Header list of 1t0y.pdb file
Complete list - r 2 2 Bytes
HEADER CHAPERONE 13-APR-04 1T0Y
TITLE SOLUTION STRUCTURE OF A UBIQUITIN-LIKE DOMAIN FROM TUBULIN-BINDING
TITLE 2 COFACTOR B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN FOLDING COFACTOR B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL UBIQUITIN-LIKE DOMAIN;
COMPND 5 SYNONYM: TUBULIN-SPECIFIC CHAPERONE B, CYTOSKELETON-ASSOCIATED
COMPND 6 PROTEIN 1, CKAP1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAENORHABDITIS ELEGANS;
SOURCE 3 ORGANISM_TAXID: 6239;
SOURCE 4 GENE: 5O73 OR F53F4.3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SG13009[PREP4];
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30T
KEYWDS UBIQUITIN-LIKE, CYTOSKELETON, MICROTUBULE, TUBULIN, CESG, STRUCTURAL
KEYWDS 2 GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, CENTER FOR EUKARYOTIC
KEYWDS 3 STRUCTURAL GENOMICS, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.L.LYTLE,F.C.PETERSON,S.H.QUI,M.LUO,B.F.VOLKMAN,J.L.MARKLEY,CENTER
AUTHOR 2 FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 7 02-MAR-22 1T0Y 1 REMARK SEQADV
REVDAT 6 24-FEB-09 1T0Y 1 VERSN
REVDAT 5 12-FEB-08 1T0Y 1 REMARK
REVDAT 4 01-FEB-05 1T0Y 1 AUTHOR KEYWDS REMARK
REVDAT 3 23-NOV-04 1T0Y 1 JRNL
REVDAT 2 21-SEP-04 1T0Y 1 KEYWDS REMARK HEADER TITLE
REVDAT 1 27-APR-04 1T0Y 0
JRNL AUTH B.L.LYTLE,F.C.PETERSON,S.H.QIU,M.LUO,Q.ZHAO,J.L.MARKLEY,
JRNL AUTH 2 B.F.VOLKMAN
JRNL TITL SOLUTION STRUCTURE OF A UBIQUITIN-LIKE DOMAIN FROM
JRNL TITL 2 TUBULIN-BINDING COFACTOR B.
JRNL REF J.BIOL.CHEM. V. 279 46787 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15364906
JRNL DOI 10.1074/JBC.M409422200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CYANA 1.0.6, XPLOR-NIH 2.0.6
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), HERRMANN, GUENTERT,
REMARK 3 WUETHRICH (CYANA), SCHWIETERS, KUSZEWSKI, TJANDRA,
REMARK 3 CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE C-TERMINAL RESIDUES 91-120 WERE
REMARK 3 DISORDERED (AS EVIDENCED BY 15N RELAXATION DATA) AND WERE
REMARK 3 EXCLUDED FROM THE MODEL. INITIAL STRUCTURES WERE GENERATED USING
REMARK 3 THE CANDID MODULE OF CYANA. ADDITIONAL NOE ASSIGNMENTS WERE
REMARK 3 DETERMINED MANUALLY. PHI AND PSI TORSION ANGLE CONSTRAINTS WERE
REMARK 3 GENERATED FROM CHEMICAL SHIFT DATABASE SEARCHING USING THE
REMARK 3 PROGRAM TALOS (G. CORNILESCU).
REMARK 4
REMARK 4 1T0Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022175.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50 MM NACL + 20 MM NAPO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM COFACTOR B UBIQUITIN-LIKE
REMARK 210 DOMAIN U-15N, 13C; 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER; 50 MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, XEASY 1.4, SPSCAN
REMARK 210 1.1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY CARTESIAN MOLECULAR DYNAMICS
REMARK 210 IN EXPLICIT SOLVENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: CHEMICAL SHIFT ASSIGNMENTS WERE OBTAINED FROM STANDARD 3D
REMARK 210 TRIPLE-RESONANCE EXPERIMENTS, USING THE AUTOMATED METHOD OF
REMARK 210 GARANT (C. BARTELS)
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 PHE A 91
REMARK 465 LYS A 92
REMARK 465 ASP A 93
REMARK 465 GLU A 94
REMARK 465 SER A 95
REMARK 465 MET A 96
REMARK 465 VAL A 97
REMARK 465 GLU A 98
REMARK 465 LYS A 99
REMARK 465 TYR A 100
REMARK 465 GLU A 101
REMARK 465 MET A 102
REMARK 465 SER A 103
REMARK 465 ASP A 104
REMARK 465 ASP A 105
REMARK 465 THR A 106
