE REMARK 3 RESTRAINTS. REMARK 4 REMARK 4 1Q0W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-03. REMARK 100 THE DEPOSITION ID IS D_1000019776. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE, PH 6.0, REMARK 210 0.2% NAN3 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C UBIQUITIN + 1 MM REMARK 210 VPS27 AMINO-TERMINAL UIM; 1 MM U- REMARK 210 15N,13C UBIQUITIN + 1 MM VPS27 REMARK 210 AMINO-TERMINAL UIM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D REMARK 210 DOUBLE HALF-FILTERED NOESY; 3D_ REMARK 210 13C-SEPARATED_NOESY; 3D 13C- REMARK 210 FILTERED,13C-EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 98.0 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND REMARK 210 SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMERS ARE THE REMARK 210 20 STRUCTURES WITH THE LOWEST REMARK 210 RESTRAINT ENERGIES, RESTRAINT REMARK 210 VIOLATIONS, AND RMS DEVIATIONS REMARK 210 FROM IDEAL COVALENT GEOMETRY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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: 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 PRO A 256 47.98 -78.17 REMARK 500 1 GLU A 257 52.12 -145.11 REMARK 500 1 SER A 274 41.96 -80.25 REMARK 500 1 ASN A 276 42.22 -79.97 REMARK 500 1 ASP B 52 49.44 -76.76 REMARK 500 2 PRO A 256 38.96 -76.94 REMARK 500 2 GLU A 257 135.14 63.61 REMARK 500 2 SER A 274 47.48 -81.92 REMARK 500 2 ASN A 276 -127.05 56.90 REMARK 500 2 SER A 277 -140.52 -69.76 REMARK 500 2 THR B 7 -151.50 -74.05 REMARK 500 2 THR B 9 54.85 -153.42 REMARK 500 2 ARG B 74 130.83 -173.28 REMARK 500 3 ARG A 275 34.04 -75.06 REMARK 500 3 ASN A 276 45.55 -82.55 REMARK 500 3 LEU B 8 43.62 -75.04 REMARK 500 3 THR B 9 33.02 -149.57 REMARK 500 3 VAL B 17 -156.74 -148.80 REMARK 500 3 ARG B 72 47.34 -76.78 REMARK 500 3 LEU B 73 131.91 64.40 REMARK 500 4 THR B 22 -152.98 -71.67 REMARK 500 4 GLU B 51 -156.19 -67.35 REMARK 500 4 ASP B 52 43.25 -142.28 REMARK 500 4 LEU B 73 -135.37 49.52 REMARK 500 5 PRO A 256 -134.70 -66.27 REMARK 500 5 SER A 274 39.34 -86.55 REMARK 500 5 SER A 277 41.99 -80.58 REMARK 500 5 SER B 20 39.31 -86.04 REMARK 500 5 ARG B 74 -44.93 -176.72 REMARK 500 6 GLU A 257 135.15 66.47 REMARK 500 6 SER A 277 -143.98 57.67 REMARK 500 6 LEU B 8 -103.76 51.87 REMARK 500 6 THR B 9 58.46 -153.46 REMARK 500 6 LYS B 33 -70.53 -67.12 REMARK 500 6 LEU B 73 133.14 61.28 REMARK 500 7 SER A 277 -43.43 74.00 REMARK 500 7 THR B 9 -46.05 -152.30 REMARK 500 7 THR B 22 -173.47 -69.11 REMARK 500 7 ASP B 52 49.31 -76.45 REMARK 500 8 ARG A 275 -133.15 58.12 REMARK 500 8 SER A 277 44.57 -179.30 REMARK 500 8 THR B 22 -158.16 -78.70 REMARK 500 8 GLU B 51 -148.47 -68.71 REMARK 500 8 ASP B 52 45.34 -151.30 REMARK 500 8 ARG B 74 135.57 66.06 REMARK 500 9 GLU A 257 -64.78 -144.61 REMARK 500 9 SER A 274 48.03 -84.12 REMARK 500 9 ASN A 276 53.87 -175.63 REMARK 500 9 SER A 277 -49.58 -172.61 REMARK 500 9 SER B 20 39.06 -92.31 REMARK 500 REMARK 500 THIS ENTRY HAS 113 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 AUTHOR DETERMINED SECONDARY STRUCTURE REMARK 700 REMARK 700 SHEET REMARK 700 AUTHOR DETERMINED SECONDARY STRUCTURE REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Q0V RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF TANDEM UIMS OF VPS27 REMARK 900 RELATED ID: 1O06 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE VPS27 CARBOXY-TERMINAL UIM DBREF 1Q0W A 255 278 UNP P40343 VPS27_YEAST 256 279 DBREF 1Q0W B 1 76 UNP P61864 UBIQ_YEAST 1 76 SEQADV 1Q0W TYR A 255 UNP P40343 THR 256 ENGINEERED MUTATION SEQRES 1 A 24 TYR PRO GLU ASP GLU GLU GLU LEU ILE ARG LYS ALA ILE SEQRES 2 A 24 GLU LEU SER LEU LYS GLU SER ARG ASN SER ALA SEQRES 1 B 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE SEQRES 2 B 76 THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL SEQRES 3 B 76 LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP SEQRES 4 B 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP SEQRES 5 B 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER SEQRES 6 B 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY HELIX 1 1 ASP A 258 GLU A 273 1 16 HELIX 2 2 THR B 22 GLU B 34 5 13 HELIX 3 3 LEU B 56 TYR B 59 1 4 SHEET 1 A 5 THR B 12 GLU B 16 0 SHEET 2 A 5 GLN B 2 THR B 7 -1 N VAL B 5 O ILE B 13 SHEET 3 A 5 THR B 66 LEU B 71 1 O LEU B 67 N LYS B 6 SHEET 4 A 5 GLN B 41 PHE B 45 -1 N ILE B 44 O HIS B 68 SHEET 5 A 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45 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 - t 27 2 Bytes