HEADER NUCLEAR PROTEIN 05-JUL-18 6DZT
TITLE CRYO-EM STRUCTURE OF NUCLEOSOME IN COMPLEX WITH A SINGLE CHAIN
TITLE 2 ANTIBODY FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3;
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;
COMPND 11 CHAIN: C, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H2B;
COMPND 15 CHAIN: D, H;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: DNA (147-MER);
COMPND 19 CHAIN: I;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: DNA (147-MER);
COMPND 23 CHAIN: J;
COMPND 24 ENGINEERED: YES;
COMPND 25 MOL_ID: 7;
COMPND 26 MOLECULE: SCFV;
COMPND 27 CHAIN: M, N;
COMPND 28 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: HIS3, HIS3:CG31613, CG31613, HIS3:CG33803, CG33803,
SOURCE 6 HIS3:CG33806, CG33806, HIS3:CG33809, CG33809, HIS3:CG33812, CG33812,
SOURCE 7 HIS3:CG33815, CG33815, HIS3:CG33818, CG33818, HIS3:CG33821, CG33821,
SOURCE 8 HIS3:CG33824, CG33824, HIS3:CG33827, CG33827, HIS3:CG33830, CG33830,
SOURCE 9 HIS3:CG33833, CG33833, HIS3:CG33836, CG33836, HIS3:CG33839, CG33839,
SOURCE 10 HIS3:CG33842, CG33842, HIS3:CG33845, CG33845, HIS3:CG33848, CG33848,
SOURCE 11 HIS3:CG33851, CG33851, HIS3:CG33854, CG33854, HIS3:CG33857, CG33857,
SOURCE 12 HIS3:CG33860, CG33860, HIS3:CG33863, CG33863, HIS3:CG33866, CG33866;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 2;
SOURCE 16 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 17 ORGANISM_COMMON: FRUIT FLY;
SOURCE 18 ORGANISM_TAXID: 7227;
SOURCE 19 GENE: HIS4, H4, HIS4R, H4R, CG3379, HIS4:CG31611, CG31611,
SOURCE 20 HIS4:CG33869, CG33869, HIS4:CG33871, CG33871, HIS4:CG33873, CG33873,
SOURCE 21 HIS4:CG33875, CG33875, HIS4:CG33877, CG33877, HIS4:CG33879, CG33879,
SOURCE 22 HIS4:CG33881, CG33881, HIS4:CG33883, CG33883, HIS4:CG33885, CG33885,
SOURCE 23 HIS4:CG33887, CG33887, HIS4:CG33889, CG33889, HIS4:CG33891, CG33891,
SOURCE 24 HIS4:CG33893, CG33893, HIS4:CG33895, CG33895, HIS4:CG33897, CG33897,
SOURCE 25 HIS4:CG33899, CG33899, HIS4:CG33901, CG33901, HIS4:CG33903, CG33903,
SOURCE 26 HIS4:CG33905, CG33905, HIS4:CG33907, CG33907, HIS4:CG33909, CG33909;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 29 MOL_ID: 3;
SOURCE 30 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 31 ORGANISM_COMMON: FRUIT FLY;
SOURCE 32 ORGANISM_TAXID: 7227;
SOURCE 33 GENE: HIS2A, H2A, HIS2A:CG31618, CG31618, HIS2A:CG33808, CG33808,
SOURCE 34 HIS2A:CG33814, CG33814, HIS2A:CG33817, CG33817, HIS2A:CG33820,
SOURCE 35 CG33820, HIS2A:CG33823, CG33823, HIS2A:CG33826, CG33826,
SOURCE 36 HIS2A:CG33829, CG33829, HIS2A:CG33832, CG33832, HIS2A:CG33835,
SOURCE 37 CG33835, HIS2A:CG33838, CG33838, HIS2A:CG33841, CG33841,
SOURCE 38 HIS2A:CG33844, CG33844, HIS2A:CG33847, CG33847, HIS2A:CG33850,
SOURCE 39 CG33850, HIS2A:CG33862, CG33862, HIS2A:CG33865, CG33865;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 42 MOL_ID: 4;
SOURCE 43 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 44 ORGANISM_COMMON: FRUIT FLY;
SOURCE 45 ORGANISM_TAXID: 7227;
SOURCE 46 GENE: HIS2B, HIS2B:CG17949, CG17949, HIS2B:CG33868, CG33868,
SOURCE 47 HIS2B:CG33870, CG33870, HIS2B:CG33872, CG33872, HIS2B:CG33874,
SOURCE 48 CG33874, HIS2B:CG33876, CG33876, HIS2B:CG33878, CG33878,
SOURCE 49 HIS2B:CG33880, CG33880, HIS2B:CG33882, CG33882, HIS2B:CG33884,
SOURCE 50 CG33884, HIS2B:CG33886, CG33886, HIS2B:CG33888, CG33888,
SOURCE 51 HIS2B:CG33890, CG33890, HIS2B:CG33892, CG33892, HIS2B:CG33894,
SOURCE 52 CG33894, HIS2B:CG33896, CG33896, HIS2B:CG33898, CG33898,