REMARK 465 TYR A 107
REMARK 465 GLY A 108
REMARK 465 LYS A 109
REMARK 465 ARG A 110
REMARK 465 THR A 111
REMARK 465 ASP A 112
REMARK 465 SER A 113
REMARK 465 VAL A 114
REMARK 465 ARG A 115
REMARK 465 ALA A 116
REMARK 465 TRP A 117
REMARK 465 LYS A 118
REMARK 465 LYS A 119
REMARK 465 LYS A 120
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 ASP A 55 -52.39 174.78
REMARK 500 1 LEU A 61 -94.04 -78.94
REMARK 500 1 THR A 62 -3.68 79.46
REMARK 500 1 ARG A 74 175.70 63.22
REMARK 500 2 ASP A 52 -175.63 -67.80
REMARK 500 2 ASP A 54 -65.06 -147.10
REMARK 500 2 ASP A 55 -47.16 170.56
REMARK 500 2 LEU A 61 -125.64 -92.03
REMARK 500 2 THR A 62 6.80 82.09
REMARK 500 2 ASP A 63 -72.00 -60.74
REMARK 500 3 ASP A 55 -35.06 175.51
REMARK 500 3 LEU A 61 -148.23 -87.61
REMARK 500 3 THR A 62 -2.38 104.26
REMARK 500 4 ASP A 55 -46.32 -174.89
REMARK 500 4 LEU A 61 -95.96 -104.61
REMARK 500 4 THR A 62 -2.93 79.69
REMARK 500 5 ASP A 55 -64.17 73.19
REMARK 500 5 LEU A 61 -151.46 -81.95
REMARK 500 5 THR A 62 -2.71 95.87
REMARK 500 6 ASP A 54 -72.50 -87.07
REMARK 500 6 ASP A 55 -32.58 -178.44
REMARK 500 6 LEU A 61 -86.00 -72.19
REMARK 500 6 THR A 62 -3.53 80.59
REMARK 500 6 GLU A 89 71.92 66.09
REMARK 500 7 ASP A 54 -46.40 69.78
REMARK 500 7 ASP A 55 -30.54 -164.76
REMARK 500 7 THR A 62 -3.77 79.69
REMARK 500 8 LEU A 61 -97.13 -110.65
REMARK 500 8 THR A 62 -1.03 80.32
REMARK 500 8 GLU A 89 92.32 63.90
REMARK 500 9 ASP A 55 -39.74 174.88
REMARK 500 9 LEU A 61 -94.91 38.43
REMARK 500 9 THR A 62 -3.58 82.16
REMARK 500 9 ASP A 63 -162.79 176.00
REMARK 500 9 GLU A 89 -34.74 60.45
REMARK 500 10 ASP A 54 -67.26 72.11
REMARK 500 10 LEU A 61 -95.02 -72.74
REMARK 500 10 THR A 62 -3.12 79.12
REMARK 500 10 ASP A 63 -72.67 -64.76
REMARK 500 10 GLU A 89 69.44 71.33
REMARK 500 11 GLU A 3 67.12 -100.54
REMARK 500 11 ASP A 54 86.63 -165.69
REMARK 500 11 ASP A 55 17.94 -167.96
REMARK 500 11 GLN A 56 -165.08 60.19
REMARK 500 11 LEU A 61 -101.18 -94.43
REMARK 500 11 ASP A 63 -76.62 -54.42
REMARK 500 11 GLU A 89 85.20 52.49
REMARK 500 12 THR A 42 -167.04 -100.65
REMARK 500 12 ASP A 52 -151.84 -81.69
REMARK 500 12 LEU A 61 -155.08 -118.49
REMARK 500
REMARK 500 THIS ENTRY HAS 91 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LPL RELATED DB: PDB
REMARK 900 CAP-GLY DOMAIN OF F53F4.3
REMARK 900 RELATED ID: GO.33910 RELATED DB: TARGETDB
DBREF 1T0Y A 1 120 UNP Q20728 YXHK_CAEEL 1 120
SEQADV 1T0Y GLY A -1 UNP Q20728 CLONING ARTIFACT
SEQADV 1T0Y SER A 0 UNP Q20728 CLONING ARTIFACT
SEQRES 1 A 122 GLY SER MET THR GLU VAL TYR ASP LEU GLU ILE THR THR
SEQRES 2 A 122 ASN ALA THR ASP PHE PRO MET GLU LYS LYS TYR PRO ALA
SEQRES 3 A 122 GLY MET SER LEU ASN ASP LEU LYS LYS LYS LEU GLU LEU
SEQRES 4 A 122 VAL VAL GLY THR THR VAL ASP SER MET ARG ILE GLN LEU
SEQRES 5 A 122 PHE ASP GLY ASP ASP GLN LEU LYS GLY GLU LEU THR ASP
SEQRES 6 A 122 GLY ALA LYS SER LEU LYS ASP LEU GLY VAL ARG ASP GLY
SEQRES 7 A 122 TYR ARG ILE HIS ALA VAL ASP VAL THR GLY GLY ASN GLU
SEQRES 8 A 122 ASP PHE LYS ASP GLU SER MET VAL GLU LYS TYR GLU MET
SEQRES 9 A 122 SER ASP ASP THR TYR GLY LYS ARG THR ASP SER VAL ARG
SEQRES 10 A 122 ALA TRP LYS LYS LYS
HELIX 1 1 SER A 27 GLY A 40 1 14
SHEET 1 A 5 MET A 18 PRO A 23 0
SHEET 2 A 5 VAL A 4 THR A 11 -1 N ILE A 9 O MET A 18
SHEET 3 A 5 TYR A 77 ASP A 83 1 O ALA A 81 N THR A 10
SHEET 4 A 5 MET A 46 PHE A 51 -1 N PHE A 51 O ARG A 78
SHEET 5 A 5 LEU A 57 GLU A 60 -1 O GLY A 59 N LEU A 50
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 - r 2 2 Bytes