Header list of 1xsx.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 20-OCT-04 1XSX
TITLE NMR STRUCTURE OF SSO10A, A HYPERTHERMOPHILE DNA-BINDING PROTEIN WITH
TITLE 2 AN EXTENDED ANTI-PARALLEL COILED COIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SSO10A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 GENE: SSO10A;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTABLUE(DE3)PLACI (NOVAGEN);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETBLUE-2
KEYWDS WINGED HELIX-TURN-HELIX, ANTI-PARALLEL COILED COIL DIMER,
KEYWDS 2 HYPERTHERMOPHILE DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
MDLTYP MINIMIZED AVERAGE
AUTHOR M.A.KAHSAI,B.VOGLER,A.T.CLARK,S.P.EDMONDSON,J.W.SHRIVER
REVDAT 3 02-MAR-22 1XSX 1 REMARK
REVDAT 2 24-FEB-09 1XSX 1 VERSN
REVDAT 1 01-MAR-05 1XSX 0
JRNL AUTH M.A.KAHSAI,B.VOGLER,A.T.CLARK,S.P.EDMONDSON,J.W.SHRIVER
JRNL TITL SOLUTION STRUCTURE, STABILITY, AND FLEXIBILITY OF SSO10A: A
JRNL TITL 2 HYPERTHERMOPHILE COILED-COIL DNA-BINDING PROTEIN(,).
JRNL REF BIOCHEMISTRY V. 44 2822 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15723526
JRNL DOI 10.1021/BI047669T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, XPLOR-NIH 2.9.6
REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER, CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NOE ASSIGNMENTS, DISTANCE RESTRAINT CALIBRATIONS, AND INITIAL
REMARK 3 STRUCTURES WERE MADE USING ARIA 1.2. FINAL STRUCTURE REFINEMNET
REMARK 3 WAS DONE USING XPLOR-NIH. RESTRAINTS CONSISTED OF 1231
REMARK 3 INTRASUBUNIT AND 83 INTERSUBUNIT NOE-DERIVED DISTANCES, 144
REMARK 3 TORSION ANGLES, 60 HNHA COUPLING CONSTANTS, 41 H-BONDS, 52 DIPOLAR
REMARK 3 COUPLINGS, 54 T1/T2 RELAXATION RATIOS, AND NON-CRYSTALLOGRAPHIC
REMARK 3 DIMER SYMMETRY RESTRAINTS. (NUMBERS OF RESTRAINTS ARE PER MONOMER.)
REMARK 3
REMARK 3 ANISOTROPY TENSORS WERE INCLUDED AS VARIABLES DURING REFINEMNET,
REMARK 3 WITH BEST FIT VALUES FOR THE MOLECULAR ALIGNMENT TENSOR (FROM RDC'
REMARK 3 S) OF DA=16 HZ AND RHOMBICITY=0.24, AND BEST FIT VALUES FOR THE
REMARK 3 DIFFUSION ANISOTROPY TENSOR (FROM 15N RELAXATION) OF DPAR/DPERP=
REMARK 3 2.0 AND RHOMBICITY=0.05 (AND TAUC=13.7 NS).
REMARK 4
REMARK 4 1XSX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-04.
REMARK 100 THE DEPOSITION ID IS D_1000030730.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 308
REMARK 210 PH : 5.0; 5.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 25 MG/ML 15N,13C SSO10A, 90%
REMARK 210 H2O, 10% D2O; 25 MG/ML 15N,13C
REMARK 210 SSO10A, 100% D2O; 12 MG/ML 15N
REMARK 210 SSO10A, 85% H2O, 10% D20, 5%
REMARK 210 C12E5/HEXANOL (R=0.87); 12 MG/ML
REMARK 210 15N SSO10A, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_12C-FILTERED_13C-EDITED_NOESY; HNHA; 2D_
REMARK 210 HSQC-IPAP; 2D_HSQC_T1_T1RHO_NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2004, NMRVIEW 5.2.2,
REMARK 210 MODELFREE 4, ARIA 1.2, XPLOR-NIH
REMARK 210 2.9.6
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 CARTESION AND TORSION ANGLE
REMARK 210 DYNAMICS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : 10 SMALLEST RMSD OUT OF 13
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: MODEL 1 IS AN ENERGY MINIMIZED AVERAGE STRUCTURE. MODELS 2
REMARK 210 THROUGH 11 ARE THE 10 BEST ENSEMBLE STRUCTURES.
