Header list of 1ust.pdb file
Complete list - n 15 2 Bytes
HEADER DNA BINDING PROTEIN 30-NOV-03 1UST
TITLE YEAST HISTONE H1 GLOBULAR DOMAIN I, HHO1P GI, SOLUTION NMR STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN I, RESIDUES 38-130;
COMPND 5 ENGINEERED: 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS DNA BINDING PROTEIN, LINKER HISTONE, DNA BINDING DOMAIN, WINGED HELIX
KEYWDS 2 FOLD
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.ALI,P.COLES,T.J.STEVENS,K.STOTT,J.O.THOMAS
REVDAT 3 15-JAN-20 1UST 1 REMARK
REVDAT 2 24-FEB-09 1UST 1 VERSN
REVDAT 1 01-APR-04 1UST 0
JRNL AUTH T.ALI,P.COLES,T.J.STEVENS,K.STOTT,J.O.THOMAS
JRNL TITL TWO HOMOLOGOUS DOMAINS OF SIMILAR STRUCTURE BUT DIFFERENT
JRNL TITL 2 STABILITY IN THE YEAST LINKER HISTONE, HHO1P
JRNL REF J.MOL.BIOL. V. 338 139 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15050829
JRNL DOI 10.1016/J.JMB.2004.02.046
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-
REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UST COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1290014057.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
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 : ARIA, CNS
REMARK 210 METHOD USED : DISTANCE GEOMETRY, BOND ANGLE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMUM 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 400
REMARK 400 COMPOUND
REMARK 400 COULD ACT AS AN H1-TYPE LINKER HISTONE. HAS BEEN SHOWN
REMARK 400 TO BIND DNA.
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 38
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 ILE A 51 H LEU A 55 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 GLU A 40 -51.39 -151.35
REMARK 500 1 ALA A 42 41.90 -82.36
REMARK 500 1 SER A 43 -142.11 -170.73
REMARK 500 1 GLU A 60 -109.36 56.20
REMARK 500 1 LYS A 62 -48.20 -175.20
REMARK 500 1 TYR A 77 73.51 -119.87
REMARK 500 1 LYS A 117 -40.72 -131.53
REMARK 500 1 PRO A 121 -178.61 -67.23
REMARK 500 1 LYS A 127 -74.13 68.34
REMARK 500 1 GLU A 128 54.29 -158.13
REMARK 500 2 GLU A 40 -136.04 57.79
REMARK 500 2 ALA A 42 -146.72 -76.26
REMARK 500 2 SER A 43 28.65 -79.53
REMARK 500 2 SER A 44 38.87 -77.33
REMARK 500 2 TYR A 47 -44.35 71.49
REMARK 500 2 GLU A 60 -113.35 58.76
REMARK 500 2 LYS A 62 -43.03 -173.29
REMARK 500 2 LYS A 118 170.63 62.23
REMARK 500 2 GLU A 122 49.56 -149.47
REMARK 500 2 GLU A 128 -35.31 75.37
REMARK 500 2 VAL A 129 -50.79 74.82
REMARK 500 3 SER A 43 -7.93 -156.90
REMARK 500 3 GLU A 60 -115.13 63.29
REMARK 500 3 LYS A 62 27.74 -179.18
REMARK 500 3 SER A 84 -62.35 69.75
REMARK 500 3 ALA A 110 43.80 -104.50
REMARK 500 3 SER A 120 120.19 72.04
REMARK 500 3 GLU A 122 42.29 -151.61
REMARK 500 3 LYS A 127 -142.95 -163.46
REMARK 500 3 VAL A 129 47.09 -165.96
REMARK 500 4 LEU A 58 30.97 -89.16
REMARK 500 4 GLU A 60 -48.82 66.63
REMARK 500 4 ARG A 61 -28.26 -155.59
REMARK 500 4 LYS A 62 -42.11 -168.05
REMARK 500 4 LYS A 119 41.72 -92.03
REMARK 500 4 GLU A 122 57.85 -174.73
REMARK 500 4 LYS A 124 45.88 -158.81
REMARK 500 4 GLU A 126 -126.46 63.86
REMARK 500 4 GLU A 128 -28.15 -171.34
REMARK 500 4 VAL A 129 -32.04 -165.96
REMARK 500 5 GLU A 41 -167.50 56.63
REMARK 500 5 SER A 43 35.98 -78.30
REMARK 500 5 SER A 44 38.50 -87.81
REMARK 500 5 GLU A 60 -106.87 57.44
REMARK 500 5 LYS A 62 -40.35 -179.61
REMARK 500 5 PRO A 106 42.08 -78.48
REMARK 500 5 LYS A 107 -48.34 -145.80
REMARK 500 5 LYS A 118 -151.89 -165.25
REMARK 500 5 GLU A 122 40.37 -91.06
REMARK 500 5 LYS A 124 -59.45 -165.95
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1USS RELATED DB: PDB
REMARK 900 YEAST HISTONE H1 GLOBULAR DOMAIN II, HHO1P GII, SOLUTION NMR
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 6161 RELATED DB: BMRB
DBREF 1UST A 38 130 UNP P53551 H1_YEAST 38 130
SEQRES 1 A 93 LYS LYS GLU GLU ALA SER SER LYS SER TYR ARG GLU LEU
SEQRES 2 A 93 ILE ILE GLU GLY LEU THR ALA LEU LYS GLU ARG LYS GLY
SEQRES 3 A 93 SER SER ARG PRO ALA LEU LYS LYS PHE ILE LYS GLU ASN
SEQRES 4 A 93 TYR PRO ILE VAL GLY SER ALA SER ASN PHE ASP LEU TYR
SEQRES 5 A 93 PHE ASN ASN ALA ILE LYS LYS GLY VAL GLU ALA GLY ASP
SEQRES 6 A 93 PHE GLU GLN PRO LYS GLY PRO ALA GLY ALA VAL LYS LEU
SEQRES 7 A 93 ALA LYS LYS LYS SER PRO GLU VAL LYS LYS GLU LYS GLU
SEQRES 8 A 93 VAL SER
HELIX 1 1 SER A 46 THR A 56 1 11
HELIX 2 2 ARG A 66 TYR A 77 1 12
HELIX 3 3 TYR A 77 SER A 82 1 6
HELIX 4 4 ASN A 85 ALA A 100 1 16
SHEET 1 AA 3 SER A 64 SER A 65 0
SHEET 2 AA 3 ALA A 112 LEU A 115 -1 O VAL A 113 N SER A 64
SHEET 3 AA 3 PHE A 103 GLU A 104 -1 O GLU A 104 N LYS A 114
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 - n 15 2 Bytes