HEADER TRANSCRIPTION 28-JUL-05 2AHQ
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL RPON DOMAIN OF SIGMA-54 FROM
TITLE 2 AQUIFEX AEOLICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA POLYMERASE SIGMA FACTOR RPON;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: SIGMA-54;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: RPON;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA (BL21 (DE3) WITH PLYSS);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS SIGMA-54, SIGMA FACTORS, SOLUTION STRUCTURE, TRANSCRIPTION, RNA
KEYWDS 2 POLYMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.DOUCLEFF,L.T.MALAK,J.G.PELTON,D.E.WEMMER
REVDAT 4 09-MAR-22 2AHQ 1 REMARK
REVDAT 3 24-FEB-09 2AHQ 1 VERSN
REVDAT 2 02-MAY-06 2AHQ 1 JRNL
REVDAT 1 11-OCT-05 2AHQ 0
JRNL AUTH M.DOUCLEFF,L.T.MALAK,J.G.PELTON,D.E.WEMMER
JRNL TITL THE C-TERMINAL RPON DOMAIN OF SIGMA54 FORMS AN UNPREDICTED
JRNL TITL 2 HELIX-TURN-HELIX MOTIF SIMILAR TO DOMAINS OF SIGMA70.
JRNL REF J.BIOL.CHEM. V. 280 41530 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16210314
JRNL DOI 10.1074/JBC.M509010200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, DYANA 1.5
REMARK 3 AUTHORS : DELAGLIO ET AL. (1995) (NMRPIPE), GUNTERT ET AL.
REMARK 3 (1997) (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL 1064
REMARK 3 RESTRAINTS: 956 DISTANCE AND 108 DIHEDRAL ANGLE
REMARK 4
REMARK 4 2AHQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033908.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 50 MM HEPES; 250 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8 MM SIGMA-54 U-15N; 50 MM
REMARK 210 HEPES; 250 MM NACL; 1 MM EDTA;
REMARK 210 90% H20; 10% D20; 0.8 MM SIGMA-
REMARK 210 54 U-15N U-13C; 50 MM HEPES; 250
REMARK 210 MM NACL; 1 MM EDTA; 90% H20; 10%
REMARK 210 D20; 0.8 MM SIGMA-54 U-15; 50 MM
REMARK 210 HEPES; 250 MM NACL; 1 MM EDTA; 5%
REMARK 210 H20; 95% D20; 0.8 MM SIGMA-54 U-
REMARK 210 15N U-10% 13C; 50 MM HEPES; 250
REMARK 210 MM NACL; 1 MM EDTA; 90% H20; 10%
REMARK 210 D20
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_N15
REMARK 210 -SEPERATED_TOCSY; HNCA-J; HCCH-
REMARK 210 TOCSY; 3D_13C-SEPARATED_NOESY;
REMARK 210 2D_C13-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 OTHER EXPERIMENTS PERFORMED AND USED FOR CHEMICAL SHIFT
REMARK 210 ASSIGNMENTS AND OBTAINING RESTRAINTS:
REMARK 210 CBCA(CO)NH, DQF-COSY, CC(CO)NH, H/D EXCHANGE VIA N15-HSQC, HNHA -
REMARK 210 J COUPLINGS
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 ILE A 68
REMARK 465 PRO A 69
REMARK 465 SER A 70
REMARK 465 SER A 71
REMARK 465 ARG A 72
REMARK 465 GLU A 73
REMARK 465 ARG A 74
REMARK 465 ARG A 75
REMARK 465 ILE A 76
