Header list of 1sxe.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION, SIGNALING PROTEIN 30-MAR-04 1SXE
TITLE THE SOLUTION STRUCTURE OF THE POINTED (PNT) DOMAIN FROM THE
TITLE 2 TRANSCRITION FACTOR ERG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR ERG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PNT DOMAIN;
COMPND 5 SYNONYM: TRANSFORMING PROTEIN ERG;
COMPND 6 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: ERG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ALPHA HELICAL, TRANSCRIPTION, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR C.D.MACKERETH,M.SCHAERPF,L.N.GENTILE,S.E.MACINTOSH,C.M.SLUPSKY,
AUTHOR 2 L.P.MCINTOSH
REVDAT 3 02-MAR-22 1SXE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SXE 1 VERSN
REVDAT 1 21-SEP-04 1SXE 0
JRNL AUTH C.D.MACKERETH,M.SCHAERPF,L.N.GENTILE,S.E.MACINTOSH,
JRNL AUTH 2 C.M.SLUPSKY,L.P.MCINTOSH
JRNL TITL DIVERSITY IN STRUCTURE AND FUNCTION OF THE ETS FAMILY PNT
JRNL TITL 2 DOMAINS.
JRNL REF J.MOL.BIOL. V. 342 1249 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15351649
JRNL DOI 10.1016/J.JMB.2004.07.094
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, ARIA 1.2
REMARK 3 AUTHORS : ACCELRYS INC. (FELIX), J.LINGE, S.O'DONOGHUE,
REMARK 3 M.NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SXE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022065.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303
REMARK 210 PH : 7.0; 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : 70 MM; 70 MM; 70 MM; 70 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ERG U-15N,13C, 20MM
REMARK 210 PHOSPHATE BUFFER PH 7.0, 50MM
REMARK 210 NACL, 2MM DTT, 90% H2O, 10% D2O;
REMARK 210 1MM ERG 100%15N,10%13C, 20MM
REMARK 210 PHOSPHATE BUFFER PH 7.0, 50MM
REMARK 210 NACL, 2MM DTT, 90% H2O, 10% D2O;
REMARK 210 2MM ERG 100%15N, 20MM PHOSPHATE
REMARK 210 BUFFER PH 7.0, 50MM NACL, 2MM
REMARK 210 DTT, 90% H2O, 10% D2O; 2MM ERG
REMARK 210 100%15N, 20MM PHOSPHATE BUFFER
REMARK 210 PH 7.0, 50MM NACL, 2MM DTT, 1%
REMARK 210 H2O, 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1995, SPARKY 3, ARIA 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 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: 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 HG LEU A 143 HG21 ILE A 157 1.26
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 11 PHE A 176 CE1 PHE A 176 CZ 0.117
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 ASN A 117 -109.93 -88.49
REMARK 500 1 GLU A 122 -98.58 62.47
REMARK 500 1 ARG A 124 -152.58 -95.28
REMARK 500 1 ILE A 126 67.60 -64.81
REMARK 500 1 ALA A 129 21.38 -62.73
REMARK 500 1 PRO A 131 34.39 -64.85
REMARK 500 1 TRP A 145 -9.05 -57.11
REMARK 500 1 LEU A 158 7.93 -63.54
REMARK 500 1 MET A 171 131.08 -29.96
REMARK 500 1 THR A 180 89.43 -157.07
REMARK 500 1 SER A 182 -134.85 51.78
REMARK 500 2 SER A 106 80.99 61.52
REMARK 500 2 MET A 108 140.46 72.06
REMARK 500 2 LYS A 111 42.86 -91.24
REMARK 500 2 PRO A 116 100.03 -28.93
REMARK 500 2 GLU A 122 -92.27 -60.81
REMARK 500 2 ARG A 123 -40.29 -147.52
REMARK 500 2 ILE A 126 66.15 -69.08
REMARK 500 2 PRO A 131 26.89 -71.14
REMARK 500 2 TRP A 145 -9.19 -56.57
REMARK 500 2 LEU A 158 8.02 -58.38
REMARK 500 2 LEU A 179 -30.48 -130.23
REMARK 500 2 THR A 180 80.31 -153.55
REMARK 500 2 PRO A 181 -156.92 -90.58
REMARK 500 2 SER A 182 -91.49 68.77
REMARK 500 3 SER A 106 77.19 -100.42
REMARK 500 3 GLU A 110 34.34 -95.41
REMARK 500 3 MET A 113 74.15 -115.52
REMARK 500 3 THR A 119 18.49 -155.53
REMARK 500 3 THR A 120 -75.43 -88.50
REMARK 500 3 ASN A 121 47.32 -81.93
REMARK 500 3 ARG A 124 -64.04 -148.83
REMARK 500 3 PRO A 131 28.35 -75.82
REMARK 500 3 ASP A 154 76.64 -152.02
REMARK 500 3 LEU A 158 6.91 -64.42
REMARK 500 3 THR A 180 95.49 -162.06
REMARK 500 3 SER A 182 -178.37 61.58
REMARK 500 3 TYR A 183 -66.81 68.87
REMARK 500 4 MET A 108 -0.74 -154.23
REMARK 500 4 GLU A 109 -77.15 -77.72
REMARK 500 4 GLU A 110 -177.28 60.03
REMARK 500 4 LYS A 111 -14.07 74.75
REMARK 500 4 PRO A 116 103.90 -35.07
REMARK 500 4 ASN A 121 115.14 -179.39
REMARK 500 4 ARG A 123 -109.97 61.17
REMARK 500 4 ARG A 124 -85.42 -61.90
REMARK 500 4 VAL A 125 -37.65 -135.45
REMARK 500 4 ILE A 126 50.94 27.69
REMARK 500 4 PRO A 131 31.68 -73.64
REMARK 500 4 PRO A 153 46.59 -92.02
REMARK 500
REMARK 500 THIS ENTRY HAS 193 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 4 TYR A 150 0.05 SIDE CHAIN
REMARK 500 10 TYR A 150 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SXE A 108 201 UNP P11308 ERG_HUMAN 115 208
SEQADV 1SXE GLY A 105 UNP P11308 CLONING ARTIFACT
SEQADV 1SXE SER A 106 UNP P11308 CLONING ARTIFACT
SEQADV 1SXE HIS A 107 UNP P11308 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER HIS MET GLU GLU LYS HIS MET PRO PRO PRO ASN
SEQRES 2 A 97 MET THR THR ASN GLU ARG ARG VAL ILE VAL PRO ALA ASP
SEQRES 3 A 97 PRO THR LEU TRP SER THR ASP HIS VAL ARG GLN TRP LEU
SEQRES 4 A 97 GLU TRP ALA VAL LYS GLU TYR GLY LEU PRO ASP VAL ASN
SEQRES 5 A 97 ILE LEU LEU PHE GLN ASN ILE ASP GLY LYS GLU LEU CYS
SEQRES 6 A 97 LYS MET THR LYS ASP ASP PHE GLN ARG LEU THR PRO SER
SEQRES 7 A 97 TYR ASN ALA ASP ILE LEU LEU SER HIS LEU HIS TYR LEU
SEQRES 8 A 97 ARG GLU THR PRO LEU PRO
HELIX 1 1 MET A 108 MET A 113 5 6
HELIX 2 2 SER A 135 GLY A 151 1 17
HELIX 3 3 ASN A 156 PHE A 160 5 5
HELIX 4 4 ASP A 164 CYS A 169 1 6
HELIX 5 5 THR A 172 GLN A 177 1 6
HELIX 6 6 PRO A 181 ARG A 196 1 16
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