HEADER DNA BINDING PROTEIN 12-MAR-19 6R0C
TITLE HUMAN-D02 NUCLEOSOME CORE PARTICLE WITH BIOTIN-STREPTAVIDIN LABEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.3;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A TYPE 1;
COMPND 11 CHAIN: C, G;
COMPND 12 SYNONYM: H2A.1,HISTONE H2A/PTL;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: HISTONE H2B TYPE 1-C/E/F/G/I;
COMPND 16 CHAIN: D, H;
COMPND 17 SYNONYM: HISTONE H2B.1 A,HISTONE H2B.A,H2B/A,HISTONE H2B.G,H2B/G,
COMPND 18 HISTONE H2B.H,H2B/H,HISTONE H2B.K,H2B/K,HISTONE H2B.L,H2B/L;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: DNA (142-MER);
COMPND 22 CHAIN: I;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: DNA (142-MER);
COMPND 26 CHAIN: J;
COMPND 27 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: H3F3A, H3.3A, H3F3, PP781, H3F3B, H3.3B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G,
SOURCE 13 H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C,
SOURCE 14 H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E,
SOURCE 15 H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N,
SOURCE 16 H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 GENE: HIST1H2AG, H2AFP, HIST1H2AI, H2AFC, HIST1H2AK, H2AFD,
SOURCE 24 HIST1H2AL, H2AFI, HIST1H2AM, H2AFN;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 MOL_ID: 4;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_COMMON: HUMAN;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 GENE: HIST1H2BC, H2BFL, HIST1H2BE, H2BFH, HIST1H2BF, H2BFG,
SOURCE 32 HIST1H2BG, H2BFA, HIST1H2BI, H2BFK;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 35 MOL_ID: 5;
SOURCE 36 SYNTHETIC: YES;
SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 38 ORGANISM_TAXID: 9606;
SOURCE 39 MOL_ID: 6;
SOURCE 40 SYNTHETIC: YES;
SOURCE 41 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 42 ORGANISM_TAXID: 9606
KEYWDS CHROMATIN, NUCLEOSOME, RETROVIRUS, DNA BINDING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR V.E.PYE,M.D.WILSON,P.CHEREPANOV,A.COSTA
REVDAT 2 18-DEC-19 6R0C 1 CRYST1 SCALE
REVDAT 1 25-SEP-19 6R0C 0
JRNL AUTH M.D.WILSON,L.RENAULT,D.P.MASKELL,M.GHONEIM,V.E.PYE,A.NANS,
JRNL AUTH 2 D.S.RUEDA,P.CHEREPANOV,A.COSTA
JRNL TITL RETROVIRAL INTEGRATION INTO NUCLEOSOMES THROUGH DNA LOOPING
JRNL TITL 2 AND SLIDING ALONG THE HISTONE OCTAMER.
JRNL REF NAT COMMUN V. 10 4189 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31519882
JRNL DOI 10.1038/S41467-019-12007-W
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, EPU, GCTF, COOT, RELION,
REMARK 3 RELION, RELION, RELION, PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3UTB
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : THE INITIAL MODEL WAS PLACED IN THE DENSITY
REMARK 3 USING CHIMERA. MANUAL BUILDING WAS PERFORMED IN COOT AND FINAL
REMARK 3 REFINEMENT WAS CARRIED OUT USING PHENIX.REAL_SPACE_REFINE.
REMARK 3 ADDITIONAL RESTRAINTS DESCRIBING PROTEIN SECONDARY STRUCTURE,
REMARK 3 DNA BASE PAIRING AND STACKING WERE USED IN PHENIX.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.200
REMARK 3 NUMBER OF PARTICLES : 62196
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6R0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-19.
