Header list of 1uhm.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 05-JUL-03 1UHM
TITLE SOLUTION STRUCTURE OF THE GLOBULAR DOMAIN OF LINKER HISTONE HOMOLOG
TITLE 2 HHO1P FROM S. CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN;
COMPND 5 SYNONYM: HISTONE HHO1P;
COMPND 6 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 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: PET21B
KEYWDS WINGED HELIX-TURN-HELIX, LINKER HISTONE, S. CEREVISIAE, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL
KEYWDS 3 GENOMICS, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.ONO,O.KUSANO,S.SHIMOTAKAHARA,M.SHIMIZU,T.YAMAZAKI,H.SHINDO,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1UHM 1 REMARK
REVDAT 2 24-FEB-09 1UHM 1 VERSN
REVDAT 1 16-DEC-03 1UHM 0
JRNL AUTH K.ONO,O.KUSANO,S.SHIMOTAKAHARA,M.SHIMIZU,T.YAMAZAKI,H.SHINDO
JRNL TITL THE LINKER HISTONE HOMOLOG HHO1P FROM SACCHAROMYCES
JRNL TITL 2 CEREVISIAE REPRESENTS A WINGED HELIX-TURN-HELIX FOLD AS
JRNL TITL 3 DETERMINED BY NMR SPECTROSCOPY.
JRNL REF NUCLEIC ACIDS RES. V. 31 7199 2003
JRNL REFN ISSN 0305-1048
JRNL PMID 14654695
JRNL DOI 10.1093/NAR/GKG931
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A.T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UHM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000005836.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HD1 U-15N,13C; 10MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 H GLU A 104 O LYS A 114 1.49
REMARK 500 O ILE A 94 H VAL A 98 1.53
REMARK 500 O LYS A 71 H GLU A 75 1.55
REMARK 500 O GLU A 49 H GLU A 53 1.55
REMARK 500 O LYS A 95 H GLU A 99 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 1 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 2 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 3 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 4 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 5 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 6 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 7 SER A 44 N - CA - CB ANGL. DEV. = -10.2 DEGREES
REMARK 500 8 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 9 SER A 44 N - CA - CB ANGL. DEV. = -10.6 DEGREES
REMARK 500 10 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 11 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 12 SER A 44 N - CA - CB ANGL. DEV. = -10.5 DEGREES
REMARK 500 13 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 14 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 15 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 16 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
REMARK 500 17 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 18 SER A 44 N - CA - CB ANGL. DEV. = -10.1 DEGREES
REMARK 500 19 SER A 44 N - CA - CB ANGL. DEV. = -10.3 DEGREES
REMARK 500 20 SER A 44 N - CA - CB ANGL. DEV. = -10.4 DEGREES
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 SER A 43 40.56 -160.96
REMARK 500 1 SER A 44 105.64 52.11
REMARK 500 1 GLU A 75 -65.25 -95.88
REMARK 500 1 SER A 82 45.46 -82.43
REMARK 500 1 ALA A 83 -127.01 -119.78
REMARK 500 1 SER A 84 -78.52 -150.68
REMARK 500 1 PRO A 106 -157.50 -80.53
REMARK 500 1 LYS A 107 -82.50 -136.96
REMARK 500 1 ALA A 110 -103.88 -167.85
REMARK 500 1 ALA A 116 139.00 169.98
REMARK 500 2 SER A 43 -156.93 56.75
REMARK 500 2 GLU A 75 -65.44 -95.42
REMARK 500 2 SER A 82 42.29 -82.32
REMARK 500 2 ALA A 83 -133.76 -122.04
REMARK 500 2 SER A 84 -92.18 -143.90
REMARK 500 2 PRO A 106 -163.97 -78.33
REMARK 500 2 ALA A 110 -91.00 -165.57
REMARK 500 3 ALA A 42 59.99 -103.29
REMARK 500 3 SER A 43 43.99 -94.93
REMARK 500 3 SER A 44 178.07 50.77
REMARK 500 3 ARG A 61 -4.00 73.26
REMARK 500 3 GLU A 75 -65.81 -92.30
REMARK 500 3 SER A 84 -67.48 -127.21
REMARK 500 3 LYS A 107 -61.56 -123.02
REMARK 500 3 ALA A 110 -97.86 -167.86
