Header list of 1hv2.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 05-JAN-01 1HV2 TITLE SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPEL- TITLE 2 LINDAU PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ELONGIN C; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ELC1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VON HIPPEL-LINDAU DISEASE TUMOR SUPPRESSOR; COMPND 8 CHAIN: B; COMPND 9 FRAGMENT: RESIDUES 157-171; COMPND 10 SYNONYM: G7 PROTEIN; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 SYNTHETIC: YES; SOURCE 9 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED KEYWDS PROTEIN-PEPTIDE COMPLEX, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.V.BOTUYAN,G.MER,G.-S.YI,C.M.KOTH,D.A.CASE,A.M.EDWARDS,W.J.CHAZIN, AUTHOR 2 C.H.ARROWSMITH REVDAT 6 23-FEB-22 1HV2 1 REMARK REVDAT 5 24-FEB-09 1HV2 1 VERSN REVDAT 4 12-AUG-03 1HV2 1 DBREF REVDAT 3 01-APR-03 1HV2 1 JRNL REVDAT 2 14-JAN-02 1HV2 1 REMARK DBREF CRYST1 MASTER REVDAT 1 06-SEP-01 1HV2 0 JRNL AUTH M.V.BOTUYAN,G.MER,G.S.YI,C.M.KOTH,D.A.CASE,A.M.EDWARDS, JRNL AUTH 2 W.J.CHAZIN,C.H.ARROWSMITH JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF YEAST ELONGIN C IN JRNL TITL 2 COMPLEX WITH A VON HIPPEL-LINDAU PEPTIDE. JRNL REF J.MOL.BIOL. V. 312 177 2001 JRNL REFN ISSN 0022-2836 JRNL PMID 11545595 JRNL DOI 10.1006/JMBI.2001.4938 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.V.BOTUYAN,C.M.KOTH,G.MER,A.CHAKRABARTTY,J.W.CONAWAY, REMARK 1 AUTH 2 R.C.CONAWAY,A.M.EDWARDS,C.H.ARROWSMITH,W.J.CHAZIN REMARK 1 TITL BINDING OF ELONGIN A OR A VON HIPPEL-LINDAU PEPTIDE REMARK 1 TITL 2 STABILIZES THE STRUCTURE OF YEAST ELONGIN C REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 96 9033 1999 REMARK 1 REFN ISSN 0027-8424 REMARK 1 DOI 10.1073/PNAS.96.16.9033 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 3, AMBER 6 REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), CASE ET AL. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HV2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-01. REMARK 100 THE DEPOSITION ID IS D_1000012604. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : U-15; U-15N,13C; 10MM SODIUM REMARK 210 PHOSPHATE BUFFER (PH 7.0); 100 REMARK 210 MM NACL; 7.5 MM DTT; U-15; U-15N, REMARK 210 13C; 10MM SODIUM PHOSPHATE REMARK 210 BUFFER (PH 7.0); 100 MM NACL; REMARK 210 7.5 MM DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY; 3D_ REMARK 210 13C/15N-FILTER-EDITED NOESY; 2D_ REMARK 210 DOUBLE-HALF FILTERED NOESY; 2D_ REMARK 210 DOUBLE-HALF FILTERED COSY; 2D_ REMARK 210 DOUBLE-HALF FILTERED TOCSY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ; 800 REMARK 210 MHZ REMARK 210 SPECTROMETER MODEL : AMX; DRX; DMX; UNITY; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA 2.8, NMRVIEW 3 REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATING REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS REMARK 210 ARE THE 20 STRUCTURES WITH THE REMARK 210 LOWEST 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: 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: 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 SER A 2 69.69 -69.41 REMARK 500 1 GLN A 3 -46.32 72.01 REMARK 500 1 ASP A 4 -1.61 73.08 REMARK 500 1 LYS A 11 -126.12 30.26 REMARK 500 1 GLU A 39 -62.32 -120.44 REMARK 500 1 SER A 40 44.43 -88.56 REMARK 500 1 GLN A 48 -41.85 -176.41 REMARK 500 1 SER A 71 -55.77 70.82 REMARK 500 1 ASP A 73 -64.50 61.77 REMARK 500 1 SER A 98 67.93 37.22 REMARK 500 2 SER A 2 38.69 -77.00 REMARK 500 2 ASP A 4 44.14 -79.17 REMARK 500 2 SER A 26 74.80 -104.32 REMARK 500 2 MET A 32 -74.28 -77.43 REMARK 500 2 ILE A 33 -94.98 