SOURCE 53 HIS2B:CG33900, CG33900, HIS2B:CG33902, CG33902, HIS2B:CG33904,
SOURCE 54 CG33904, HIS2B:CG33906, CG33906, HIS2B:CG33908, CG33908,
SOURCE 55 HIS2B:CG33910, CG33910;
SOURCE 56 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 57 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 58 MOL_ID: 5;
SOURCE 59 SYNTHETIC: YES;
SOURCE 60 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 61 ORGANISM_TAXID: 562;
SOURCE 62 MOL_ID: 6;
SOURCE 63 SYNTHETIC: YES;
SOURCE 64 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 65 ORGANISM_TAXID: 562;
SOURCE 66 MOL_ID: 7;
SOURCE 67 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 68 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 69 ORGANISM_TAXID: 10090;
SOURCE 70 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 71 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEOSOME, SINGLE CHAIN ANTIBODY, CHARGE-CHARGE INTERACTION, ACIDIC
KEYWDS 2 PATCH., NUCLEAR PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR K.N.S.YADAV,B.-R.ZHOU
REVDAT 6 18-DEC-19 6DZT 1 SCALE
REVDAT 5 04-DEC-19 6DZT 1 REMARK
REVDAT 4 20-NOV-19 6DZT 1 REMARK
REVDAT 3 19-JUN-19 6DZT 1 JRNL
REVDAT 2 12-JUN-19 6DZT 1 JRNL
REVDAT 1 22-MAY-19 6DZT 0
JRNL AUTH B.R.ZHOU,K.N.S.YADAV,M.BORGNIA,J.HONG,B.CAO,A.L.OLINS,
JRNL AUTH 2 D.E.OLINS,Y.BAI,P.ZHANG
JRNL TITL ATOMIC RESOLUTION CRYO-EM STRUCTURE OF A NATIVE-LIKE CENP-A
JRNL TITL 2 NUCLEOSOME AIDED BY AN ANTIBODY FRAGMENT.
JRNL REF NAT COMMUN V. 10 2301 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31127102
JRNL DOI 10.1038/S41467-019-10247-4
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
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) : 2.990
REMARK 3 NUMBER OF PARTICLES : 238790
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING ONLY
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6DZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235493.
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 : NUCLEOSOME-ANTIBODY COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : OTHER
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 40.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : NULL
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: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: M, N
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 ALA 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 ALA A 135
REMARK 465 MET B -1
REMARK 465 ILE B 0
REMARK 465 THR 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 GLY B 102
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLY C 3
REMARK 465 ARG C 4
REMARK 465 GLY C 5
REMARK 465 LYS C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 VAL C 10
REMARK 465 LYS C 11
REMARK 465 GLY C 12
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 LYS C 122
REMARK 465 LYS C 123
REMARK 465 ALA C 124
REMARK 465 MET D -1
REMARK 465 ILE D 0
REMARK 465 PRO D 1
REMARK 465 PRO D 2
REMARK 465 LYS D 3
REMARK 465 THR D 4
REMARK 465 SER D 5
REMARK 465 GLY D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 LYS D 10
REMARK 465 LYS D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 LYS D 14
REMARK 465 ALA D 15
REMARK 465 GLN D 16
REMARK 465 LYS D 17
REMARK 465 ASN D 18
REMARK 465 ILE D 19
REMARK 465 THR D 20
REMARK 465 LYS D 21
REMARK 465 THR D 22
REMARK 465 ASP D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 LYS D 26
REMARK 465 LYS D 27
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 ALA 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 ARG E 134