REMARK 100 THE DEPOSITION ID IS D_1292100775.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : HUMAN-D02 NUCLEOSOME CORE
REMARK 245 PARTICLE WITH BIOTIN-
REMARK 245 STREPTAVIDIN LABEL; HISTONES;
REMARK 245 DNA
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.18
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.00
REMARK 245 SAMPLE DETAILS : HUMAN HISTONES REFOLDED AS AN
REMARK 245 OCTAMER WITH NATIVE HUMAN D02 SEQUENCE WITH FLEXIBLE LINKER
REMARK 245 BIOTIN.TETRAVALENT STREPTAVIDIN ADDED ONTO REFOLDED NUCLEOSOMES
REMARK 245 AND SAMPLE CROSSLINKED WITH GLUTARALDEHYDE; HISTONES; DNA
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4182
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1.50
REMARK 245 MAXIMUM DEFOCUS (NM) : 3.50
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 28.30
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 75000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 51850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 77490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -392.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 SER A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 LYS A 37
REMARK 465 PRO A 38
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 ALA C 10
REMARK 465 ARG C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 ALA C 14
REMARK 465 LYS C 15
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 HIS C 123
REMARK 465 HIS C 124
REMARK 465 LYS C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 GLY C 128
REMARK 465 LYS C 129
REMARK 465 MET D -3
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 ALA D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
REMARK 465 LYS D 27
REMARK 465 ARG D 28
REMARK 465 LYS D 122
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 SER E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 PRO E 38
REMARK 465 MET F 0
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 LYS F 16
REMARK 465 ARG F 17
REMARK 465 HIS F 18
REMARK 465 ARG F 19
REMARK 465 LYS F 20
REMARK 465 VAL F 21
REMARK 465 LEU F 22
REMARK 465 ARG F 23
REMARK 465 ASP F 24
REMARK 465 GLY F 101
REMARK 465 GLY F 102
REMARK 465 MET G 0
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 ALA G 10
REMARK 465 ARG G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 HIS G 123
REMARK 465 HIS G 124
REMARK 465 LYS G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 GLY G 128
REMARK 465 LYS G 129
REMARK 465 MET H -3
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 ALA H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 ARG H 26
REMARK 465 LYS H 27
REMARK 465 ARG H 28
REMARK 465 LYS H 122
REMARK 465 DT I -74
REMARK 465 DG I -73
REMARK 465 DT I -72
REMARK 465 DA J 72
REMARK 465 DC J 73
REMARK 465 DA J 74
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O2 DC I 42 N2 DG J -42 1.90
REMARK 500 O2 DC I 37 N2 DG J -37 2.08
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 DT J -19 O4' DT J -19 C4' 0.088
REMARK 500 DC J -18 O4' DC J -18 C4' 0.077
REMARK 500 DC J -8 O4' DC J -8 C4' 0.062
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 DG I -68 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC I -37 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG I -7 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DT I 21 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DT I 30 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DA I 62 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG I 68 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J -46 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT J -36 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J 6 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG J 14 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT J 16 O4' - C1' - N1 ANGL. DEV. = 2.2 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 ASP A 81 63.63 62.43
REMARK 500 LYS B 44 -61.88 -94.95
REMARK 500 PHE B 100 16.67 -140.48
REMARK 500 THR D 87 -169.82 -121.12
REMARK 500 THR H 87 -169.79 -121.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-4692 RELATED DB: EMDB
REMARK 900 HUMAN-D02 NUCLEOSOME CORE PARTICLE WITH BIOTIN-STREPTAVIDIN LABEL
DBREF 6R0C A 0 135 UNP P84243 H33_HUMAN 1 136
DBREF 6R0C B 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 6R0C C 0 129 UNP P0C0S8 H2A1_HUMAN 1 130