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 O VAL A 59 H ARG A 63 1.54
REMARK 500 O ILE A 46 H GLU A 49 1.58
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 TYR A 2 -43.08 -179.02
REMARK 500 1 ARG A 5 170.20 56.89
REMARK 500 1 PHE A 8 79.03 -175.16
REMARK 500 1 GLU A 11 96.21 -57.73
REMARK 500 1 SER A 12 155.04 59.28
REMARK 500 1 GLU A 14 49.04 -80.38
REMARK 500 1 LEU A 16 160.15 -40.73
REMARK 500 1 GLU A 32 -151.52 -62.20
REMARK 500 1 LYS A 36 63.81 -167.10
REMARK 500 1 GLU A 42 -70.65 -61.35
REMARK 500 1 VAL A 54 -150.41 -110.18
REMARK 500 1 ALA A 55 142.70 160.23
REMARK 500 1 LEU A 66 -67.67 -151.56
REMARK 500 2 TYR A 2 135.50 67.98
REMARK 500 2 LEU A 4 -165.62 -127.04
REMARK 500 2 VAL A 9 -103.63 -90.81
REMARK 500 2 ARG A 10 -58.00 -177.49
REMARK 500 2 GLU A 11 172.13 75.92
REMARK 500 2 SER A 12 150.88 63.20
REMARK 500 2 GLU A 14 71.64 -156.84
REMARK 500 2 LEU A 16 168.85 -44.79
REMARK 500 2 ASN A 31 52.29 -158.69
REMARK 500 2 GLU A 32 -156.95 -62.12
REMARK 500 2 PRO A 37 -160.12 -75.00
REMARK 500 2 TYR A 38 51.83 -153.29
REMARK 500 2 PHE A 52 -114.15 19.48
REMARK 500 2 LYS A 53 44.84 -160.81
REMARK 500 2 VAL A 54 -160.01 -108.80
REMARK 500 2 ALA A 55 146.80 161.03
REMARK 500 2 LEU A 66 -73.65 -81.98
REMARK 500 3 TYR A 2 -63.12 179.29
REMARK 500 3 PHE A 8 159.38 178.71
REMARK 500 3 VAL A 9 -107.07 -144.81
REMARK 500 3 ARG A 10 -71.29 -177.54
REMARK 500 3 GLU A 11 164.46 78.30
REMARK 500 3 SER A 12 -175.49 -54.38
REMARK 500 3 ALA A 13 161.48 -41.49
REMARK 500 3 GLU A 14 174.85 -57.89
REMARK 500 3 LEU A 16 153.97 -40.16
REMARK 500 3 GLU A 32 -157.73 -62.34
REMARK 500 3 LYS A 34 -76.54 -50.26
REMARK 500 3 PRO A 37 -160.44 -75.05
REMARK 500 3 TYR A 38 53.58 -153.41
REMARK 500 3 GLN A 41 -73.84 -65.24
REMARK 500 3 VAL A 54 -167.47 -116.56
REMARK 500 3 ALA A 55 148.37 174.15
REMARK 500 3 LEU A 66 -71.67 -83.07
REMARK 500 4 SER A 3 173.57 175.01
REMARK 500 4 PHE A 8 -177.35 -178.08
REMARK 500 4 VAL A 9 91.31 59.61
REMARK 500
REMARK 500 THIS ENTRY HAS 321 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2AHQ A 1 76 UNP O66858 O66858_AQUAE 323 398
SEQRES 1 A 76 THR TYR SER LEU ARG THR PHE PHE VAL ARG GLU SER ALA
SEQRES 2 A 76 GLU GLY LEU THR GLN GLY GLU LEU MET LYS LEU ILE LYS
SEQRES 3 A 76 GLU ILE VAL GLU ASN GLU ASP LYS ARG LYS PRO TYR SER
SEQRES 4 A 76 ASP GLN GLU ILE ALA ASN ILE LEU LYS GLU LYS GLY PHE
SEQRES 5 A 76 LYS VAL ALA ARG ARG THR VAL ALA LYS TYR ARG GLU MET
SEQRES 6 A 76 LEU GLY ILE PRO SER SER ARG GLU ARG ARG ILE
HELIX 1 1 THR A 17 VAL A 29 1 13
HELIX 2 2 GLU A 30 GLU A 32 5 3
HELIX 3 3 SER A 39 LYS A 48 1 10
HELIX 4 4 ALA A 55 LEU A 66 1 12
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
(ATOM LINES ARE NOT SHOWN.)
END