REMARK 465 ALA E 135
REMARK 465 MET F -1
REMARK 465 ILE F 0
REMARK 465 THR 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 GLY F 102
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLY G 3
REMARK 465 ARG G 4
REMARK 465 GLY G 5
REMARK 465 LYS G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 VAL G 10
REMARK 465 LYS G 11
REMARK 465 GLY G 12
REMARK 465 LYS G 13
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 LYS G 122
REMARK 465 LYS G 123
REMARK 465 ALA G 124
REMARK 465 MET H -1
REMARK 465 ILE H 0
REMARK 465 PRO H 1
REMARK 465 PRO H 2
REMARK 465 LYS H 3
REMARK 465 THR H 4
REMARK 465 SER H 5
REMARK 465 GLY H 6
REMARK 465 LYS H 7
REMARK 465 ALA H 8
REMARK 465 ALA H 9
REMARK 465 LYS H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 GLY H 13
REMARK 465 LYS H 14
REMARK 465 ALA H 15
REMARK 465 GLN H 16
REMARK 465 LYS H 17
REMARK 465 ASN H 18
REMARK 465 ILE H 19
REMARK 465 THR H 20
REMARK 465 LYS H 21
REMARK 465 THR H 22
REMARK 465 ASP H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 LYS H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 122
REMARK 465 MET M 3
REMARK 465 LYS M 4
REMARK 465 SER M 5
REMARK 465 SER M 6
REMARK 465 HIS M 7
REMARK 465 HIS M 8
REMARK 465 HIS M 9
REMARK 465 HIS M 10
REMARK 465 HIS M 11
REMARK 465 HIS M 12
REMARK 465 GLU M 13
REMARK 465 ASN M 14
REMARK 465 LEU M 15
REMARK 465 TYR M 16
REMARK 465 PHE M 17
REMARK 465 GLN M 18
REMARK 465 SER M 19
REMARK 465 ASN M 20
REMARK 465 ALA M 21
REMARK 465 MET M 22
REMARK 465 SER M 142
REMARK 465 GLY M 143
REMARK 465 GLY M 144
REMARK 465 GLY M 145
REMARK 465 GLY M 146
REMARK 465 SER M 147
REMARK 465 GLY M 148
REMARK 465 GLY M 149
REMARK 465 GLY M 150
REMARK 465 GLY M 151
REMARK 465 SER M 152
REMARK 465 GLY M 153
REMARK 465 GLY M 154
REMARK 465 GLY M 155
REMARK 465 GLY M 156
REMARK 465 SER M 157
REMARK 465 MET M 158
REMARK 465 ARG M 266
REMARK 465 ALA M 267
REMARK 465 MET N 3
REMARK 465 LYS N 4
REMARK 465 SER N 5
REMARK 465 SER N 6
REMARK 465 HIS N 7
REMARK 465 HIS N 8
REMARK 465 HIS N 9
REMARK 465 HIS N 10
REMARK 465 HIS N 11
REMARK 465 HIS N 12
REMARK 465 GLU N 13
REMARK 465 ASN N 14
REMARK 465 LEU N 15
REMARK 465 TYR N 16
REMARK 465 PHE N 17
REMARK 465 GLN N 18
REMARK 465 SER N 19
REMARK 465 ASN N 20
REMARK 465 ALA N 21
REMARK 465 MET N 22
REMARK 465 SER N 142
REMARK 465 GLY N 143
REMARK 465 GLY N 144
REMARK 465 GLY N 145
REMARK 465 GLY N 146
REMARK 465 SER N 147
REMARK 465 GLY N 148
REMARK 465 GLY N 149
REMARK 465 GLY N 150
REMARK 465 GLY N 151
REMARK 465 SER N 152
REMARK 465 GLY N 153
REMARK 465 GLY N 154
REMARK 465 GLY N 155
REMARK 465 GLY N 156
REMARK 465 SER N 157
REMARK 465 MET N 158
REMARK 465 ARG N 266
REMARK 465 ALA N 267
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 DA I 90 O3' DA I 90 C3' -0.040
REMARK 500 DG I 101 O3' DG I 101 C3' -0.037
REMARK 500 DC J 111 O3' DC J 111 C3' -0.037
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 DC I 49 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT I 58 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT J 112 O4' - C1' - N1 ANGL. DEV. = 1.8 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 LYS D 29 37.52 -146.02
REMARK 500 ARG D 30 68.74 60.79
REMARK 500 GLU D 32 73.08 61.96
REMARK 500 ARG H 30 71.18 61.29
REMARK 500 GLU H 32 70.97 61.74
REMARK 500 GLU M 111 49.47 -86.54
REMARK 500 ASP M 112 17.98 -143.07
REMARK 500 SER M 184 -62.56 -92.42
REMARK 500 ALA M 209 -8.30 66.66
REMARK 500 PRO N 75 0.29 -66.94
REMARK 500 GLU N 111 46.34 -87.42
