Header list of 1yqa.pdb file
Complete list - t 20 2 Bytes
HEADER DNA BINDING PROTEIN 01-FEB-05 1YQA
TITLE ENGINEERING THE STRUCTURAL STABILITY AND FUNCTIONAL PROPERTIES OF THE
TITLE 2 GI DOMAIN INTO THE INTRINSICALLY UNFOLDED GII DOMAIN OF THE YEAST
TITLE 3 LINKER HISTONE HHO1P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GII LOOP MUTANT (GII-L), RESIDUES 171-258;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: HHO1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS WINGED-HELIX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.SANDERSON,K.STOTT,T.J.STEVENS,J.O.THOMAS
REVDAT 3 20-OCT-21 1YQA 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1YQA 1 VERSN
REVDAT 1 24-MAY-05 1YQA 0
JRNL AUTH A.SANDERSON,K.STOTT,T.J.STEVENS,J.O.THOMAS
JRNL TITL ENGINEERING THE STRUCTURAL STABILITY AND FUNCTIONAL
JRNL TITL 2 PROPERTIES OF THE GI DOMAIN INTO THE INTRINSICALLY UNFOLDED
JRNL TITL 3 GII DOMAIN OF THE YEAST LINKER HISTONE HHO1P.
JRNL REF J.MOL.BIOL. V. 349 608 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15878177
JRNL DOI 10.1016/J.JMB.2005.03.085
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.ALI,P.COLES,T.J.STEVENS,K.STOTT,J.O.THOMAS
REMARK 1 TITL TWO HOMOLOGOUS DOMAINS OF SIMILAR STRUCTURE BUT DIFFERENT
REMARK 1 TITL 2 STABILITY IN THE YEAST LINKER HISTONE, HHO1P
REMARK 1 REF J.MOL.BIOL. V. 338 139 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 15050829
REMARK 1 DOI 10.1016/J.JMB.2004.02.046
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YQA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031804.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM GII-L U-15N,13C; 100MM
REMARK 210 PHOSPHATE BUFFER; 1MM EDTA; 1-
REMARK 210 2MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AZARA 2.7, ANALYSIS 1.0, ARIA
REMARK 210 1.1.2, CNS 1.1
REMARK 210 METHOD USED : SEE JOURNAL CITATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: 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
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 PRO A 175 -144.76 -75.04
REMARK 500 1 ASN A 249 -70.32 -74.12
REMARK 500 1 LYS A 252 31.19 -79.77
REMARK 500 1 VAL A 253 106.73 -164.69
REMARK 500 1 LYS A 254 32.58 -164.12
REMARK 500 2 PRO A 175 33.38 -74.94
REMARK 500 2 SER A 176 -64.95 68.45
REMARK 500 2 ASN A 218 39.61 -92.65
REMARK 500 2 LYS A 251 -44.27 -175.19
REMARK 500 2 LYS A 254 76.43 64.46
REMARK 500 2 SER A 256 -117.55 -169.29
REMARK 500 3 PRO A 175 -140.82 -77.60
REMARK 500 3 ASN A 192 -59.25 68.71
REMARK 500 3 ASP A 193 -36.64 175.86
REMARK 500 3 SER A 215 -48.74 -171.33
REMARK 500 3 SER A 243 -123.01 -143.16
REMARK 500 3 LYS A 251 -48.79 68.20
REMARK 500 3 SER A 256 47.05 -160.72
REMARK 500 4 ALA A 172 91.29 -69.12
