Header list of 1irf.pdb file
Complete list - 29 20 Bytes
HEADER TRANSCRIPTION REGULATION 24-NOV-97 1IRF
TITLE INTERFERON REGULATORY FACTOR-2 DNA BINDING DOMAIN, NMR, MINIMIZED
TITLE 2 AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON REGULATORY FACTOR-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-113;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 CELLULAR_LOCATION: NUCLEUS;
SOURCE 7 GENE: POTENTIAL;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 LAMBDA DE3;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS TRANSCRIPTION REGULATION, WINGED HELIX-TURN-HELIX
EXPDTA SOLUTION NMR
AUTHOR J.FURUI,K.UEGAKI,T.YAMAZAKI,M.SHIRAKAWA,M.B.SWINDELLS,H.HARADA,
AUTHOR 2 T.TANIGUCHI,Y.KYOGOKU
REVDAT 4 29-NOV-17 1IRF 1 REMARK HELIX
REVDAT 3 24-FEB-09 1IRF 1 VERSN
REVDAT 2 05-APR-00 1IRF 1 JRNL
REVDAT 1 28-JAN-98 1IRF 0
JRNL AUTH J.FURUI,K.UEGAKI,T.YAMAZAKI,M.SHIRAKAWA,M.B.SWINDELLS,
JRNL AUTH 2 H.HARADA,T.TANIGUCHI,Y.KYOGOKU
JRNL TITL SOLUTION STRUCTURE OF THE IRF-2 DNA-BINDING DOMAIN: A NOVEL
JRNL TITL 2 SUBGROUP OF THE WINGED HELIX-TURN-HELIX FAMILY.
JRNL REF STRUCTURE V. 6 491 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9562558
JRNL DOI 10.1016/S0969-2126(98)00050-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.UEGAKI,M.SHIRAKAWA,H.HARADA,T.TANIGUCHI,Y.KYOGOKU
REMARK 1 TITL SECONDARY STRUCTURE AND FOLDING TOPOLOGY OF THE DNA BINDING
REMARK 1 TITL 2 DOMAIN OF INTERFERON REGULATORY FACTOR 2, AS REVEALED BY NMR
REMARK 1 TITL 3 SPECTROSCOPY
REMARK 1 REF FEBS LETT. V. 359 184 1995
REMARK 1 REFN ISSN 0014-5793
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: ENERGY INCLUDING L-J POTENTIAL,
REMARK 3 ELECTROSTATIC POTENTIAL AND EXPERIMENTAL RESTRAINTS WAS
REMARK 3 MINIMIZED FROM AVERAGE STRUCTURE.
REMARK 4
REMARK 4 1IRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174238.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 5.70
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED 3D NOESY; 13C -EDITED
REMARK 210 3D NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500; ARX500; ALPHA600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
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 : THE AVERAGE STRUCTURE OF 20
REMARK 210 STRUCTURES WITH THE LOWEST
REMARK 210 TARGET FUNCTIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 OG1 THR A 62 HZ3 LYS A 64 1.36
REMARK 500 OD1 ASN A 28 HZ2 LYS A 31 1.37
REMARK 500 HH21 ARG A 97 OG SER A 98 1.37
REMARK 500 HZ1 LYS A 64 OD1 ASN A 80 1.37
REMARK 500 O ALA A 41 HH21 ARG A 43 1.38
REMARK 500 OD1 ASP A 73 HZ2 LYS A 75 1.38
REMARK 500 HZ2 LYS A 25 OE1 GLN A 35 1.38
REMARK 500 O ARG A 43 HZ1 LYS A 78 1.39
REMARK 500 OD2 ASP A 96 HZ3 LYS A 100 1.39
REMARK 500 OD1 ASP A 70 HZ1 LYS A 71 1.40
REMARK 500 O VAL A 3 HH22 ARG A 5 1.41
REMARK 500 OE1 GLU A 49 HZ3 LYS A 50 1.42
