Header list of 1l7y.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-MAR-02 1L7Y
TITLE SOLUTION NMR STRUCTURE OF C. ELEGANS PROTEIN ZK652.3. NORTHEAST
TITLE 2 STRUCTURAL GENOMICS CONSORTIUM TARGET WR41.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN ZK652.3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: ZK652.3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS C.ELEGANS, UNKNOWN FUNCTION, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, ZK652.3, UBIQUITIN FOLD, BETA-GRASP FOLD, UFM1,
KEYWDS 3 UBIQUITIN-FOLD MODIFIER 1, NESG, STRUCTURAL GENOMICS, STRUCTURAL
KEYWDS 4 PROTEOMICS, HYPOTHETICAL, PSI, PROTEIN STRUCTURE INITIATIVE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR J.R.CORT,Y.CHIANG,D.ZHENG,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 23-FEB-22 1L7Y 1 REMARK
REVDAT 4 24-FEB-09 1L7Y 1 VERSN
REVDAT 3 27-MAY-08 1L7Y 1 KEYWDS
REVDAT 2 25-JAN-05 1L7Y 1 AUTHOR KEYWDS REMARK
REVDAT 1 14-AUG-02 1L7Y 0
JRNL AUTH J.R.CORT,Y.CHIANG,D.ZHENG,G.T.MONTELIONE,M.A.KENNEDY
JRNL TITL NMR STRUCTURE OF CONSERVED EUKARYOTIC PROTEIN ZK652.3 FROM
JRNL TITL 2 C. ELEGANS: A UBIQUITIN-LIKE FOLD.
JRNL REF PROTEINS V. 48 733 2002
JRNL REFN ISSN 0887-3585
JRNL PMID 12211038
JRNL DOI 10.1002/PROT.10197
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.840
REMARK 3 AUTHORS : VARIAN, INC. (VNMR), A.T. BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE X-PLOR ROUTINES DG_FULL_EMBED.INP,
REMARK 3 DGSA.INP, AND REFINE_GENTLE.INP WERE USED TO PRODUCE THE
REMARK 3 STRUCTURAL ENSEMBLE
REMARK 4
REMARK 4 1L7Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015728.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 10 MM AMMONIUM ACETATE, 50 MM
REMARK 210 NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM 99%-13C,99%-15N-ZK652.3
REMARK 210 10 MM AMMONIUM ACETATE, 50 MM
REMARK 210 NACL, 10 MM DTT, 5% D2O, PH 5.5;
REMARK 210 0.9 MM 13C,15N-ZK652.3 10 MM
REMARK 210 AMMONIUM ACETATE, 50 MM NACL, 10
REMARK 210 MM DTT, 99% D2O; 0.9 MM 10%-13C,
REMARK 210 99%-15N-ZK652.3 10 MM AMMONIUM
REMARK 210 ACETATE, 50 MM NACL, 10 MM DTT,
REMARK 210 5% D2O, PH 5.5; 0.9 MM 99%-15N-
REMARK 210 ZK652.3 10 MM AMMONIUM ACETATE,
REMARK 210 50 MM NACL, 10 MM DTT, 5% D2O,
REMARK 210 PH 5.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY;
REMARK 210 3D_SIMULTANEOUS_13C,15N-SEPARATED_NOESY; HNHA; 3D_15N-SEPARATED_
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR 3.840
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 26
