Header list of 1r36.pdb file
Complete list - t 27 2 Bytes
HEADER TRANSCRIPTION 30-SEP-03 1R36
TITLE NMR-BASED STRUCTURE OF AUTOINHIBITED MURINE ETS-1 DELTAN301
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: C-ETS-1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AUTOINHIBITION MODULE, RESIDUES 301-440;
COMPND 5 SYNONYM: ETS-1 DELTAN301; P54; E26 AVIAN LEUKEMIA ONCOGENE 1, 5'
COMPND 6 DOMAIN; ETS1 PROTEIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS TRANSCRIPTION FACTOR; AUTOINHIBITION MODULE; WINGED HELIX-TURN-HELIX;
KEYWDS 2 HELICAL BUNDLE, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR G.M.LEE,L.W.DONALDSON,M.A.PUFALL,H.-S.KANG,I.POT,B.J.GRAVES,
AUTHOR 2 L.P.MCINTOSH
REVDAT 5 27-OCT-21 1R36 1 SEQADV
REVDAT 4 05-FEB-20 1R36 1 REMARK ATOM
REVDAT 3 24-FEB-09 1R36 1 VERSN
REVDAT 2 01-MAR-05 1R36 1 JRNL
REVDAT 1 09-NOV-04 1R36 0
SPRSDE 09-NOV-04 1R36 1ETC 1ETD
JRNL AUTH G.M.LEE,L.W.DONALDSON,M.A.PUFALL,H.-S.KANG,I.POT,B.J.GRAVES,
JRNL AUTH 2 L.P.MCINTOSH
JRNL TITL THE STRUCTURAL AND DYNAMIC BASIS OF ETS-1 DNA BINDING
JRNL TITL 2 AUTOINHIBITION
JRNL REF J.BIOL.CHEM. V. 280 7088 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15591056
JRNL DOI 10.1074/JBC.M410722200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 2000, ARIA 1.2, CNS 1.1
REMARK 3 AUTHORS : ACCELRYS, INC. (FELIX), LINGE, J., ET AL. (ARIA),
REMARK 3 BRUNGER, A., ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3268 UNAMBIGUOUS AND 537 AMBIGUOUS NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS, 237 DIHEDRAL ANGLE RESTRAINTS, 80 HYDROGEN BOND
REMARK 3 RESTRAINTS, AND 49 RESIDUAL DIPOLAR COUPLING RESTRAINTS.
REMARK 4
REMARK 4 1R36 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020379.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 500MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3-0.8MM ETS-1 DN301, U-15N;
REMARK 210 20MM PHOSPHATE (PH 6.5), 500MM
REMARK 210 NACL, 5MM DTT, 0.02% NAN3; 0.3-
REMARK 210 0.8MM ETS-1 DN301, U-15N, U-13C;
REMARK 210 20MM PHOSPHATE (PH 6.5), 500MM
REMARK 210 NACL, 5MM DTT, 0.02% NAN3; 0.3-
REMARK 210 0.8MM ETS-1 DN301, U-15N, U-13C,
REMARK 210 U-2H; 20MM PHOSPHATE (PH 6.5),
REMARK 210 500MM NACL, 5MM DTT, 0.02% NAN3;
REMARK 210 0.3-0.8MM ETS-1 DN301, U-15N, U-
REMARK 210 10% 13C; 20MM PHOSPHATE (PH 6.5),
REMARK 210 500MM NACL, 5MM DTT, 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 3D_SIMULTANEOUS_ALIPHATIC_15N-13C-NOESY; 3D_15N-15N-1H-NOESY; 3D_
REMARK 210 SIMULTANEOUS_AROMATIC_15N-13C-NOESY; 3D_SIMULTANEOUS_METHYL_15N-
REMARK 210 13C-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6X
REMARK 210 METHOD USED : MOLECULAR DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 HB VAL A 320 HB THR A 346 1.20
REMARK 500 O LEU A 342 HG1 THR A 346 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 5 TYR A 412 CE1 TYR A 412 CZ 0.078
REMARK 500 5 TYR A 412 CZ TYR A 412 CE2 -0.081
REMARK 500 6 TYR A 412 CE1 TYR A 412 CZ 0.088
REMARK 500 6 TYR A 412 CZ TYR A 412 CE2 -0.087
REMARK 500 8 TYR A 412 CE1 TYR A 412 CZ 0.105
REMARK 500 8 TYR A 412 CZ TYR A 412 CE2 -0.097
REMARK 500 16 TYR A 412 CE1 TYR A 412 CZ 0.080
REMARK 500 16 TYR A 412 CZ TYR A 412 CE2 -0.080
REMARK 500 25 TYR A 412 CE1 TYR A 412 CZ 0.084
REMARK 500 25 TYR A 412 CZ TYR A 412 CE2 -0.085
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 ARG A 311 -83.61 -117.45
REMARK 500 1 ASP A 313 33.13 -145.60
REMARK 500 1 LEU A 314 -77.63 -69.35
REMARK 500 1 ASN A 315 -56.22 -139.10