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 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 PHE B 73 H ARG B 77 1.45
REMARK 500 O PHE A 73 H ARG A 77 1.45
REMARK 500 O MET B 80 H LYS B 84 1.46
REMARK 500 O MET A 80 H LYS A 84 1.46
REMARK 500 O ARG B 51 H MET B 58 1.49
REMARK 500 O ALA A 16 HG SER A 21 1.49
REMARK 500 O ALA B 16 HG SER B 21 1.50
REMARK 500 O LEU B 36 H ARG B 39 1.51
REMARK 500 O LEU A 36 H ARG A 39 1.51
REMARK 500 O THR B 37 H TYR B 40 1.56
REMARK 500 O THR A 37 H TYR A 40 1.57
REMARK 500 O ASN A 79 H LEU A 83 1.58
REMARK 500 O SER B 92 H GLN B 95 1.59
REMARK 500 O LYS B 42 H ASP B 46 1.59
REMARK 500 O ASN B 79 H LEU B 83 1.59
REMARK 500 O SER A 33 H LEU A 36 1.60
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 LYS A 3 -9.57 176.87
REMARK 500 1 LYS A 6 -36.33 -178.68
REMARK 500 1 LEU A 7 -63.13 -99.21
REMARK 500 1 LYS A 18 -1.56 -51.68
REMARK 500 1 SER A 19 28.02 -159.50
REMARK 500 1 TYR A 34 -46.78 -14.91
REMARK 500 1 GLU A 48 80.79 81.36
REMARK 500 1 ILE A 49 -37.52 -152.23
REMARK 500 1 SER A 92 -25.18 59.49
REMARK 500 1 ILE A 93 -74.68 81.74
REMARK 500 1 ARG A 94 17.32 -149.45
REMARK 500 1 LYS B 3 -5.03 -179.76
REMARK 500 1 LYS B 4 -148.85 -144.63
REMARK 500 1 SER B 5 12.08 46.85
REMARK 500 1 LYS B 6 -38.41 -177.66
REMARK 500 1 LEU B 7 -60.62 -98.87
REMARK 500 1 LYS B 18 -1.77 -51.58
REMARK 500 1 SER B 19 37.13 -160.87
REMARK 500 1 TYR B 28 -2.56 -58.76
REMARK 500 1 LEU B 32 102.76 32.25
REMARK 500 1 SER B 33 21.00 -72.43
REMARK 500 1 TYR B 34 -51.04 -10.74
REMARK 500 1 GLU B 48 70.44 79.21
REMARK 500 1 ILE B 49 -36.47 -145.46
REMARK 500 1 LYS B 55 -3.08 83.19
REMARK 500 1 SER B 92 29.13 37.68
REMARK 500 1 ILE B 93 -83.72 42.12
REMARK 500 1 ARG B 94 24.66 -143.42
REMARK 500 2 LYS A 3 -27.08 -163.97
REMARK 500 2 LYS A 4 -116.36 -60.63
REMARK 500 2 LYS A 6 -5.13 73.25
REMARK 500 2 LEU A 7 -64.06 -96.70
REMARK 500 2 LYS A 18 -4.18 -47.59
REMARK 500 2 SER A 19 36.55 -160.42
REMARK 500 2 ASN A 31 13.88 -68.51
REMARK 500 2 LEU A 32 100.79 32.63
REMARK 500 2 SER A 33 14.80 -65.81
