Header list of 1g6j.pdb file
Complete list - b 23 2 Bytes
HEADER GENE REGULATION, CELL CYCLE 06-NOV-00 1G6J
TITLE STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS REVERSE MICELLE, AOT, ENCAPSULATION, GENE REGULATION, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR C.R.BABU,P.F.FLYNN,A.J.WAND
REVDAT 3 23-FEB-22 1G6J 1 REMARK
REVDAT 2 24-FEB-09 1G6J 1 VERSN
REVDAT 1 28-MAR-01 1G6J 0
JRNL AUTH C.R.BABU,P.F.FLYNN,A.J.WAND
JRNL TITL VALIDATION OF PROTEIN STRUCTURE FROM PREPARATIONS OF
JRNL TITL 2 ENCAPSULATED PROTEINS DISSOLVED IN LOW VISCOSITY FLUIDS.
JRNL REF J.AM.CHEM.SOC. V. 123 2691 2001
JRNL REFN ISSN 0002-7863
JRNL PMID 11456950
JRNL DOI 10.1021/JA005766D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.J.WAND,M.R.EHRHARDT,P.F.FLYNN
REMARK 1 TITL HIGH-RESOLUTION NMR OF ENCAPSULATED PROTEINS DISSOLVED IN
REMARK 1 TITL 2 LOW-VISCOSITY FLUIDS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 15299 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.95.26.15299
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.R.EHRHARDT,P.F.FLYNN,A.J.WAND
REMARK 1 TITL PREPARATION OF ENCAPSULATED PROTEINS DISSOLVED IN LOW
REMARK 1 TITL 2 VISCOSITY FLUIDS
REMARK 1 REF J.BIOMOL.NMR V. 14 75 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008354507250
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, P., MUMENTHALER, C., WUTHRICH, K.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1805 NOES
REMARK 3 AND 63 PHI RESTRAINTS
REMARK 4
REMARK 4 1G6J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012295.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293
REMARK 210 PH : NULL; NULL
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; 50 PSI
REMARK 210 SAMPLE CONTENTS : 4 MG C13/N15 UBIQUITIN IN 13.5
REMARK 210 UL OF BUFFER (50MM SODIUM
REMARK 210 ACETATE, 250MM SODIUM CHLORIDE,
REMARK 210 PH 5.0) AND 1 ML D12-PENTANE; 8
REMARK 210 MG 13/N15 UBIQUITIN IN 27 UL OF
REMARK 210 BUFFER (50MM SODIUM ACETATE,
REMARK 210 250MM SODIUM CHLORIDE, PH 5.0);
REMARK 210 4 MG N15 UBIQUITIN IN 13.5 UL OF
REMARK 210 BUFFER (50MM SODIUM ACETATE,
REMARK 210 250MM SODIUM CHLORIDE, PH 5.0)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 97, XEASY 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS USING
REMARK 210 DYANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION VALUES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 25
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: 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: 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 LYS A 33 -73.21 -77.13
REMARK 500 1 LEU A 73 -72.95 -80.05
REMARK 500 1 ARG A 74 -149.56 -86.20
REMARK 500 2 LYS A 33 -70.03 -79.10
REMARK 500 2 ASP A 52 104.76 -47.41
REMARK 500 2 ARG A 74 -153.50 -90.16
REMARK 500 3 LYS A 33 -73.05 -74.72
REMARK 500 3 ASP A 52 104.00 -47.01
REMARK 500 3 ARG A 74 -149.98 -90.19
REMARK 500 4 LYS A 33 -73.02 -74.84
REMARK 500 4 ASP A 52 104.22 -47.17
REMARK 500 4 ARG A 74 -150.69 -90.15
REMARK 500 5 THR A 9 44.41 -99.73
REMARK 500 5 LYS A 33 -74.81 -75.41
REMARK 500 5 ASP A 52 102.65 -46.96
REMARK 500 5 ARG A 74 -150.02 -90.11
REMARK 500 6 LYS A 33 -71.13 -79.73
REMARK 500 6 ASP A 52 105.63 -47.05
REMARK 500 6 ARG A 74 -156.27 -90.39
REMARK 500 7 LYS A 33 -75.12 -74.41
REMARK 500 7 ARG A 74 -149.94 -90.10
REMARK 500 8 ARG A 74 -150.18 -90.25
REMARK 500 9 LYS A 33 -74.94 -77.29
REMARK 500 9 LEU A 73 -73.56 -78.55
REMARK 500 10 THR A 9 39.87 -99.71
REMARK 500 10 LYS A 33 -77.50 -74.74
REMARK 500 10 ASP A 52 104.00 -46.77
REMARK 500 10 LEU A 73 -71.96 -79.45
REMARK 500 10 ARG A 74 -150.32 -90.34
REMARK 500 11 ASP A 52 104.81 -47.42
REMARK 500 11 ASN A 60 66.20 60.85
REMARK 500 11 LEU A 73 -70.84 -79.58
REMARK 500 11 ARG A 74 -150.03 -90.09
REMARK 500 12 THR A 9 43.82 -99.48
REMARK 500 12 LYS A 33 -72.46 -74.73
REMARK 500 12 ASP A 52 104.01 -47.35
REMARK 500 12 LEU A 73 -71.28 -77.30
REMARK 500 12 ARG A 74 -153.70 -90.35
REMARK 500 13 LYS A 33 -74.87 -74.64
REMARK 500 13 ARG A 74 -150.21 -90.07
REMARK 500 14 LYS A 33 -71.53 -74.58
REMARK 500 14 ASP A 52 106.35 -47.41
REMARK 500 14 ARG A 74 -149.93 -87.44
REMARK 500 15 LYS A 33 -78.23 -75.07
REMARK 500 15 ASP A 52 104.62 -47.39
REMARK 500 15 ASN A 60 66.19 62.57
REMARK 500 15 ARG A 74 -151.25 -90.31
REMARK 500 16 LYS A 33 -77.45 -78.76
REMARK 500 16 ARG A 74 -150.83 -90.23
REMARK 500 17 LYS A 33 -75.44 -75.11
REMARK 500
REMARK 500 THIS ENTRY HAS 103 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UBQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UBIQUITIN
REMARK 900 RELATED ID: 1D3Z RELATED DB: PDB
REMARK 900 STRUCTURE OF UBIQUITIN IN AQUEOUS BUFFER
DBREF 1G6J A 1 76 UNP P62988 UBIQ_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 GLU A 34 1 13
HELIX 2 2 LEU A 56 ASN A 60 5 5
SHEET 1 A 5 THR A 12 GLU A 16 0
SHEET 2 A 5 GLN A 2 LYS A 6 -1 O ILE A 3 N LEU A 15
SHEET 3 A 5 SER A 65 VAL A 70 1 O SER A 65 N PHE A 4
SHEET 4 A 5 ARG A 42 PHE A 45 -1 O ARG A 42 N VAL A 70
SHEET 5 A 5 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
Complete list - b 23 2 Bytes