REMARK 500 OD2 ASP A 47 HZ2 LYS A 50 1.43
REMARK 500 HZ3 LYS A 95 O ASP A 96 1.44
REMARK 500 O ARG A 5 HH11 ARG A 7 1.46
REMARK 500 HH21 ARG A 82 OD1 ASN A 86 1.46
REMARK 500 O TRP A 58 HG1 THR A 62 1.47
REMARK 500 OE2 GLU A 30 HZ1 LYS A 31 1.47
REMARK 500 O ILE A 99 HZ2 LYS A 101 1.47
REMARK 500 HH12 ARG A 9 OXT PRO A 113 1.51
REMARK 500 OE2 GLU A 14 HG SER A 18 1.52
REMARK 500 H2 PRO A 2 OE1 GLU A 4 1.52
REMARK 500 OE2 GLU A 13 HZ3 LYS A 29 1.52
REMARK 500 O ASP A 47 HZ1 LYS A 50 1.53
REMARK 500 O GLY A 23 HZ1 LYS A 25 1.53
REMARK 500 OE1 GLU A 92 HH11 ARG A 110 1.54
REMARK 500 OD2 ASP A 73 HG1 THR A 76 1.55
REMARK 500 O ASN A 57 H HIS A 61 1.57
REMARK 500 O LEU A 88 H ASP A 90 1.59
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 VAL A 3 68.68 -107.19
REMARK 500 ARG A 7 125.74 80.67
REMARK 500 ASN A 19 60.18 63.78
REMARK 500 PRO A 22 78.94 -68.30
REMARK 500 TRP A 38 179.07 71.70
REMARK 500 MET A 39 46.06 -101.33
REMARK 500 HIS A 44 -80.01 -128.09
REMARK 500 TRP A 46 -89.86 -149.77
REMARK 500 ILE A 69 -50.18 -121.01
REMARK 500 SER A 87 -158.27 -114.97
REMARK 500 LEU A 88 93.57 34.35
REMARK 500 PRO A 89 44.76 -66.68
REMARK 500 ASP A 90 12.60 -148.08
REMARK 500 ASP A 96 174.56 68.94
REMARK 500 ARG A 97 -52.93 -137.99
REMARK 500 SER A 98 33.71 -143.13
REMARK 500 ILE A 99 -77.06 -132.46
REMARK 500 ASN A 103 -57.65 -173.09
REMARK 500 ASN A 104 -52.21 -145.71
REMARK 500 ALA A 105 63.81 63.61
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 5 0.30 SIDE CHAIN
REMARK 500 ARG A 7 0.31 SIDE CHAIN
REMARK 500 ARG A 9 0.30 SIDE CHAIN
REMARK 500 ARG A 43 0.27 SIDE CHAIN
REMARK 500 ARG A 56 0.30 SIDE CHAIN
REMARK 500 ARG A 82 0.28 SIDE CHAIN
REMARK 500 ARG A 97 0.27 SIDE CHAIN
REMARK 500 ARG A 107 0.09 SIDE CHAIN
REMARK 500 ARG A 110 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IRG RELATED DB: PDB
DBREF 1IRF A 2 113 UNP P23906 IRF2_MOUSE 2 113
SEQRES 1 A 112 PRO VAL GLU ARG MET ARG MET ARG PRO TRP LEU GLU GLU
SEQRES 2 A 112 GLN ILE ASN SER ASN THR ILE PRO GLY LEU LYS TRP LEU
SEQRES 3 A 112 ASN LYS GLU LYS LYS ILE PHE GLN ILE PRO TRP MET HIS
SEQRES 4 A 112 ALA ALA ARG HIS GLY TRP ASP VAL GLU LYS ASP ALA PRO
SEQRES 5 A 112 LEU PHE ARG ASN TRP ALA ILE HIS THR GLY LYS HIS GLN
SEQRES 6 A 112 PRO GLY ILE ASP LYS PRO ASP PRO LYS THR TRP LYS ALA
SEQRES 7 A 112 ASN PHE ARG CYS ALA MET ASN SER LEU PRO ASP ILE GLU
SEQRES 8 A 112 GLU VAL LYS ASP ARG SER ILE LYS LYS GLY ASN ASN ALA
SEQRES 9 A 112 PHE ARG VAL TYR ARG MET LEU PRO
HELIX 1 H1 MET A 8 SER A 18 1 11
HELIX 2 H2 ALA A 52 HIS A 61 1 10
HELIX 3 H3 PRO A 74 MET A 85 1 12
SHEET 1 A 4 ILE A 91 VAL A 94 0
SHEET 2 A 4 ARG A 107 MET A 111 -1 N ARG A 110 O GLU A 92
SHEET 3 A 4 ILE A 33 ILE A 36 -1 N ILE A 36 O ARG A 107
SHEET 4 A 4 LYS A 25 ASN A 28 -1 N ASN A 28 O ILE A 33
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 - 29 20 Bytes