REMARK 500 4 SER A 173 -56.40 -156.84
REMARK 500 4 PRO A 175 -134.94 -75.19
REMARK 500 4 SER A 176 -47.94 -152.69
REMARK 500 4 ASN A 218 38.52 -90.07
REMARK 500 4 SER A 256 -48.48 -147.00
REMARK 500 5 SER A 215 48.26 -95.45
REMARK 500 5 LYS A 250 36.50 -76.61
REMARK 500 5 LEU A 255 -131.35 -80.57
REMARK 500 6 ALA A 172 43.01 -81.97
REMARK 500 6 PRO A 175 -136.35 -72.17
REMARK 500 6 SER A 176 -46.89 -155.35
REMARK 500 6 ASN A 218 36.78 -95.01
REMARK 500 7 PRO A 175 -143.04 -70.25
REMARK 500 7 SER A 215 51.89 -160.23
REMARK 500 7 ILE A 245 114.87 -160.74
REMARK 500 7 LYS A 254 145.01 71.21
REMARK 500 8 PRO A 175 -148.80 -71.01
REMARK 500 8 ASN A 218 35.58 -87.04
REMARK 500 8 SER A 256 133.69 -172.45
REMARK 500 9 PRO A 175 -144.25 -75.84
REMARK 500 9 SER A 176 -39.96 -140.28
REMARK 500 9 LYS A 250 53.64 -167.09
REMARK 500 10 ALA A 172 -139.20 -94.92
REMARK 500 10 PRO A 175 -140.48 -69.34
REMARK 500 10 SER A 215 33.95 -97.82
REMARK 500 10 ASN A 218 48.67 -92.99
REMARK 500 10 SER A 243 42.67 -84.18
REMARK 500 10 ASN A 249 86.82 -69.55
REMARK 500 10 LYS A 250 42.01 -87.70
REMARK 500 10 LYS A 254 146.85 64.56
REMARK 500 10 LEU A 255 -143.66 -78.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UST RELATED DB: PDB
REMARK 900 YEAST HISTONE H1 GLOBULAR DOMAIN I, HHO1P GI
REMARK 900 RELATED ID: 1USS RELATED DB: PDB
REMARK 900 YEAST HISTONE H1 GLOBULAR DOMAIN II, HHO1P GII
DBREF 1YQA A 171 257 UNP P53551 H1_YEAST 171 258
SEQADV 1YQA TYR A 210 UNP P53551 PHE 210 ENGINEERED MUTATION
SEQADV 1YQA PRO A 211 UNP P53551 SER 211 ENGINEERED MUTATION
SEQADV 1YQA ILE A 212 UNP P53551 SER 212 ENGINEERED MUTATION
SEQADV 1YQA VAL A 213 UNP P53551 LYS 213 ENGINEERED MUTATION
SEQADV 1YQA GLY A 214 UNP P53551 LEU 214 ENGINEERED MUTATION
SEQADV 1YQA SER A 215 UNP P53551 LYS 215 ENGINEERED MUTATION
SEQADV 1YQA ALA A 216 UNP P53551 THR 216 ENGINEERED MUTATION
SEQADV 1YQA A UNP P53551 SER 217 DELETION
SEQRES 1 A 87 LYS ALA SER SER PRO SER SER LEU THR TYR LYS GLU MET
SEQRES 2 A 87 ILE LEU LYS SER MET PRO GLN LEU ASN ASP GLY LYS GLY
SEQRES 3 A 87 SER SER ARG ILE VAL LEU LYS LYS TYR VAL LYS ASP THR
SEQRES 4 A 87 TYR PRO ILE VAL GLY SER ALA SER ASN PHE ASP TYR LEU
SEQRES 5 A 87 PHE ASN SER ALA ILE LYS LYS CYS VAL GLU ASN GLY GLU
SEQRES 6 A 87 LEU VAL GLN PRO LYS GLY PRO SER GLY ILE ILE LYS LEU
SEQRES 7 A 87 ASN LYS LYS LYS VAL LYS LEU SER THR
HELIX 1 1 THR A 179 MET A 188 1 10
HELIX 2 2 GLN A 190 LYS A 195 5 6
HELIX 3 3 SER A 198 TYR A 210 1 13
HELIX 4 4 TYR A 210 ALA A 216 1 7
HELIX 5 5 ASN A 218 GLY A 234 1 17
SHEET 1 A 2 LEU A 236 VAL A 237 0
SHEET 2 A 2 LYS A 247 LEU A 248 -1 O LYS A 247 N VAL A 237
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 20 2 Bytes