REMARK 500 ASP N 112 10.01 -142.78
REMARK 500 ALA N 209 -9.93 67.08
REMARK 500 ASN N 234 -62.42 -95.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8938 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF NUCLEOSOME IN COMPLEX WITH A SINGLE CHAIN
REMARK 900 ANTIBODY FRAGMENT
REMARK 900 RELATED ID: EMD-8945 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-8949 RELATED DB: EMDB
DBREF 6DZT A 0 135 UNP P02299 H3_DROME 1 136
DBREF 6DZT B 1 102 UNP P84040 H4_DROME 2 103
DBREF 6DZT C 1 124 UNP P84051 H2A_DROME 1 124
DBREF 6DZT D 1 122 UNP P02283 H2B_DROME 2 123
DBREF 6DZT E 0 135 UNP P02299 H3_DROME 1 136
DBREF 6DZT F 1 102 UNP P84040 H4_DROME 2 103
DBREF 6DZT G 1 124 UNP P84051 H2A_DROME 1 124
DBREF 6DZT H 1 122 UNP P02283 H2B_DROME 2 123
DBREF 6DZT I 1 147 PDB 6DZT 6DZT 1 147
DBREF 6DZT J 1 147 PDB 6DZT 6DZT 1 147
DBREF 6DZT M 3 267 PDB 6DZT 6DZT 3 267
DBREF 6DZT N 3 267 PDB 6DZT 6DZT 3 267
SEQADV 6DZT MET B -1 UNP P84040 INITIATING METHIONINE
SEQADV 6DZT ILE B 0 UNP P84040 EXPRESSION TAG
SEQADV 6DZT MET D -1 UNP P02283 INITIATING METHIONINE
SEQADV 6DZT ILE D 0 UNP P02283 EXPRESSION TAG
SEQADV 6DZT MET F -1 UNP P84040 INITIATING METHIONINE
SEQADV 6DZT ILE F 0 UNP P84040 EXPRESSION TAG
SEQADV 6DZT MET H -1 UNP P02283 INITIATING METHIONINE
SEQADV 6DZT ILE H 0 UNP P02283 EXPRESSION TAG
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 ALA 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 SER ALA VAL MET
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 104 MET ILE THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY
SEQRES 2 B 104 LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP
SEQRES 3 B 104 ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU
SEQRES 4 B 104 ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE
SEQRES 5 B 104 TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU
SEQRES 6 B 104 ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA
SEQRES 7 B 104 LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA
SEQRES 8 B 104 LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 124 MET SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS
SEQRES 2 C 124 ALA LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 C 124 VAL GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 C 124 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 C 124 ALA VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU
SEQRES 6 C 124 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 C 124 ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU
SEQRES 8 C 124 GLU LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN
SEQRES 9 C 124 GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO
SEQRES 10 C 124 LYS LYS THR GLU LYS LYS ALA
SEQRES 1 D 124 MET ILE PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS
SEQRES 2 D 124 ALA GLY LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS
SEQRES 3 D 124 LYS LYS LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR
SEQRES 4 D 124 ILE TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY
SEQRES 5 D 124 ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL
SEQRES 6 D 124 ASN ASP ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG
SEQRES 7 D 124 LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG
SEQRES 8 D 124 GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU
SEQRES 9 D 124 LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL
SEQRES 10 D 124 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 ALA 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 SER ALA VAL MET