35.13 REMARK 500 2 PRO A 36 78.28 -44.94 REMARK 500 2 SER A 40 -116.91 -106.38 REMARK 500 2 LYS A 41 70.79 51.33 REMARK 500 2 GLN A 48 -45.40 -175.17 REMARK 500 2 GLU A 72 -45.88 176.00 REMARK 500 2 ASP A 74 73.27 -68.29 REMARK 500 2 GLU A 79 89.78 -69.61 REMARK 500 2 PRO A 83 78.75 -61.16 REMARK 500 2 THR A 84 -83.11 41.72 REMARK 500 3 ASP A 4 17.76 -69.78 REMARK 500 3 LYS A 11 -56.40 64.80 REMARK 500 3 ASP A 12 -43.75 -163.99 REMARK 500 3 ASP A 13 32.04 -164.78 REMARK 500 3 SER A 26 72.56 -111.78 REMARK 500 3 GLU A 39 -39.40 -139.16 REMARK 500 3 LYS A 47 73.87 -67.62 REMARK 500 3 GLN A 48 -34.62 167.13 REMARK 500 3 GLU A 72 -67.09 38.77 REMARK 500 3 ASP A 75 -98.47 -94.70 REMARK 500 3 PRO A 83 76.58 -61.95 REMARK 500 3 THR A 84 -94.54 42.10 REMARK 500 4 LYS A 11 -109.17 5.86 REMARK 500 4 PRO A 36 46.29 -69.79 REMARK 500 4 GLU A 39 -58.34 -133.52 REMARK 500 4 SER A 40 46.99 -90.75 REMARK 500 4 GLN A 48 -37.19 162.37 REMARK 500 4 GLU A 72 -70.33 62.25 REMARK 500 4 ASP A 74 45.54 -83.96 REMARK 500 4 PRO A 83 77.39 -57.37 REMARK 500 4 THR A 84 -98.49 34.94 REMARK 500 5 LYS A 11 -116.41 8.30 REMARK 500 5 ARG A 38 46.87 -82.36 REMARK 500 5 SER A 40 42.21 -85.64 REMARK 500 5 GLN A 48 -53.79 -162.68 REMARK 500 5 SER A 71 77.56 -69.29 REMARK 500 REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS. 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 1 TYR A 60 0.12 SIDE CHAIN REMARK 500 1 TYR A 63 0.08 SIDE CHAIN REMARK 500 2 TYR A 63 0.08 SIDE CHAIN REMARK 500 2 TYR A 67 0.22 SIDE CHAIN REMARK 500 3 TYR A 60 0.11 SIDE CHAIN REMARK 500 4 TYR A 60 0.07 SIDE CHAIN REMARK 500 5 PHE A 80 0.09 SIDE CHAIN REMARK 500 5 TYR A 96 0.15 SIDE CHAIN REMARK 500 6 TYR A 16 0.08 SIDE CHAIN REMARK 500 8 HIS A 52 0.08 SIDE CHAIN REMARK 500 8 TYR A 60 0.09 SIDE CHAIN REMARK 500 8 TYR A 63 0.11 SIDE CHAIN REMARK 500 9 TYR A 16 0.08 SIDE CHAIN REMARK 500 9 TYR A 60 0.12 SIDE CHAIN REMARK 500 9 TYR A 63 0.13 SIDE CHAIN REMARK 500 10 TYR A 63 0.08 SIDE CHAIN REMARK 500 10 TYR A 67 0.07 SIDE CHAIN REMARK 500 10 PHE A 80 0.09 SIDE CHAIN REMARK 500 16 TYR A 60 0.10 SIDE CHAIN REMARK 500 16 TYR A 63 0.10 SIDE CHAIN REMARK 500 16 TYR A 67 0.07 SIDE CHAIN REMARK 500 16 PHE A 80 0.16 SIDE CHAIN REMARK 500 18 HIS A 52 0.10 SIDE CHAIN REMARK 500 18 TYR A 60 0.09 SIDE CHAIN REMARK 500 18 TYR A 63 0.12 SIDE CHAIN REMARK 500 19 TYR A 63 0.09 SIDE CHAIN REMARK 500 19 TYR A 96 0.08 SIDE CHAIN REMARK 500 20 TYR A 60 0.10 SIDE CHAIN REMARK 500 20 TYR A 63 0.10 SIDE CHAIN REMARK 500 20 ARG B 161 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1HV2 A 1 99 UNP Q03071 Q03071_YEAST 1 99 DBREF 1HV2 B 157 171 UNP P40338 VHL_MOUSE 157 171 SEQRES 1 A 99 MET SER GLN ASP PHE VAL THR LEU VAL SER LYS ASP ASP SEQRES 2 A 99 LYS GLU TYR GLU ILE SER ARG SER ALA ALA MET ILE SER SEQRES 3 A 99 PRO THR LEU LYS ALA MET ILE GLU GLY PRO PHE ARG GLU SEQRES 4 A 99 SER LYS GLY ARG ILE GLU LEU LYS GLN PHE ASP SER HIS SEQRES 5 A 99 ILE LEU GLU LYS ALA VAL GLU TYR LEU ASN TYR ASN LEU SEQRES 6 A 99 LYS TYR SER GLY VAL SER GLU ASP ASP ASP GLU ILE PRO SEQRES 7 A 99 GLU PHE GLU ILE PRO THR GLU MET SER LEU GLU LEU LEU SEQRES 8 A 99 LEU ALA ALA ASP TYR LEU SER ILE SEQRES 1 B 15 THR LEU LYS GLU ARG CYS LEU GLN VAL VAL ARG SER LEU SEQRES 2 B 15 VAL LYS HELIX 1 1 ARG A 20 MET A 24 1 5 HELIX 2 2 SER A 26 GLY A 35 1 10 HELIX 3 3 ASP A 50 SER A 71 1 22 HELIX 4 4 PRO A 83 SER A 98 1 16 HELIX 5 5 THR B 157 LYS B 171 1 15 SHEET 1 A 3 LYS A 14 SER A 19 0 SHEET 2 A 3 PHE A 5 SER A 10 -1 O VAL A 6 N ILE A 18 SHEET 3 A 3 ARG A 43 GLU A 45 1 N ILE A 44 O THR A 7 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