HEADER LIGASE 27-SEP-10 2L3Z
TITLE PROTON-DETECTED 4D DREAM SOLID-STATE NMR STRUCTURE OF UBIQUITIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-76;
COMPND 5 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: UBC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21
KEYWDS SOLID-STATE NMR STRUCTURE, SPARSE ISOTOPE LABELLING, LIGASE
EXPDTA SOLID-STATE NMR
NUMMDL 20
AUTHOR M.HUBER,S.HILLER,P.SCHANDA,M.ERNST,A.BOCKMANN,R.VEREL,B.H.MEIER
REVDAT 2 13-APR-11 2L3Z 1 JRNL
REVDAT 1 16-FEB-11 2L3Z 0
JRNL AUTH M.HUBER,S.HILLER,P.SCHANDA,M.ERNST,A.BOCKMANN,R.VEREL,
JRNL AUTH 2 B.H.MEIER
JRNL TITL A PROTON-DETECTED 4D SOLID-STATE NMR EXPERIMENT FOR PROTEIN
JRNL TITL 2 STRUCTURE DETERMINATION.
JRNL REF CHEMPHYSCHEM V. 12 915 2011
JRNL REFN
JRNL PMID 21442705
JRNL DOI 10.1002/CPHC.201100062
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2L3Z COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-10.
REMARK 100 THE RCSB ID CODE IS RCSB101927.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.1
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 100 % [U-13C; U-15N; U-2H]
REMARK 210 UBIQUITIN, 20% H2O, 80% D2O IN
REMARK 210 CRYSTALLIZATION BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D 13C-1H-1H-13C METHYL-METHYL
REMARK 210 DREAM (DIPOLAR); 3D 1H-15N-1H
REMARK 210 DREAM
REMARK 210 SPECTROMETER FIELD STRENGTH : 850 MHZ
REMARK 210 SPECTROMETER MODEL : ADVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 STRUCTURES FOR LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 217
REMARK 217 SOLID STATE NMR STUDY
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 217 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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 4 ARG A 54 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 GLU A 64 16.40 52.65
REMARK 500 2 LYS A 11 -63.70 -94.00
REMARK 500 2 GLU A 64 16.62 53.31
REMARK 500 3 GLU A 64 16.13 52.16
REMARK 500 4 LYS A 11 33.10 -74.49
REMARK 500 5 GLU A 64 16.71 51.71
REMARK 500 7 GLU A 64 16.23 51.96
REMARK 500 8 THR A 9 6.94 -67.21
REMARK 500 8 ARG A 72 -61.03 -109.77
REMARK 500 9 LEU A 73 55.38 26.15
REMARK 500 10 LEU A 8 -9.59 -57.09
REMARK 500 11 ARG A 72 159.03 179.08
REMARK 500 12 THR A 9 117.36 -160.12
REMARK 500 16 GLU A 64 17.84 54.25
REMARK 500 17 LEU A 71 -167.99 -123.10
REMARK 500 17 ARG A 72 -51.29 -127.71
REMARK 500 18 LYS A 11 106.53 -58.84
REMARK 500 18 LEU A 73 -151.18 -99.71
REMARK 500 19 GLU A 64 15.58 58.00
REMARK 500 20 GLU A 64 18.35 55.28
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 54 0.08 SIDE CHAIN
REMARK 500 3 ARG A 72 0.09 SIDE CHAIN
REMARK 500 11 ARG A 74 0.11 SIDE CHAIN
REMARK 500 13 ARG A 72 0.10 SIDE CHAIN
REMARK 500 14 TYR A 59 0.07 SIDE CHAIN
REMARK 500 14 ARG A 72 0.10 SIDE CHAIN
REMARK 500 15 ARG A 72 0.08 SIDE CHAIN
REMARK 500 16 ARG A 54 0.11 SIDE CHAIN
REMARK 500 18 ARG A 54 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2L3Z A 1 76 UNP P0CG48 UBC_HUMAN 1 76
SEQRES 1 A 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 A 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 A 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 A 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 A 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 A 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HELIX 1 1 THR A 22 GLY A 35 1 14
HELIX 2 2 PRO A 37 GLN A 41 5 5
SHEET 1 A 4 PHE A 4 THR A 7 0
SHEET 2 A 4 THR A 66 VAL A 70 1 O LEU A 67 N LYS A 6
SHEET 3 A 4 ARG A 42 PHE A 45 -1 N ARG A 42 O VAL A 70
SHEET 4 A 4 LYS A 48 GLN A 49 -1 O LYS A 48 N PHE A 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
(ATOM LINES ARE NOT SHOWN.)
END