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 104 MET ILE THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY
SEQRES 2 F 104 LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP
SEQRES 3 F 104 ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU
SEQRES 4 F 104 ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE
SEQRES 5 F 104 TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU
SEQRES 6 F 104 ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA
SEQRES 7 F 104 LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA
SEQRES 8 F 104 LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 124 MET SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS
SEQRES 2 G 124 ALA LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 G 124 VAL GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 G 124 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 G 124 ALA VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU
SEQRES 6 G 124 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 G 124 ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU
SEQRES 8 G 124 GLU LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN
SEQRES 9 G 124 GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO
SEQRES 10 G 124 LYS LYS THR GLU LYS LYS ALA
SEQRES 1 H 124 MET ILE PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS
SEQRES 2 H 124 ALA GLY LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS
SEQRES 3 H 124 LYS LYS LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR
SEQRES 4 H 124 ILE TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY
SEQRES 5 H 124 ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL
SEQRES 6 H 124 ASN ASP ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG
SEQRES 7 H 124 LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG
SEQRES 8 H 124 GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU
SEQRES 9 H 124 LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL
SEQRES 10 H 124 THR LYS TYR THR SER SER LYS
SEQRES 1 I 147 DA DT DC DG DG DA DT DG DT DA DT DA DT
SEQRES 2 I 147 DA DT DC DT DG DA DC DA DC DG DT DG DC
SEQRES 3 I 147 DC DT DG DG DA DG DA DC DT DA DG DG DG
SEQRES 4 I 147 DA DG DT DA DA DT DC DC DC DC DT DT DG
SEQRES 5 I 147 DG DC DG DG DT DT DA DA DA DA DC DG DC
SEQRES 6 I 147 DG DG DG DG DG DA DC DA DG DC DG DC DG
SEQRES 7 I 147 DT DA DC DG DT DG DC DG DT DT DT DA DA
SEQRES 8 I 147 DG DC DG DG DT DG DC DT DA DG DA DG DC
SEQRES 9 I 147 DT DG DT DC DT DA DC DG DA DC DC DA DA
SEQRES 10 I 147 DT DT DG DA DG DC DG DG DC DC DT DC DG
SEQRES 11 I 147 DG DC DA DC DC DG DG DG DA DT DT DC DT
SEQRES 12 I 147 DC DG DA DT
SEQRES 1 J 147 DA DT DC DG DA DG DA DA DT DC DC DC DG
SEQRES 2 J 147 DG DT DG DC DC DG DA DG DG DC DC DG DC
SEQRES 3 J 147 DT DC DA DA DT DT DG DG DT DC DG DT DA
SEQRES 4 J 147 DG DA DC DA DG DC DT DC DT DA DG DC DA
SEQRES 5 J 147 DC DC DG DC DT DT DA DA DA DC DG DC DA
SEQRES 6 J 147 DC DG DT DA DC DG DC DG DC DT DG DT DC
SEQRES 7 J 147 DC DC DC DC DG DC DG DT DT DT DT DA DA
SEQRES 8 J 147 DC DC DG DC DC DA DA DG DG DG DG DA DT
SEQRES 9 J 147 DT DA DC DT DC DC DC DT DA DG DT DC DT
SEQRES 10 J 147 DC DC DA DG DG DC DA DC DG DT DG DT DC
SEQRES 11 J 147 DA DG DA DT DA DT DA DT DA DC DA DT DC
SEQRES 12 J 147 DC DG DA DT
SEQRES 1 M 265 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 M 265 TYR PHE GLN SER ASN ALA MET GLU VAL GLN LEU GLN GLN
SEQRES 3 M 265 SER GLY PRO GLU LEU VAL GLU PRO GLY THR SER VAL LYS