DBREF 6R0C D -3 122 UNP P62807 H2B1C_HUMAN 1 126
DBREF 6R0C E 0 135 UNP P84243 H33_HUMAN 1 136
DBREF 6R0C F 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 6R0C G 0 129 UNP P0C0S8 H2A1_HUMAN 1 130
DBREF 6R0C H -3 122 UNP P62807 H2B1C_HUMAN 1 126
DBREF 6R0C I -74 70 PDB 6R0C 6R0C -74 70
DBREF 6R0C J -70 74 PDB 6R0C 6R0C -70 74
SEQRES 1 A 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 A 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 A 136 ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO
SEQRES 4 A 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 A 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 A 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 A 136 PHE LYS THR ASP LEU ARG PHE GLN SER ALA ALA ILE GLY
SEQRES 8 A 136 ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 A 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 A 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 A 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 B 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 B 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 B 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 B 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 B 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 B 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 B 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 B 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 130 MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA
SEQRES 2 C 130 LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 3 C 130 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 4 C 130 TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 5 C 130 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 6 C 130 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 7 C 130 ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP
SEQRES 8 C 130 GLU GLU LEU ASN LYS LEU LEU GLY LYS VAL THR ILE ALA
SEQRES 9 C 130 GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU
SEQRES 10 C 130 PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS
SEQRES 1 D 126 MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS
SEQRES 2 D 126 GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP
SEQRES 3 D 126 GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER
SEQRES 4 D 126 VAL TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP
SEQRES 5 D 126 THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER
SEQRES 6 D 126 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA
SEQRES 7 D 126 SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR
SEQRES 8 D 126 SER ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO
SEQRES 9 D 126 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS
SEQRES 10 D 126 ALA VAL THR LYS TYR THR SER SER LYS
SEQRES 1 E 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 E 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 E 136 ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO
SEQRES 4 E 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 E 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 E 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 E 136 PHE LYS THR ASP LEU ARG PHE GLN SER ALA ALA ILE GLY
SEQRES 8 E 136 ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 E 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 E 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 E 136 ILE ARG GLY GLU ARG ALA
SEQRES 1 F 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 F 103 GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 F 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 F 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 F 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 F 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 F 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 F 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 130 MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA
SEQRES 2 G 130 LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 3 G 130 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 4 G 130 TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 5 G 130 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 6 G 130 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 7 G 130 ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP
