Header list of 1h6q.pdb file
Complete list - 17 20 Bytes
HEADER TUMOR-ASSOCIATED PROTEIN 20-JUN-01 1H6Q
TITLE TRANSLATIONALLY CONTROLLED TUMOR-ASSOCIATED PROTEIN P23FYP FROM
TITLE 2 SCHIZOSACCHAROMYCES POMBE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSLATIONALLY CONTROLLED TUMOR PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TCTP, P23FYP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SCHIZOSACCHAROMYCES POMBE;
SOURCE 3 ORGANISM_COMMON: FISSION YEAST;
SOURCE 4 ORGANISM_TAXID: 4896;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS TUMOR-ASSOCIATED PROTEIN, FUNCTION UNKNOWN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR P.THAW,N.J.BAXTER,S.E.SEDELNIKOVA,C.PRICE,J.P.WALTHO,C.J.CRAVEN
REVDAT 3 17-JAN-18 1H6Q 1 JRNL
REVDAT 2 24-FEB-09 1H6Q 1 VERSN
REVDAT 1 09-AUG-01 1H6Q 0
JRNL AUTH P.THAW,N.J.BAXTER,A.M.HOUNSLOW,C.PRICE,J.P.WALTHO,C.J.CRAVEN
JRNL TITL STRUCTURE OF TCTP REVEALS UNEXPECTED RELATIONSHIP WITH
JRNL TITL 2 GUANINE NUCLEOTIDE-FREE CHAPERONES.
JRNL REF NAT. STRUCT. BIOL. V. 8 701 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11473261
JRNL DOI 10.1038/90415
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STANDARD SIMULATED ANNEALING PROTOCOL
REMARK 4
REMARK 4 1H6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1290008081.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.1
REMARK 210 IONIC STRENGTH : 250MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: CLOSEST STRUCTURE TO THE MEAN. THE STRUCTURE WAS
REMARK 210 DETERMINED USING TRIPLE-RESONANCE NMR 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 SER A 9 43.12 164.56
REMARK 500 ASP A 11 99.66 57.10
REMARK 500 GLU A 12 81.75 44.73
REMARK 500 ASP A 19 130.30 155.44
REMARK 500 ASP A 25 -106.98 -65.78
REMARK 500 ILE A 26 49.86 -162.98
REMARK 500 ASP A 42 -53.19 -144.88
REMARK 500 VAL A 43 81.08 43.77
REMARK 500 ASP A 44 -172.93 51.17
REMARK 500 ILE A 45 57.03 -93.81
REMARK 500 ALA A 47 49.55 169.18
REMARK 500 PRO A 49 -89.65 -78.49
REMARK 500 ALA A 54 -63.59 -109.80
REMARK 500 GLU A 55 -91.08 64.63
REMARK 500 GLU A 59 123.75 179.56
REMARK 500 ARG A 73 44.06 37.84
REMARK 500 SER A 102 -78.21 -105.08
REMARK 500 ASN A 124 54.53 -154.76
REMARK 500 ASP A 129 177.62 50.88
REMARK 500 ALA A 140 -156.87 -98.39
REMARK 500 ARG A 148 -171.71 -58.75
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 ARG A 73 0.27 SIDE CHAIN
REMARK 500 ARG A 98 0.29 SIDE CHAIN
REMARK 500 ARG A 106 0.09 SIDE CHAIN
REMARK 500 ARG A 148 0.19 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1H7Y RELATED DB: PDB
REMARK 900 TRANSLATIONALLY CONTROLLED TUMOR-ASSOCIATED PROTEIN P23FYP FROM
REMARK 900 SCHIZOSACCHAROMYCES POMBE
REMARK 900 RELATED ID: 4447 RELATED DB: BMRB
DBREF 1H6Q A 1 168 UNP Q10344 TCTP_SCHPO 1 168
SEQRES 1 A 168 MET LEU LEU TYR LYS ASP VAL ILE SER GLY ASP GLU LEU
SEQRES 2 A 168 VAL SER ASP ALA TYR ASP LEU LYS GLU VAL ASP ASP ILE
SEQRES 3 A 168 VAL TYR GLU ALA ASP CYS GLN MET VAL THR VAL LYS GLN
SEQRES 4 A 168 GLY GLY ASP VAL ASP ILE GLY ALA ASN PRO SER ALA GLU
SEQRES 5 A 168 ASP ALA GLU GLU ASN ALA GLU GLU GLY THR GLU THR VAL
SEQRES 6 A 168 ASN ASN LEU VAL TYR SER PHE ARG LEU SER PRO THR SER
SEQRES 7 A 168 PHE ASP LYS LYS SER TYR MET SER TYR ILE LYS GLY TYR
SEQRES 8 A 168 MET LYS ALA ILE LYS ALA ARG LEU GLN GLU SER ASN PRO
SEQRES 9 A 168 GLU ARG VAL PRO VAL PHE GLU LYS ASN ALA ILE GLY PHE
SEQRES 10 A 168 VAL LYS LYS ILE LEU ALA ASN PHE LYS ASP TYR ASP PHE
SEQRES 11 A 168 TYR ILE GLY GLU SER MET ASP PRO ASP ALA MET VAL VAL
SEQRES 12 A 168 LEU MET ASN TYR ARG GLU ASP GLY ILE THR PRO TYR MET
SEQRES 13 A 168 ILE PHE PHE LYS ASP GLY LEU VAL SER GLU LYS PHE
HELIX 1 H1 ASN A 67 PHE A 72 1 6
HELIX 2 H2 LYS A 81 SER A 102 1 22
HELIX 3 H3 ARG A 106 TYR A 128 1 23
SHEET 1 A 4 LEU A 20 VAL A 23 0
SHEET 2 A 4 VAL A 27 ASP A 31 -1 O VAL A 27 N VAL A 23
SHEET 3 A 4 PRO A 154 PHE A 159 -1 O MET A 156 N ALA A 30
SHEET 4 A 4 MET A 145 TYR A 147 -1 O ASN A 146 N TYR A 155
SHEET 1 B 3 VAL A 14 SER A 15 0
SHEET 2 B 3 LEU A 2 LYS A 5 -1 O TYR A 4 N VAL A 14
SHEET 3 B 3 VAL A 164 LYS A 167 -1 O VAL A 164 N LYS A 5
SHEET 1 C 2 GLN A 33 LYS A 38 0
SHEET 2 C 2 GLU A 63 ASN A 66 -1 O GLU A 63 N VAL A 37
SHEET 1 D 2 SER A 75 THR A 77 0
SHEET 2 D 2 PHE A 130 ILE A 132 -1 O PHE A 130 N THR A 77
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
Complete list - 17 20 Bytes