Header list of 2bug.pdb file
Complete list - n 15 2 Bytes
HEADER HYDROLASE 13-JUN-05 2BUG
TITLE SOLUTION STRUCTURE OF THE TPR DOMAIN FROM PROTEIN PHOSPHATASE 5 IN
TITLE 2 COMPLEX WITH HSP90 DERIVED PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE PROTEIN PHOSPHATASE 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TETRATRICOPEPTIDE DOMAIN, RESIDUES 19-147;
COMPND 5 SYNONYM: PROTEIN PHOSPHATASE 5, PP5, PPT;
COMPND 6 EC: 3.1.3.16;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 OTHER_DETAILS: RESIDUES 19-147 WITH N-TERMINAL HIS-TAG;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: HSP90;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: C-TERMINAL PENTAPEPTIDE, RESIDUES 1-5;
COMPND 14 SYNONYM: DSCR1;
COMPND 15 ENGINEERED: YES;
COMPND 16 OTHER_DETAILS: N-TERMINALLY ACETYLATED
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE31;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS TETRATRICOPEPTIDE DOMAIN, PROTEIN PHOSPHATASE, HSP90 BINDING,
KEYWDS 2 HYDROLASE, IRON, MANGANESE, METAL-BINDING
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR M.J.CLIFF,R.HARRIS,D.BARFORD,J.E.LADBURY,M.A.WILLIAMS
REVDAT 3 15-JAN-20 2BUG 1 LINK
REVDAT 2 24-FEB-09 2BUG 1 VERSN
REVDAT 1 16-MAR-06 2BUG 0
JRNL AUTH M.J.CLIFF,R.HARRIS,D.BARFORD,J.E.LADBURY,M.A.WILLIAMS
JRNL TITL CONFORMATIONAL DIVERSITY IN THE TPR DOMAIN-MEDIATED
JRNL TITL 2 INTERACTION OF PROTEIN PHOSPHATASE 5 WITH HSP90.
JRNL REF STRUCTURE V. 14 415 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16531226
JRNL DOI 10.1016/J.STR.2005.12.009
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 JOURNAL CITATION ABOVE
REMARK 4
REMARK 4 2BUG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1290024024.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.0; 298.0; 298.0; 298.0
REMARK 210 PH : 6.0; 6.0; 6.0; 6.0
REMARK 210 IONIC STRENGTH : 55; 55; 55; 55
REMARK 210 PRESSURE : 1.0 ATM; 1.0 ATM; 1.0 ATM; 1.0
REMARK 210 ATM
REMARK 210 SAMPLE CONTENTS : 50MM MES, 5MM DTT (PH6.0)
REMARK 210 10%D2O, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCO; CBCACONH; 1H15N-
REMARK 210 TOWNY-HSQC; HNHB; 1H15N-
REMARK 210 NOESYHSQC; 1H13CNOESYHSQC; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA 1.2
REMARK 210 METHOD USED : ARIA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST RESTRAINT ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING DISTANCE RESTRAINTS
REMARK 210 DETERMINED FROM 1H13C-NOESYHSQC (13C,15N- LABELLED PROTEIN) AND
REMARK 210 1H15N-NOESYHSQC EXPERIMENTS (15N- LABELLED PROTEIN), AND ALSO
REMARK 210 HYDROGEN BOND RESTRAINTS FROM HYDROGEN EXCHANGE DATE, ANGLE
REMARK 210 RESTRAINTS DERIVED FROM CHEMICAL SHIFT DATA BY TALOS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLY 83 TO ASN
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 1-19
REMARK 465 RES C SSSEQI
REMARK 465 MET A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
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 HZ1 LYS A 135 OE2 GLU A 138 1.58
REMARK 500 HZ3 LYS A 40 OE2 GLU B 2 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 14 TYR A 80 CE1 TYR A 80 CZ 0.104
REMARK 500 14 TYR A 80 CZ TYR A 80 CE2 -0.106
REMARK 500 15 TYR A 99 CE1 TYR A 99 CZ 0.109
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 22 -101.39 -38.51
REMARK 500 1 PRO A 59 -64.60 -107.81
REMARK 500 1 CYS A 77 36.62 -89.64
REMARK 500 2 ASP A 22 -101.10 -39.10
REMARK 500 2 PRO A 59 -79.28 -107.86
REMARK 500 2 THR A 75 -84.64 -83.37
REMARK 500 2 GLU A 76 22.85 -175.73