REMARK 500 3 ALA A 116 57.48 31.91
REMARK 500 4 SER A 44 -175.95 50.15
REMARK 500 4 GLU A 60 157.81 56.19
REMARK 500 4 ARG A 61 166.17 167.96
REMARK 500 4 GLU A 75 -65.36 -94.00
REMARK 500 4 ALA A 83 -171.04 -51.67
REMARK 500 4 ALA A 110 -107.25 -162.66
REMARK 500 4 ALA A 116 108.07 -172.03
REMARK 500 5 SER A 44 -172.47 50.14
REMARK 500 5 LYS A 59 16.83 56.67
REMARK 500 5 GLU A 60 -152.47 -78.47
REMARK 500 5 ARG A 61 -150.33 -68.50
REMARK 500 5 GLU A 75 -65.70 -96.03
REMARK 500 5 ALA A 83 -151.35 -81.27
REMARK 500 5 SER A 84 -74.59 -132.78
REMARK 500 5 LYS A 107 -91.40 -98.17
REMARK 500 5 ALA A 110 -105.18 -164.97
REMARK 500 5 ALA A 116 60.09 14.83
REMARK 500 6 SER A 44 174.28 51.71
REMARK 500 6 GLU A 60 -159.06 -99.67
REMARK 500 6 ARG A 61 -46.14 -144.62
REMARK 500 6 GLU A 75 -65.02 -94.61
REMARK 500 6 ALA A 83 -169.20 -52.08
REMARK 500 6 SER A 84 -65.80 -124.62
REMARK 500 6 PRO A 106 -155.87 -89.94
REMARK 500
REMARK 500 THIS ENTRY HAS 199 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 1 ARG A 48 0.31 SIDE CHAIN
REMARK 500 1 ARG A 61 0.30 SIDE CHAIN
REMARK 500 1 ARG A 66 0.29 SIDE CHAIN
REMARK 500 2 ARG A 48 0.31 SIDE CHAIN
REMARK 500 2 ARG A 61 0.20 SIDE CHAIN
REMARK 500 2 ARG A 66 0.30 SIDE CHAIN
REMARK 500 3 ARG A 48 0.23 SIDE CHAIN
REMARK 500 3 ARG A 61 0.32 SIDE CHAIN
REMARK 500 3 ARG A 66 0.31 SIDE CHAIN
REMARK 500 4 ARG A 48 0.28 SIDE CHAIN
REMARK 500 4 ARG A 61 0.32 SIDE CHAIN
REMARK 500 4 ARG A 66 0.30 SIDE CHAIN
REMARK 500 5 ARG A 48 0.31 SIDE CHAIN
REMARK 500 5 ARG A 61 0.31 SIDE CHAIN
REMARK 500 5 ARG A 66 0.31 SIDE CHAIN
REMARK 500 6 ARG A 48 0.17 SIDE CHAIN
REMARK 500 6 ARG A 61 0.12 SIDE CHAIN
REMARK 500 7 ARG A 48 0.15 SIDE CHAIN
REMARK 500 7 ARG A 61 0.32 SIDE CHAIN
REMARK 500 7 ARG A 66 0.32 SIDE CHAIN
REMARK 500 8 ARG A 48 0.22 SIDE CHAIN
REMARK 500 8 ARG A 61 0.20 SIDE CHAIN
REMARK 500 8 ARG A 66 0.20 SIDE CHAIN
REMARK 500 9 ARG A 48 0.26 SIDE CHAIN
REMARK 500 9 ARG A 61 0.24 SIDE CHAIN
REMARK 500 9 ARG A 66 0.21 SIDE CHAIN
REMARK 500 10 ARG A 48 0.30 SIDE CHAIN
REMARK 500 10 ARG A 61 0.29 SIDE CHAIN
REMARK 500 10 ARG A 66 0.23 SIDE CHAIN
REMARK 500 11 ARG A 48 0.32 SIDE CHAIN
REMARK 500 11 ARG A 61 0.31 SIDE CHAIN
REMARK 500 11 ARG A 66 0.24 SIDE CHAIN
REMARK 500 12 ARG A 48 0.25 SIDE CHAIN
REMARK 500 12 ARG A 61 0.30 SIDE CHAIN
REMARK 500 12 ARG A 66 0.30 SIDE CHAIN
REMARK 500 13 ARG A 48 0.22 SIDE CHAIN
REMARK 500 13 ARG A 61 0.24 SIDE CHAIN
REMARK 500 13 ARG A 66 0.32 SIDE CHAIN
REMARK 500 14 ARG A 48 0.19 SIDE CHAIN
REMARK 500 14 ARG A 61 0.32 SIDE CHAIN
REMARK 500 14 ARG A 66 0.31 SIDE CHAIN
REMARK 500 15 ARG A 48 0.15 SIDE CHAIN
REMARK 500 15 ARG A 61 0.31 SIDE CHAIN
REMARK 500 15 ARG A 66 0.20 SIDE CHAIN
REMARK 500 16 ARG A 48 0.24 SIDE CHAIN
REMARK 500 16 ARG A 61 0.28 SIDE CHAIN
REMARK 500 16 ARG A 66 0.30 SIDE CHAIN
REMARK 500 17 ARG A 48 0.16 SIDE CHAIN
REMARK 500 17 ARG A 61 0.22 SIDE CHAIN
REMARK 500 17 ARG A 66 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 58 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TRT001000359.1 RELATED DB: TARGETDB
DBREF 1UHM A 41 118 UNP P53551 H1_YEAST 41 118
SEQRES 1 A 78 GLU ALA SER SER LYS SER TYR ARG GLU LEU ILE ILE GLU
SEQRES 2 A 78 GLY LEU THR ALA LEU LYS GLU ARG LYS GLY SER SER ARG
SEQRES 3 A 78 PRO ALA LEU LYS LYS PHE ILE LYS GLU ASN TYR PRO ILE
SEQRES 4 A 78 VAL GLY SER ALA SER ASN PHE ASP LEU TYR PHE ASN ASN
SEQRES 5 A 78 ALA ILE LYS LYS GLY VAL GLU ALA GLY ASP PHE GLU GLN
SEQRES 6 A 78 PRO LYS GLY PRO ALA GLY ALA VAL LYS LEU ALA LYS LYS
HELIX 1 1 SER A 46 LYS A 59 1 14
HELIX 2 2 ARG A 66 GLU A 75 1 10
HELIX 3 3 ASN A 85 ALA A 100 1 16
SHEET 1 A 3 SER A 64 SER A 65 0
SHEET 2 A 3 ALA A 112 LEU A 115 -1 O VAL A 113 N SER A 64
SHEET 3 A 3 PHE A 103 GLU A 104 -1 N GLU A 104 O 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 - r 2 2 Bytes