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
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: 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 ALA A 70 -41.72 -132.96
REMARK 500 2 THR A 5 -70.40 -112.20
REMARK 500 2 ALA A 6 -120.76 -96.04
REMARK 500 2 ALA A 7 55.10 -103.80
REMARK 500 2 LYS A 25 124.74 67.42
REMARK 500 2 ALA A 70 -42.69 -135.52
REMARK 500 2 SER A 82 -50.87 -124.20
REMARK 500 3 THR A 5 -44.62 -143.03
REMARK 500 3 THR A 8 -72.21 -128.43
REMARK 500 3 THR A 9 -62.83 -138.09
REMARK 500 3 GLU A 83 106.43 -58.20
REMARK 500 4 THR A 5 130.88 67.91
REMARK 500 4 GLU A 35 82.73 -66.62
REMARK 500 4 SER A 36 -38.80 178.77
REMARK 500 4 PHE A 50 -83.26 -83.21
REMARK 500 4 LYS A 51 33.59 174.83
REMARK 500 4 ALA A 70 31.14 -142.34
REMARK 500 4 VAL A 92 -63.59 -107.95
REMARK 500 5 THR A 5 49.05 -155.00
REMARK 500 5 ALA A 10 -61.22 -128.50
REMARK 500 5 LYS A 25 73.48 -167.73
REMARK 500 5 LEU A 26 -66.10 -145.96
REMARK 500 5 GLU A 35 83.23 -64.72
REMARK 500 5 SER A 36 -39.33 -179.13
REMARK 500 5 ALA A 70 34.32 -144.35
REMARK 500 5 ARG A 89 144.26 71.38
REMARK 500 6 SER A 2 97.06 69.37
REMARK 500 6 GLU A 35 83.49 -65.05
REMARK 500 6 SER A 36 -37.62 -179.78
REMARK 500 6 LYS A 51 33.70 76.45
REMARK 500 6 ALA A 70 31.06 -153.80
REMARK 500 6 HIS A 80 -62.81 -93.33
REMARK 500 6 ASP A 90 78.25 -115.93
REMARK 500 7 ALA A 7 34.51 -93.56
REMARK 500 7 THR A 9 135.28 73.89
REMARK 500 7 LEU A 26 -58.22 -176.42
REMARK 500 7 PHE A 50 -81.97 -80.31
REMARK 500 7 LYS A 51 36.27 175.14
REMARK 500 7 ALA A 70 -39.82 -131.72
REMARK 500 7 HIS A 80 -65.28 -90.90
REMARK 500 7 ARG A 89 119.76 69.46
REMARK 500 7 ARG A 91 -153.38 -91.65
REMARK 500 8 ALA A 70 -43.40 -134.84
REMARK 500 8 HIS A 80 -63.42 -100.60
REMARK 500 8 GLU A 83 99.27 -62.81
REMARK 500 8 ASP A 90 106.55 63.90
REMARK 500 9 SER A 2 -55.83 -127.07
REMARK 500 9 THR A 5 -64.19 -105.81
REMARK 500 9 ALA A 70 -48.65 -139.80
REMARK 500 9 HIS A 80 -62.31 -94.19
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 ARG A 85 0.31 SIDE CHAIN
REMARK 500 1 ARG A 89 0.32 SIDE CHAIN
REMARK 500 1 ARG A 91 0.30 SIDE CHAIN
REMARK 500 2 ARG A 85 0.26 SIDE CHAIN
REMARK 500 2 ARG A 89 0.31 SIDE CHAIN
REMARK 500 2 ARG A 91 0.31 SIDE CHAIN
REMARK 500 3 ARG A 85 0.30 SIDE CHAIN
REMARK 500 3 ARG A 89 0.30 SIDE CHAIN
REMARK 500 3 ARG A 91 0.31 SIDE CHAIN
REMARK 500 4 ARG A 85 0.26 SIDE CHAIN
REMARK 500 4 ARG A 89 0.32 SIDE CHAIN
REMARK 500 4 ARG A 91 0.31 SIDE CHAIN
REMARK 500 5 ARG A 85 0.32 SIDE CHAIN
