Header list of 2a2y.pdb file
Complete list - r 9 2 Bytes
HEADER DNA,RNA BINDING PROTEIN 23-JUN-05 2A2Y
TITLE NMR STRUCTUE OF SSO10B2 FROM SULFOLOBUS SOLFATARICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA/RNA-BINDING PROTEIN ALBA 2;
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: ALBA2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTABLUE(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETBLUE-2
KEYWDS HYPERTHERMOPHILE PROTEIN, DIMER, DNA, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR K.BIYANI,M.A.KAHSAI,A.T.CLARK,T.L.ARMSTRONG,S.P.EDMONDSON,J.W.SHRIVER
REVDAT 3 09-MAR-22 2A2Y 1 REMARK
REVDAT 2 24-FEB-09 2A2Y 1 VERSN
REVDAT 1 08-NOV-05 2A2Y 0
JRNL AUTH K.BIYANI,M.A.KAHSAI,A.T.CLARK,T.L.ARMSTRONG,S.P.EDMONDSON,
JRNL AUTH 2 J.W.SHRIVER
JRNL TITL SOLUTION STRUCTURE, STABILITY, AND NUCLEIC ACID BINDING OF
JRNL TITL 2 THE HYPERTHERMOPHILE PROTEIN SSO10B2.
JRNL REF BIOCHEMISTRY V. 44 14217 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16245938
JRNL DOI 10.1021/BI051266R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, XPLOR-NIH 2.9.7
REMARK 3 AUTHORS : VARIAN, INC. (VNMR), G.M. CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NOE ASSIGNMENTS, DISTANCE RESTRAINT
REMARK 3 CALIBRATIONS, AND INITIAL STRUCTURES WERE MADE USING ARIA 1.2.
REMARK 3 FINAL STRUCTURE REFINEMENT WAS DONE USING XPLOR-NIH WITH THE NOE
REMARK 3 DERIVED DISTANCE RESTRAINTS, 126 PHI/PSI DIHEDRAL ANGLES, 48
REMARK 3 HNHA COUPLING CONSTANTS, 33 HYDROGEN BONDS, 80 DIPOLAR COUPLINGS,
REMARK 3 57 T1/T2 RELAXATION RATIOS, AND NON-CRYSTALLOGRAPHIC DIMER
REMARK 3 SYMMETRY RESTRAINTS (NUMBERS ARE PER MONOMER). ANISOTROPY
REMARK 3 TENSORS WERE REFINED SIMULTANEOUSLY WITH THE STRUCTURE.
REMARK 4
REMARK 4 2A2Y COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033424.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM SSO10B2, U-15N, U-13C, PH
REMARK 210 4.8, 90% H2O, 10% D2O; 1 MM
REMARK 210 SSO10B2, U-15N, U-13C, PH 4.8,
REMARK 210 99.996% D2O; 1 MM SSO10B2, U-15N,
REMARK 210 PH 4.8, 90% H2O, 10% D2O;
REMARK 210 HETERO-LABELED DIMER CONSISTING
REMARK 210 OF 0.5 MM SSO10B2 U-15N, U-13C,
REMARK 210 0.5 MM SSO10B2 UNLABLED PH 5.0,
REMARK 210 99.996% D2O; 1 MM SSO10B2, U-15N,
REMARK 210 PH 4.8, 90% H2O, 10% D2O WITH
REMARK 210 ALIGNMENT MEDIA CONSISTING OF 5%
REMARK 210 C12E5/HEXANOL (R=.87)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; T1_T1RHO_
REMARK 210 HSQC; 2D_1H-15N_NOE; 12C-
REMARK 210 FILTERED_C13-EDITED_NOESY; IPAP_
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2004, NMRVIEW 5.2.2,
REMARK 210 ARIA 1.2, TENSOR2 2
REMARK 210 METHOD USED : SIMULATED ANNEALING USING
REMARK 210 CARTESIAN AND TORSION ANGLE
REMARK 210 DYNAMICS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : 10 STRUCTURES WITH THE LOWEST
REMARK 210 TOTAL ENERGY INCLUDING RESTRAINT
REMARK 210 TERMS
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 27 H GLY B 30 1.49
REMARK 500 H SER A 70 OD1 ASN B 51 1.50
REMARK 500 O GLN B 62 H LYS B 86 1.52
REMARK 500 O LEU A 57 H ASP A 59 1.55
REMARK 500 H VAL B 10 O LYS B 37 1.58
REMARK 500 O ASP A 48 H SER A 52 1.58
REMARK 500 OD1 ASN A 51 H SER B 70 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 1 LYS A 4 59.14 -146.59
REMARK 500 1 LEU A 5 52.55 -172.51
REMARK 500 1 ASN A 15 -179.44 -69.00