REMARK 500 2 TYR A 34 -46.81 -16.99
REMARK 500 2 THR A 37 -38.71 -36.20
REMARK 500 2 GLU A 48 65.38 80.91
REMARK 500 2 ILE A 49 -41.92 -139.45
REMARK 500 2 LYS A 55 6.67 81.79
REMARK 500 2 SER A 92 -28.45 60.04
REMARK 500 2 ILE A 93 -59.64 62.05
REMARK 500 2 ARG A 94 -20.46 -157.01
REMARK 500 2 LYS B 3 -27.54 -165.85
REMARK 500 2 LYS B 4 -114.89 -60.41
REMARK 500 2 LYS B 6 -5.46 74.49
REMARK 500 2 LEU B 7 -62.68 -96.65
REMARK 500 2 LYS B 18 -5.99 -46.38
REMARK 500
REMARK 500 THIS ENTRY HAS 339 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XSX A 1 95 UNP Q5W1E8 Q5W1E8_SULSO 2 96
DBREF 1XSX B 1 95 UNP Q5W1E8 Q5W1E8_SULSO 2 96
SEQRES 1 A 95 ALA LYS LYS LYS SER LYS LEU GLU ILE ILE GLN ALA ILE
SEQRES 2 A 95 LEU GLU ALA CYS LYS SER GLY SER PRO LYS THR ARG ILE
SEQRES 3 A 95 MET TYR GLY ALA ASN LEU SER TYR ALA LEU THR GLY ARG
SEQRES 4 A 95 TYR ILE LYS MET LEU MET ASP LEU GLU ILE ILE ARG GLN
SEQRES 5 A 95 GLU GLY LYS GLN TYR MET LEU THR LYS LYS GLY GLU GLU
SEQRES 6 A 95 LEU LEU GLU ASP ILE ARG LYS PHE ASN GLU MET ARG LYS
SEQRES 7 A 95 ASN MET ASP GLN LEU LYS GLU LYS ILE ASN SER VAL LEU
SEQRES 8 A 95 SER ILE ARG GLN
SEQRES 1 B 95 ALA LYS LYS LYS SER LYS LEU GLU ILE ILE GLN ALA ILE
SEQRES 2 B 95 LEU GLU ALA CYS LYS SER GLY SER PRO LYS THR ARG ILE
SEQRES 3 B 95 MET TYR GLY ALA ASN LEU SER TYR ALA LEU THR GLY ARG
SEQRES 4 B 95 TYR ILE LYS MET LEU MET ASP LEU GLU ILE ILE ARG GLN
SEQRES 5 B 95 GLU GLY LYS GLN TYR MET LEU THR LYS LYS GLY GLU GLU
SEQRES 6 B 95 LEU LEU GLU ASP ILE ARG LYS PHE ASN GLU MET ARG LYS
SEQRES 7 B 95 ASN MET ASP GLN LEU LYS GLU LYS ILE ASN SER VAL LEU
SEQRES 8 B 95 SER ILE ARG GLN
HELIX 1 H1 GLU A 8 SER A 19 1 12
HELIX 2 H2 LYS A 23 GLY A 29 1 7
HELIX 3 H3 TYR A 34 ASP A 46 1 13
HELIX 4 H4 LYS A 61 LEU A 91 1 31
HELIX 5 H5 GLU B 8 SER B 19 1 12
HELIX 6 H6 LYS B 23 GLY B 29 1 7
HELIX 7 H7 TYR B 34 ASP B 46 1 13
HELIX 8 H8 LYS B 61 LEU B 91 1 31
SHEET 1 1 1 ILE A 50 GLU A 53 0
SHEET 1 2 1 GLN A 56 LEU A 59 0
SHEET 1 3 1 ILE B 50 GLU B 53 0
SHEET 1 4 1 GLN B 56 LEU B 59 0
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