REMARK 500 5 ARG A 89 0.30 SIDE CHAIN
REMARK 500 5 ARG A 91 0.32 SIDE CHAIN
REMARK 500 6 ARG A 85 0.32 SIDE CHAIN
REMARK 500 6 ARG A 89 0.31 SIDE CHAIN
REMARK 500 6 ARG A 91 0.31 SIDE CHAIN
REMARK 500 7 ARG A 85 0.31 SIDE CHAIN
REMARK 500 7 ARG A 89 0.27 SIDE CHAIN
REMARK 500 7 ARG A 91 0.31 SIDE CHAIN
REMARK 500 8 ARG A 85 0.27 SIDE CHAIN
REMARK 500 8 ARG A 89 0.31 SIDE CHAIN
REMARK 500 8 ARG A 91 0.28 SIDE CHAIN
REMARK 500 9 ARG A 85 0.31 SIDE CHAIN
REMARK 500 9 ARG A 89 0.32 SIDE CHAIN
REMARK 500 9 ARG A 91 0.23 SIDE CHAIN
REMARK 500 10 ARG A 85 0.31 SIDE CHAIN
REMARK 500 10 ARG A 89 0.22 SIDE CHAIN
REMARK 500 10 ARG A 91 0.29 SIDE CHAIN
REMARK 500 11 ARG A 85 0.30 SIDE CHAIN
REMARK 500 11 ARG A 89 0.32 SIDE CHAIN
REMARK 500 11 ARG A 91 0.21 SIDE CHAIN
REMARK 500 12 ARG A 85 0.31 SIDE CHAIN
REMARK 500 12 ARG A 89 0.32 SIDE CHAIN
REMARK 500 12 ARG A 91 0.32 SIDE CHAIN
REMARK 500 13 ARG A 85 0.32 SIDE CHAIN
REMARK 500 13 ARG A 89 0.32 SIDE CHAIN
REMARK 500 13 ARG A 91 0.32 SIDE CHAIN
REMARK 500 14 ARG A 85 0.31 SIDE CHAIN
REMARK 500 14 ARG A 89 0.32 SIDE CHAIN
REMARK 500 14 ARG A 91 0.28 SIDE CHAIN
REMARK 500 15 ARG A 85 0.28 SIDE CHAIN
REMARK 500 15 ARG A 89 0.32 SIDE CHAIN
REMARK 500 15 ARG A 91 0.32 SIDE CHAIN
REMARK 500 16 ARG A 85 0.27 SIDE CHAIN
REMARK 500 16 ARG A 89 0.31 SIDE CHAIN
REMARK 500 16 ARG A 91 0.31 SIDE CHAIN
REMARK 500 17 ARG A 85 0.32 SIDE CHAIN
REMARK 500 17 ARG A 89 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 72 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: WR41 RELATED DB: TARGETDB
DBREF 1L7Y A 1 94 UNP P34661 U185_CAEEL 1 94
SEQRES 1 A 94 MET SER GLY GLY THR ALA ALA THR THR ALA GLY SER LYS
SEQRES 2 A 94 VAL THR PHE LYS ILE THR LEU THR SER ASP PRO LYS LEU
SEQRES 3 A 94 PRO PHE LYS VAL LEU SER VAL PRO GLU SER THR PRO PHE
SEQRES 4 A 94 THR ALA VAL LEU LYS PHE ALA ALA GLU GLU PHE LYS VAL
SEQRES 5 A 94 PRO ALA ALA THR SER ALA ILE ILE THR ASN ASP GLY VAL
SEQRES 6 A 94 GLY VAL ASN PRO ALA GLN PRO ALA GLY ASN ILE PHE LEU
SEQRES 7 A 94 LYS HIS GLY SER GLU LEU ARG LEU ILE PRO ARG ASP ARG
SEQRES 8 A 94 VAL GLY HIS
HELIX 1 1 PRO A 38 LYS A 51 1 14
HELIX 2 2 PRO A 72 HIS A 80 1 9
SHEET 1 A 5 LYS A 29 PRO A 34 0
SHEET 2 A 5 LYS A 13 LEU A 20 -1 N VAL A 14 O VAL A 33
SHEET 3 A 5 GLU A 83 PRO A 88 1 O LEU A 86 N THR A 19
SHEET 4 A 5 SER A 57 ILE A 60 -1 N ALA A 58 O ILE A 87
SHEET 5 A 5 GLY A 66 VAL A 67 -1 O VAL A 67 N ILE A 59
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