REMARK 500 3 ASP A 22 30.07 -79.83
REMARK 500 3 PRO A 59 -79.80 -108.97
REMARK 500 3 THR A 75 33.60 -88.99
REMARK 500 3 GLU B 2 -153.15 -84.22
REMARK 500 3 GLU B 3 156.21 75.20
REMARK 500 4 ASP A 18 -178.26 -65.32
REMARK 500 4 ASP A 22 -101.61 -38.91
REMARK 500 4 PRO A 59 -82.22 -108.27
REMARK 500 4 SER A 60 45.65 -83.72
REMARK 500 4 THR A 75 -83.98 -77.02
REMARK 500 4 GLU A 76 17.99 -174.64
REMARK 500 5 ASP A 18 -178.69 -64.26
REMARK 500 5 ASP A 22 -100.87 -39.05
REMARK 500 5 PRO A 59 -74.97 -108.39
REMARK 500 5 THR A 75 -83.40 -76.41
REMARK 500 5 GLU A 76 21.73 -177.11
REMARK 500 6 ASP A 22 -100.16 -39.64
REMARK 500 6 PRO A 59 -71.25 -106.21
REMARK 500 6 CYS A 77 35.43 -95.77
REMARK 500 7 ASP A 18 -178.45 -68.31
REMARK 500 7 ASP A 22 -100.89 -39.56
REMARK 500 7 LEU A 57 -60.45 -96.41
REMARK 500 7 PRO A 59 -87.65 -109.11
REMARK 500 7 CYS A 77 36.44 -98.64
REMARK 500 8 ASP A 22 30.32 -80.35
REMARK 500 8 PRO A 59 -85.06 -108.57
REMARK 500 8 THR A 75 -84.91 -76.41
REMARK 500 8 GLU A 76 23.24 -175.25
REMARK 500 8 VAL B 4 -85.18 41.72
REMARK 500 9 ASP A 22 -99.15 -39.45
REMARK 500 9 PRO A 59 -83.43 -109.02
REMARK 500 9 CYS A 77 36.02 -94.15
REMARK 500 9 GLU B 2 66.16 -158.46
REMARK 500 9 VAL B 4 70.18 43.05
REMARK 500 10 ASP A 22 29.68 -78.96
REMARK 500 10 LYS A 42 9.14 80.76
REMARK 500 10 PRO A 59 -78.56 -108.90
REMARK 500 10 THR A 75 -83.13 -76.37
REMARK 500 10 GLU A 76 29.32 -179.22
REMARK 500 10 GLU B 2 -81.55 -165.66
REMARK 500 10 GLU B 3 -33.92 -178.89
REMARK 500 10 VAL B 4 -86.99 26.57
REMARK 500 11 ASP A 22 -100.65 -39.11
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 15 TYR A 99 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A17 RELATED DB: PDB
REMARK 900 TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5
REMARK 900 RELATED ID: 1S95 RELATED DB: PDB
REMARK 900 STRUCTURE OF SERINE/THREONINE PROTEIN PHOSPHATASE 5
REMARK 900 RELATED ID: 1WAO RELATED DB: PDB
REMARK 900 PP5 STRUCTURE
REMARK 900 RELATED ID: 6696 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 G83N MUTATION AND N-TERMINAL HIS TAG
DBREF 2BUG A 8 18 PDB 2BUG 2BUG 8 18
DBREF 2BUG A 19 147 UNP P53041 PPP5_HUMAN 19 147
DBREF 2BUG B 0 0 PDB 2BUG 2BUG 0 0
DBREF 2BUG B 1 5 UNP Q9H2A1 Q9H2A1_HUMAN 1 5
SEQADV 2BUG ASN A 83 UNP P53041 GLY 83 ENGINEERED MUTATION
SEQRES 1 A 140 MET SER GLY HIS HIS HIS HIS HIS HIS THR ASP PRO PRO
SEQRES 2 A 140 ALA ASP GLY ALA LEU LYS ARG ALA GLU GLU LEU LYS THR
SEQRES 3 A 140 GLN ALA ASN ASP TYR PHE LYS ALA LYS ASP TYR GLU ASN
SEQRES 4 A 140 ALA ILE LYS PHE TYR SER GLN ALA ILE GLU LEU ASN PRO
SEQRES 5 A 140 SER ASN ALA ILE TYR TYR GLY ASN ARG SER LEU ALA TYR
SEQRES 6 A 140 LEU ARG THR GLU CYS TYR GLY TYR ALA LEU ASN ASP ALA
SEQRES 7 A 140 THR ARG ALA ILE GLU LEU ASP LYS LYS TYR ILE LYS GLY
SEQRES 8 A 140 TYR TYR ARG ARG ALA ALA SER ASN MET ALA LEU GLY LYS
SEQRES 9 A 140 PHE ARG ALA ALA LEU ARG ASP TYR GLU THR VAL VAL LYS
SEQRES 10 A 140 VAL LYS PRO HIS ASP LYS ASP ALA LYS MET LYS TYR GLN
SEQRES 11 A 140 GLU CYS ASN LYS ILE VAL LYS GLN LYS ALA
SEQRES 1 B 6 ACE MET GLU GLU VAL ASP
HET ACE B 0 6
HETNAM ACE ACETYL GROUP
FORMUL 2 ACE C2 H4 O
HELIX 1 1 ALA A 21 ALA A 41 1 21
HELIX 2 2 ASP A 43 ASN A 58 1 16
HELIX 3 3 ASN A 61 THR A 75 1 15
HELIX 4 4 CYS A 77 ASP A 92 1 16
HELIX 5 5 TYR A 95 GLY A 110 1 16
HELIX 6 6 LYS A 111 LYS A 126 1 16
HELIX 7 7 ASP A 129 LYS A 146 1 18
LINK C ACE B 0 N MET B 1 1555 1555 1.34
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 - n 15 2 Bytes