SEQRES 8 G 130 GLU GLU LEU ASN LYS LEU LEU GLY LYS VAL THR ILE ALA
SEQRES 9 G 130 GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU
SEQRES 10 G 130 PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS
SEQRES 1 H 126 MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS
SEQRES 2 H 126 GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP
SEQRES 3 H 126 GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER
SEQRES 4 H 126 VAL TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP
SEQRES 5 H 126 THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER
SEQRES 6 H 126 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA
SEQRES 7 H 126 SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR
SEQRES 8 H 126 SER ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO
SEQRES 9 H 126 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS
SEQRES 10 H 126 ALA VAL THR LYS TYR THR SER SER LYS
SEQRES 1 I 145 DT DG DT DC DC DA DG DG DT DT DC DT DC
SEQRES 2 I 145 DC DC DT DG DT DG DG DT DG DA DA DA DA
SEQRES 3 I 145 DC DC DA DA DC DT DA DA DC DT DA DC DC
SEQRES 4 I 145 DT DT DC DC DC DA DG DG DA DA DA DC DA
SEQRES 5 I 145 DG DG DT DT DT DC DA DC DC DA DG DC DC
SEQRES 6 I 145 DA DG DG DC DC DT DT DG DA DA DT DG DC
SEQRES 7 I 145 DA DA DT DT DG DT DC DT DT DA DC DT DA
SEQRES 8 I 145 DG DG DA DA DT DA DT DT DT DG DG DA DC
SEQRES 9 I 145 DT DT DC DC DC DC DA DC DC DT DA DC DC
SEQRES 10 I 145 DA DT DT DC DA DG DG DT DA DA DC DT DT
SEQRES 11 I 145 DG DA DT DA DC DA DA DA DC DA DC DA DG
SEQRES 12 I 145 DC DC
SEQRES 1 J 145 DG DG DC DT DG DT DG DT DT DT DG DT DA
SEQRES 2 J 145 DT DC DA DA DG DT DT DA DC DC DT DG DA
SEQRES 3 J 145 DA DT DG DG DT DA DG DG DT DG DG DG DG
SEQRES 4 J 145 DA DA DG DT DC DC DA DA DA DT DA DT DT
SEQRES 5 J 145 DC DC DT DA DG DT DA DA DG DA DC DA DA
SEQRES 6 J 145 DT DT DG DC DA DT DT DC DA DA DG DG DC
SEQRES 7 J 145 DC DT DG DG DC DT DG DG DT DG DA DA DA
SEQRES 8 J 145 DC DC DT DG DT DT DT DC DC DT DG DG DG
SEQRES 9 J 145 DA DA DG DG DT DA DG DT DT DA DG DT DT
SEQRES 10 J 145 DG DG DT DT DT DT DC DA DC DC DA DC DA
SEQRES 11 J 145 DG DG DG DA DG DA DA DC DC DT DG DG DA
SEQRES 12 J 145 DC DA
HET MN A 201 1
HETNAM MN MANGANESE (II) ION
FORMUL 11 MN MN 2+
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 LYS A 79 1 17
HELIX 3 AA3 GLN A 85 ALA A 114 1 30
HELIX 4 AA4 MET A 120 GLY A 132 1 13
HELIX 5 AA5 ASN B 25 ILE B 29 5 5
HELIX 6 AA6 THR B 30 GLY B 42 1 13
HELIX 7 AA7 LEU B 49 ALA B 76 1 28
HELIX 8 AA8 THR B 82 GLY B 94 1 13
HELIX 9 AA9 ARG C 17 GLY C 22 1 6
HELIX 10 AB1 PRO C 26 LYS C 36 1 11
HELIX 11 AB2 GLY C 46 ASP C 72 1 27
HELIX 12 AB3 ILE C 79 ARG C 88 1 10
HELIX 13 AB4 ASP C 90 LEU C 97 1 8
HELIX 14 AB5 GLN C 112 LEU C 116 5 5
HELIX 15 AB6 TYR D 34 HIS D 46 1 13
HELIX 16 AB7 SER D 52 ASN D 81 1 30
HELIX 17 AB8 THR D 87 LEU D 99 1 13
HELIX 18 AB9 PRO D 100 SER D 121 1 22
HELIX 19 AC1 GLY E 44 SER E 57 1 14
HELIX 20 AC2 ARG E 63 LYS E 79 1 17
HELIX 21 AC3 GLN E 85 ALA E 114 1 30
HELIX 22 AC4 MET E 120 GLY E 132 1 13
HELIX 23 AC5 ASN F 25 ILE F 29 5 5
HELIX 24 AC6 THR F 30 GLY F 41 1 12
HELIX 25 AC7 LEU F 49 ALA F 76 1 28
HELIX 26 AC8 THR F 82 GLY F 94 1 13
HELIX 27 AC9 THR G 16 GLY G 22 1 7
HELIX 28 AD1 PRO G 26 LYS G 36 1 11
HELIX 29 AD2 GLY G 46 ASP G 72 1 27
HELIX 30 AD3 ILE G 79 ASP G 90 1 12
HELIX 31 AD4 GLU G 91 LEU G 97 1 7
HELIX 32 AD5 GLN G 112 LEU G 116 5 5
HELIX 33 AD6 TYR H 34 HIS H 46 1 13
HELIX 34 AD7 SER H 52 ASN H 81 1 30
HELIX 35 AD8 THR H 87 LEU H 99 1 13
HELIX 36 AD9 PRO H 100 SER H 121 1 22
SHEET 1 AA1 2 ARG A 83 PHE A 84 0
SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 AA2 2 THR A 118 ILE A 119 0
SHEET 2 AA2 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 AA3 2 THR B 96 LEU B 97 0
SHEET 2 AA3 2 VAL G 100 THR G 101 1 O THR G 101 N THR B 96
SHEET 1 AA4 2 ARG C 42 VAL C 43 0
SHEET 2 AA4 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 AA5 2 VAL C 100 THR C 101 0
SHEET 2 AA5 2 THR F 96 LEU F 97 1 O THR F 96 N THR C 101
SHEET 1 AA6 2 ARG E 83 PHE E 84 0
SHEET 2 AA6 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA7 2 THR E 118 ILE E 119 0
SHEET 2 AA7 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SITE 1 AC1 1 ASP A 77
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
(ATOM LINES ARE NOT SHOWN.)
END