REMARK 500 1 ASP A 55 -6.96 -57.63
REMARK 500 1 LEU A 57 -29.03 -152.42
REMARK 500 1 ASP A 74 40.20 85.69
REMARK 500 1 LYS B 4 59.25 -150.84
REMARK 500 1 LEU B 5 49.60 -172.56
REMARK 500 1 LYS B 14 -113.94 -83.80
REMARK 500 1 ASP B 55 -7.78 -56.26
REMARK 500 1 LEU B 57 -35.27 -157.14
REMARK 500 1 ASP B 74 41.84 82.20
REMARK 500 2 GLU A 3 -49.29 -165.69
REMARK 500 2 LYS A 4 53.86 -156.53
REMARK 500 2 LEU A 5 49.99 -172.10
REMARK 500 2 LYS A 14 -130.41 -90.44
REMARK 500 2 ALA A 46 -38.18 -29.22
REMARK 500 2 VAL A 47 -74.88 -73.64
REMARK 500 2 ASP A 55 -7.90 -56.53
REMARK 500 2 LEU A 57 -24.37 -153.73
REMARK 500 2 ASP A 74 39.75 77.73
REMARK 500 2 GLU B 3 -50.11 -165.82
REMARK 500 2 LYS B 4 58.43 -160.21
REMARK 500 2 LEU B 5 46.85 -175.91
REMARK 500 2 LYS B 14 -115.91 -92.97
REMARK 500 2 LYS B 45 -71.33 -63.32
REMARK 500 2 ALA B 46 -43.29 -24.53
REMARK 500 2 LEU B 57 -23.59 -154.61
REMARK 500 2 ASP B 74 39.13 78.21
REMARK 500 3 GLU A 3 -53.83 -164.53
REMARK 500 3 LYS A 4 57.67 -158.63
REMARK 500 3 LEU A 5 46.25 -176.21
REMARK 500 3 LEU A 57 -3.95 -161.83
REMARK 500 3 ASP A 74 36.50 87.19
REMARK 500 3 GLU B 3 -51.11 -166.17
REMARK 500 3 LYS B 4 58.45 -161.64
REMARK 500 3 LEU B 5 47.82 -173.93
REMARK 500 3 LYS B 14 -131.00 -99.34
REMARK 500 3 ASP B 55 -11.84 -49.98
REMARK 500 3 LEU B 57 -3.78 -159.83
REMARK 500 3 ASP B 74 35.44 86.91
REMARK 500 4 THR A 2 -72.11 -96.37
REMARK 500 4 GLU A 3 -32.93 74.02
REMARK 500 4 LYS A 4 53.42 -155.88
REMARK 500 4 ASN A 6 94.51 177.45
REMARK 500 4 LYS A 45 -70.43 -66.17
REMARK 500 4 ALA A 46 -51.34 -29.46
REMARK 500 4 ASP A 55 -9.21 -56.05
REMARK 500 4 LEU A 57 -15.45 -153.86
REMARK 500 4 ASN A 65 148.61 -172.59
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2A2Y A 1 89 UNP Q97ZF4 ALBA2_SULSO 1 89
DBREF 2A2Y B 1 89 UNP Q97ZF4 ALBA2_SULSO 1 89
SEQRES 1 A 89 MET THR GLU LYS LEU ASN GLU ILE VAL VAL ARG LYS THR
SEQRES 2 A 89 LYS ASN VAL GLU ASP HIS VAL LEU ASP VAL ILE VAL LEU
SEQRES 3 A 89 PHE ASN GLN GLY ILE ASP GLU VAL ILE LEU LYS GLY THR
SEQRES 4 A 89 GLY ARG GLU ILE SER LYS ALA VAL ASP VAL TYR ASN SER
SEQRES 5 A 89 LEU LYS ASP ARG LEU GLY ASP GLY VAL GLN LEU VAL ASN
SEQRES 6 A 89 VAL GLN THR GLY SER GLU VAL ARG ASP ARG ARG ARG ILE
SEQRES 7 A 89 SER TYR ILE LEU LEU ARG LEU LYS ARG VAL TYR
SEQRES 1 B 89 MET THR GLU LYS LEU ASN GLU ILE VAL VAL ARG LYS THR
SEQRES 2 B 89 LYS ASN VAL GLU ASP HIS VAL LEU ASP VAL ILE VAL LEU
SEQRES 3 B 89 PHE ASN GLN GLY ILE ASP GLU VAL ILE LEU LYS GLY THR
SEQRES 4 B 89 GLY ARG GLU ILE SER LYS ALA VAL ASP VAL TYR ASN SER
SEQRES 5 B 89 LEU LYS ASP ARG LEU GLY ASP GLY VAL GLN LEU VAL ASN
SEQRES 6 B 89 VAL GLN THR GLY SER GLU VAL ARG ASP ARG ARG ARG ILE
SEQRES 7 B 89 SER TYR ILE LEU LEU ARG LEU LYS ARG VAL TYR
HELIX 1 1 ASN A 15 PHE A 27 1 13
HELIX 2 2 ARG A 41 GLY A 58 1 18
HELIX 3 3 ASN B 15 GLN B 29 1 15
HELIX 4 4 ARG B 41 ASP B 55 1 15
SHEET 1 A 4 ASN A 6 VAL A 9 0
SHEET 2 A 4 VAL A 34 THR A 39 1 O ILE A 35 N ILE A 8
SHEET 3 A 4 ARG A 77 LEU A 85 -1 O LEU A 83 N LEU A 36
SHEET 4 A 4 VAL A 66 VAL A 72 -1 N GLN A 67 O LEU A 82
SHEET 1 B 4 ASN B 6 VAL B 9 0
SHEET 2 B 4 VAL B 34 THR B 39 1 O ILE B 35 N ILE B 8
SHEET 3 B 4 ARG B 77 LEU B 85 -1 O LEU B 83 N LEU B 36
SHEET 4 B 4 VAL B 66 VAL B 72 -1 N GLN B 67 O LEU B 82
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 9 2 Bytes