Header list of 1otr.pdb file
Complete list - b 23 2 Bytes
HEADER CELL CYCLE 22-MAR-03 1OTR
TITLE SOLUTION STRUCTURE OF A CUE-UBIQUITIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN CUE2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AMINO-TERMINAL CUE DOMAIN, RESIDUES 6-54;
COMPND 5 SYNONYM: HYPOTHETICAL 50.9 KD PROTEIN IN BUD2-MIF2 INTERGENIC REGION;
COMPND 6 HYPOTHETICAL PROTEIN YKL090W;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN;
COMPND 10 CHAIN: B;
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 GENE: CUE2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: UBI1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-3A
KEYWDS PROTEIN-PROTEIN COMPLEX, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.S.KANG,C.M.DANIELS,W.J.SALERNO,I.RADHAKRISHNAN
REVDAT 3 23-FEB-22 1OTR 1 REMARK
REVDAT 2 24-FEB-09 1OTR 1 VERSN
REVDAT 1 24-JUN-03 1OTR 0
JRNL AUTH R.S.KANG,C.M.DANIELS,S.A.FRANCIS,S.C.SHIH,W.J.SALERNO,
JRNL AUTH 2 L.HICKE,I.RADHAKRISHNAN
JRNL TITL SOLUTION STRUCTURE OF A CUE-UBIQUITIN COMPLEX REVEALS A
JRNL TITL 2 CONSERVED MODE OF UBIQUITIN BINDING
JRNL REF CELL(CAMBRIDGE,MASS.) V. 113 621 2003
JRNL REFN ISSN 0092-8674
JRNL PMID 12787503
JRNL DOI 10.1016/S0092-8674(03)00362-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, ARIA 1.2, CNS 1.1
REMARK 3 AUTHORS : VARIAN (VNMR), LINGE AND NILGES (ARIA), BRUNGER ET
REMARK 3 AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 3328 DISTANCE RESTRAINTS,
REMARK 3 INCLUDING 3238 NOE-DERIVED DISTANCE RESTRAINTS [2560 UNAMBIGUOUS
REMARK 3 AND 678 AMBIGUOUS RESTRAINTS], 90 HYDROGEN BONDING DISTANCE
REMARK 3 RESTRAINTS,
REMARK 3 AND 150 TORSION ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1OTR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018659.
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 : 20 MM SODIUM PHOSPHATE, PH 7.0,
REMARK 210 0.2% NAN3
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM U-15N,13C CUE2 + 1 MM
REMARK 210 UBIQUITIN; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 0.2%
REMARK 210 NAN3; 1 MM U-15N,13C CUE2 + 1 MM
REMARK 210 UBIQUITIN; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 0.2%
REMARK 210 NAN3; 1 MM CUE2 + 1 MM U-15N,13C
REMARK 210 UBIQUITIN; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 0.2%
REMARK 210 NAN3; 1 MM CUE2 + 1 MM U-15N,13C
REMARK 210 UBIQUITIN; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, PH 7.0, 0.2%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C-FILTERED,_13C-EDITED_NOESY; 2D_DOUBLE_
REMARK 210 HALF-FILTERED_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 AND 2000, CNS 1.1,
REMARK 210 ARIA 1.2
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 CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST RESTRAINT ENERGIES,
REMARK 210 RESTRAINT VIOLATIONS, AND RMS
REMARK 210 DEVIATIONS FROM IDEAL COVALENT
REMARK 210 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: 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 ASP A 7 -39.04 -151.63
REMARK 500 1 ASP A 8 39.48 -150.67
REMARK 500 1 ALA A 22 -41.22 -163.53
REMARK 500 1 ASN A 35 33.65 -77.74
REMARK 500 1 ASN A 50 45.78 -79.87
REMARK 500 1 ASP A 52 134.98 -176.67
REMARK 500 1 ASP B 21 -126.88 -83.06
REMARK 500 1 LYS B 48 138.94 -173.19
REMARK 500 1 GLN B 62 -154.64 -76.75
REMARK 500 1 ARG B 74 -141.22 59.27
REMARK 500 2 ASP A 8 54.60 -174.81
REMARK 500 2 ALA A 22 -44.38 -168.37
REMARK 500 2 ASN A 36 -72.96 64.57
REMARK 500 2 ASN A 37 -30.33 -162.09
REMARK 500 2 ASP A 38 123.04 -39.27
REMARK 500 2 LYS A 48 43.00 -80.83
REMARK 500 2 ASN A 50 39.74 -81.05
REMARK 500 2 ASP A 52 129.89 63.97
REMARK 500 2 ASP B 21 -123.38 -84.29
REMARK 500 2 THR B 22 141.35 -171.72
REMARK 500 2 TYR B 59 31.91 -85.74
REMARK 500 2 LYS B 63 140.74 -179.93
REMARK 500 2 ARG B 74 133.34 64.31
REMARK 500 3 ASP A 7 -47.19 75.78
REMARK 500 3 ALA A 22 -39.76 -165.74
REMARK 500 3 ASN A 35 38.69 -81.23
REMARK 500 3 LYS A 48 39.77 -78.93
REMARK 500 3 ASN A 50 41.60 -90.07
REMARK 500 3 ASP A 51 133.95 -176.15
REMARK 500 3 ASP A 52 132.94 -171.09
REMARK 500 3 LYS B 11 116.12 -164.68
REMARK 500 3 SER B 20 36.60 -92.39
REMARK 500 3 ASP B 21 -134.04 -80.52
REMARK 500 3 THR B 22 143.70 -175.94
REMARK 500 3 GLU B 34 -32.19 -140.40
REMARK 500 3 ALA B 46 -34.25 69.43
REMARK 500 3 LEU B 50 35.96 -82.87
REMARK 500 3 GLU B 51 -167.26 51.16
REMARK 500 3 ARG B 74 46.87 -173.63
REMARK 500 4 ASP A 7 138.12 69.30
REMARK 500 4 ASP A 8 40.03 -76.06
REMARK 500 4 ALA A 22 -42.93 -166.93
REMARK 500 4 ASN A 35 37.48 -77.64
REMARK 500 4 ASN A 50 -133.15 -69.62
REMARK 500 4 ASP A 51 -24.32 71.79
REMARK 500 4 LYS A 53 -43.31 -169.57
REMARK 500 4 LEU B 8 102.13 -42.60
REMARK 500 4 LYS B 11 139.28 -172.88
REMARK 500 4 SER B 19 43.54 -77.35
REMARK 500 4 SER B 20 49.68 -168.58
REMARK 500
REMARK 500 THIS ENTRY HAS 272 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OTR A 6 54 UNP P36075 CUE2_YEAST 6 54
DBREF 1OTR B 1 76 UNP P61864 UBIQ_YEAST 1 76
SEQRES 1 A 49 ASN ASP ASP HIS GLU SER LYS LEU SER ILE LEU MET ASP
SEQRES 2 A 49 MET PHE PRO ALA ILE SER LYS SER LYS LEU GLN VAL HIS
SEQRES 3 A 49 LEU LEU GLU ASN ASN ASN ASP LEU ASP LEU THR ILE GLY
SEQRES 4 A 49 LEU LEU LEU LYS GLU ASN ASP ASP LYS SER
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 HIS A 9 MET A 19 1 11
HELIX 2 2 LYS A 25 GLU A 34 1 10
HELIX 3 3 LEU A 39 LEU A 47 1 9
HELIX 4 4 ILE B 23 GLU B 34 1 12
HELIX 5 5 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 ILE B 3 O LEU B 15
SHEET 3 A 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4
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 - b 23 2 Bytes