REMARK 500 1 ASP A 317 83.60 -54.64
REMARK 500 1 LYS A 318 -55.98 -127.11
REMARK 500 1 ILE A 335 157.34 61.07
REMARK 500 1 ILE A 354 86.98 -165.00
REMARK 500 1 LYS A 383 38.64 -91.02
REMARK 500 1 LYS A 404 96.67 -64.21
REMARK 500 1 ASP A 417 97.68 59.36
REMARK 500 2 THR A 303 -160.64 -78.76
REMARK 500 2 ARG A 311 -74.41 -131.58
REMARK 500 2 ASP A 313 48.61 -156.30
REMARK 500 2 LEU A 314 -77.94 -71.69
REMARK 500 2 ASN A 315 -66.65 -141.30
REMARK 500 2 LYS A 316 36.48 -94.16
REMARK 500 2 ASP A 317 80.27 -60.94
REMARK 500 2 ILE A 335 131.86 63.79
REMARK 500 2 ILE A 354 88.19 -165.55
REMARK 500 2 ASP A 367 78.12 -115.16
REMARK 500 2 LYS A 404 95.95 -69.30
REMARK 500 3 THR A 303 -158.56 -84.14
REMARK 500 3 ARG A 311 -79.13 -118.75
REMARK 500 3 ASP A 313 56.19 -148.86
REMARK 500 3 LEU A 314 -74.04 -86.46
REMARK 500 3 ASN A 315 -62.99 -146.93
REMARK 500 3 ASP A 317 41.31 38.38
REMARK 500 3 ILE A 335 170.86 60.16
REMARK 500 3 ILE A 354 88.33 -166.25
REMARK 500 3 ASP A 367 79.47 -117.29
REMARK 500 3 LYS A 404 101.14 -59.18
REMARK 500 3 PRO A 437 11.51 -63.40
REMARK 500 4 THR A 303 -160.64 -77.73
REMARK 500 4 ARG A 311 -69.69 -121.25
REMARK 500 4 LEU A 314 -78.66 -95.46
REMARK 500 4 ASN A 315 -53.45 -144.08
REMARK 500 4 ASP A 317 26.85 45.64
REMARK 500 4 ILE A 335 -179.87 56.38
REMARK 500 4 ILE A 354 87.71 -165.45
REMARK 500 4 LYS A 383 33.67 -97.73
REMARK 500 4 TYR A 410 61.43 60.10
REMARK 500 4 PRO A 437 45.75 -73.72
REMARK 500 5 THR A 303 -159.25 -87.76
REMARK 500 5 ARG A 311 -79.06 -126.76
REMARK 500 5 ASP A 313 24.65 -145.70
REMARK 500 5 LEU A 314 -73.60 -58.94
REMARK 500 5 ASN A 315 -66.87 -143.69
REMARK 500 5 ASP A 317 -31.49 61.12
REMARK 500 5 ILE A 335 176.91 60.34
REMARK 500
REMARK 500 THIS ENTRY HAS 264 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 8 TYR A 412 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5991 RELATED DB: BMRB
REMARK 900 THE CHEMICAL SHIFTS FOR BACKBONE AND SIDECHAIN 1H, 15N, AND 13C
REMARK 900 ATOMS. ALSO INCLUDES THE BACKBONE 15N DYNAMICS PARAMETERS (T1, T2,
REMARK 900 1H{15N}NOE, S2).
DBREF 1R36 A 301 440 UNP P27577 ETS1_MOUSE 301 440
SEQADV 1R36 SER A 416 UNP P27577 CYS 416 ENGINEERED MUTATION
SEQRES 1 A 140 LYS GLY THR PHE LYS ASP TYR VAL ARG ASP ARG ALA ASP
SEQRES 2 A 140 LEU ASN LYS ASP LYS PRO VAL ILE PRO ALA ALA ALA LEU
SEQRES 3 A 140 ALA GLY TYR THR GLY SER GLY PRO ILE GLN LEU TRP GLN
SEQRES 4 A 140 PHE LEU LEU GLU LEU LEU THR ASP LYS SER CYS GLN SER
SEQRES 5 A 140 PHE ILE SER TRP THR GLY ASP GLY TRP GLU PHE LYS LEU
SEQRES 6 A 140 SER ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY LYS ARG
SEQRES 7 A 140 LYS ASN LYS PRO LYS MET ASN TYR GLU LYS LEU SER ARG
SEQRES 8 A 140 GLY LEU ARG TYR TYR TYR ASP LYS ASN ILE ILE HIS LYS
SEQRES 9 A 140 THR ALA GLY LYS ARG TYR VAL TYR ARG PHE VAL SER ASP
SEQRES 10 A 140 LEU GLN SER LEU LEU GLY TYR THR PRO GLU GLU LEU HIS
SEQRES 11 A 140 ALA MET LEU ASP VAL LYS PRO ASP ALA ASP
HELIX 1 1 PHE A 304 ASP A 310 1 7
HELIX 2 2 ALA A 323 THR A 330 1 8
HELIX 3 3 LEU A 337 THR A 346 1 10
HELIX 4 4 PRO A 368 ARG A 378 1 11
HELIX 5 5 TYR A 386 ASP A 398 1 13
HELIX 6 6 LEU A 418 LEU A 422 1 5
HELIX 7 7 PRO A 426 ALA A 431 1 6
SHEET 1 A 4 ILE A 354 TRP A 356 0
SHEET 2 A 4 GLU A 362 LEU A 365 -1 O LYS A 364 N SER A 355
SHEET 3 A 4 ILE A 402 THR A 405 -1 N HIS A 403 O ARG A 413
SHEET 4 A 4 VAL A 411 PHE A 414 -1 O TYR A 412 N PHE A 363
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 - t 27 2 Bytes