Header list of 1uss.pdb file
Complete list - n 15 2 Bytes
HEADER DNA BINDING PROTEIN 30-NOV-03 1USS
TITLE YEAST HISTONE H1 GLOBULAR DOMAIN II, HHO1P GII, SOLUTION NMR
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN II, RESIDUES 171-258;
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
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR T.ALI,P.COLES,T.J.STEVENS,K.STOTT,J.O.THOMAS
REVDAT 3 15-JAN-20 1USS 1 REMARK
REVDAT 2 24-FEB-09 1USS 1 VERSN
REVDAT 1 01-APR-04 1USS 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 1USS 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_1290014084.
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 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 HB VAL A 238 HB2 ASN A 250 1.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 6 TYR A 180 CE1 TYR A 180 CZ 0.079
REMARK 500 6 TYR A 180 CZ TYR A 180 CE2 -0.088
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 PHE A 210 32.19 -92.91
REMARK 500 1 SER A 212 38.87 -96.26
REMARK 500 1 LYS A 213 -49.09 -158.76
REMARK 500 1 THR A 216 39.45 39.87
REMARK 500 1 SER A 218 -44.72 -160.41
REMARK 500 1 ASN A 219 38.89 -88.25
REMARK 500 1 LYS A 252 117.93 -166.11
REMARK 500 2 SER A 173 22.05 -151.88
REMARK 500 2 SER A 176 -43.15 -169.73
REMARK 500 2 LEU A 191 -61.23 -90.60
REMARK 500 2 ASN A 192 135.37 -172.76
REMARK 500 2 SER A 197 114.13 -160.75
REMARK 500 2 PHE A 210 35.48 -94.07
REMARK 500 2 LYS A 213 34.50 -82.55
REMARK 500 2 SER A 217 -146.13 -156.05
REMARK 500 2 SER A 218 33.89 -77.50
REMARK 500 2 ASN A 219 29.87 -142.63
REMARK 500 2 PRO A 240 -175.26 -67.58
REMARK 500 2 SER A 244 71.60 -151.26
REMARK 500 2 LYS A 255 121.07 73.34
REMARK 500 3 SER A 173 -134.25 -101.44
REMARK 500 3 SER A 177 -179.64 -177.55
REMARK 500 3 ASN A 192 -90.22 61.47
REMARK 500 3 THR A 216 147.54 -170.71
REMARK 500 3 SER A 217 -19.33 -163.35
REMARK 500 3 LYS A 241 36.49 -93.49
REMARK 500 3 ILE A 247 99.30 -68.17
REMARK 500 3 LYS A 252 36.06 -161.45
REMARK 500 3 LYS A 255 136.74 71.52
REMARK 500 4 SER A 173 -44.84 70.16
REMARK 500 4 SER A 176 -167.73 -107.37
REMARK 500 4 ASN A 192 48.86 -87.94
REMARK 500 4 SER A 197 134.14 -171.72
REMARK 500 4 SER A 218 44.63 -166.78
REMARK 500 4 GLN A 239 85.63 -164.42
REMARK 500 4 PRO A 243 47.30 -71.83
REMARK 500 4 SER A 244 39.87 -170.27
REMARK 500 4 LYS A 251 14.21 -151.04
REMARK 500 4 LYS A 252 123.44 -178.52
REMARK 500 4 LYS A 253 113.47 66.56
REMARK 500 5 SER A 173 -41.42 -165.08
REMARK 500 5 PRO A 175 41.60 -71.72
REMARK 500 5 SER A 176 -40.05 68.93
REMARK 500 5 SER A 177 -151.98 64.11
REMARK 500 5 LYS A 215 -40.33 77.03
REMARK 500 5 THR A 216 -46.21 64.03
REMARK 500 5 SER A 218 -49.56 69.35
REMARK 500 5 ASN A 219 45.30 -84.06
REMARK 500 5 SER A 244 40.98 -89.45
REMARK 500 5 LYS A 253 -151.25 -143.71
REMARK 500
REMARK 500 THIS ENTRY HAS 91 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 4 TYR A 222 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UST RELATED DB: PDB
REMARK 900 EAST HISTONE H1 GLOBULAR DOMAIN I, HHO1P GI, SOLUTION NMR STRUCTURES
REMARK 900 RELATED ID: 6162 RELATED DB: BMRB
DBREF 1USS A 171 258 UNP P53551 H1_YEAST 171 258
SEQRES 1 A 88 LYS ALA SER SER PRO SER SER LEU THR TYR LYS GLU MET
SEQRES 2 A 88 ILE LEU LYS SER MET PRO GLN LEU ASN ASP GLY LYS GLY
SEQRES 3 A 88 SER SER ARG ILE VAL LEU LYS LYS TYR VAL LYS ASP THR
SEQRES 4 A 88 PHE SER SER LYS LEU LYS THR SER SER ASN PHE ASP TYR
SEQRES 5 A 88 LEU PHE ASN SER ALA ILE LYS LYS CYS VAL GLU ASN GLY
SEQRES 6 A 88 GLU LEU VAL GLN PRO LYS GLY PRO SER GLY ILE ILE LYS
SEQRES 7 A 88 LEU ASN LYS LYS LYS VAL LYS LEU SER THR
HELIX 1 1 THR A 179 LEU A 191 1 13
HELIX 2 2 SER A 198 PHE A 210 1 13
HELIX 3 3 ASN A 219 GLY A 235 1 17
SHEET 1 AA 2 LEU A 237 VAL A 238 0
SHEET 2 AA 2 LYS A 248 LEU A 249 -1 O LYS A 248 N VAL A 238
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