SEQRES 4 M 265 MET PRO CYS LYS ALA SER GLY TYR THR PHE THR SER TYR
SEQRES 5 M 265 THR ILE GLN TRP VAL LYS GLN THR PRO ARG GLN GLY LEU
SEQRES 6 M 265 GLU TRP ILE GLY TYR ILE TYR PRO TYR ASN ALA GLY THR
SEQRES 7 M 265 LYS TYR ASN GLU LYS PHE LYS GLY LYS ALA THR LEU THR
SEQRES 8 M 265 SER ASP LYS SER SER SER THR VAL TYR MET GLU LEU SER
SEQRES 9 M 265 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA
SEQRES 10 M 265 ARG LYS SER SER ARG LEU ARG SER THR LEU ASP TYR TRP
SEQRES 11 M 265 GLY GLN GLY THR SER VAL THR VAL SER SER GLY GLY GLY
SEQRES 12 M 265 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER MET
SEQRES 13 M 265 ASP ILE LYS MET THR GLN SER PRO SER SER MET HIS ALA
SEQRES 14 M 265 SER LEU GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES 15 M 265 GLN ASP ILE ARG SER TYR LEU SER TRP TYR GLN GLN LYS
SEQRES 16 M 265 PRO TRP LYS SER PRO LYS THR LEU ILE TYR TYR ALA THR
SEQRES 17 M 265 SER LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 18 M 265 GLY SER GLY GLN ASP PHE SER LEU THR ILE ASN ASN LEU
SEQRES 19 M 265 GLU SER ASP ASP THR ALA THR TYR TYR CYS LEU GLN HIS
SEQRES 20 M 265 GLY GLU SER PRO TYR THR PHE GLY SER GLY THR LYS LEU
SEQRES 21 M 265 GLU ILE LYS ARG ALA
SEQRES 1 N 265 MET LYS SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU
SEQRES 2 N 265 TYR PHE GLN SER ASN ALA MET GLU VAL GLN LEU GLN GLN
SEQRES 3 N 265 SER GLY PRO GLU LEU VAL GLU PRO GLY THR SER VAL LYS
SEQRES 4 N 265 MET PRO CYS LYS ALA SER GLY TYR THR PHE THR SER TYR
SEQRES 5 N 265 THR ILE GLN TRP VAL LYS GLN THR PRO ARG GLN GLY LEU
SEQRES 6 N 265 GLU TRP ILE GLY TYR ILE TYR PRO TYR ASN ALA GLY THR
SEQRES 7 N 265 LYS TYR ASN GLU LYS PHE LYS GLY LYS ALA THR LEU THR
SEQRES 8 N 265 SER ASP LYS SER SER SER THR VAL TYR MET GLU LEU SER
SEQRES 9 N 265 SER LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA
SEQRES 10 N 265 ARG LYS SER SER ARG LEU ARG SER THR LEU ASP TYR TRP
SEQRES 11 N 265 GLY GLN GLY THR SER VAL THR VAL SER SER GLY GLY GLY
SEQRES 12 N 265 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER MET
SEQRES 13 N 265 ASP ILE LYS MET THR GLN SER PRO SER SER MET HIS ALA
SEQRES 14 N 265 SER LEU GLY GLU ARG VAL THR ILE THR CYS LYS ALA SER
SEQRES 15 N 265 GLN ASP ILE ARG SER TYR LEU SER TRP TYR GLN GLN LYS
SEQRES 16 N 265 PRO TRP LYS SER PRO LYS THR LEU ILE TYR TYR ALA THR
SEQRES 17 N 265 SER LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 18 N 265 GLY SER GLY GLN ASP PHE SER LEU THR ILE ASN ASN LEU
SEQRES 19 N 265 GLU SER ASP ASP THR ALA THR TYR TYR CYS LEU GLN HIS
SEQRES 20 N 265 GLY GLU SER PRO TYR THR PHE GLY SER GLY THR LYS LEU
SEQRES 21 N 265 GLU ILE LYS ARG ALA
HELIX 1 AA1 GLY A 44 GLN A 55 1 12
HELIX 2 AA2 ARG A 63 ALA A 75 1 13
HELIX 3 AA3 GLN A 76 PHE A 78 5 3
HELIX 4 AA4 GLN A 85 ALA A 114 1 30
HELIX 5 AA5 MET A 120 ARG A 131 1 12
HELIX 6 AA6 ASN B 25 ILE B 29 5 5
HELIX 7 AA7 THR B 30 GLY B 41 1 12
HELIX 8 AA8 LEU B 49 ALA B 76 1 28
HELIX 9 AA9 THR B 82 ARG B 92 1 11
HELIX 10 AB1 SER C 16 GLY C 22 1 7
HELIX 11 AB2 PRO C 26 LYS C 36 1 11
HELIX 12 AB3 GLY C 46 ASN C 73 1 28
HELIX 13 AB4 ILE C 79 ASN C 89 1 11
HELIX 14 AB5 ASP C 90 LEU C 97 1 8
HELIX 15 AB6 GLN C 112 LEU C 116 5 5
HELIX 16 AB7 TYR D 34 HIS D 46 1 13
HELIX 17 AB8 SER D 52 ASN D 81 1 30
HELIX 18 AB9 THR D 87 LEU D 99 1 13
HELIX 19 AC1 GLU D 102 THR D 119 1 18
HELIX 20 AC2 GLY E 44 GLN E 55 1 12
HELIX 21 AC3 ARG E 63 ALA E 75 1 13
HELIX 22 AC4 GLN E 76 PHE E 78 5 3
HELIX 23 AC5 GLN E 85 ALA E 114 1 30
HELIX 24 AC6 MET E 120 GLY E 132 1 13
HELIX 25 AC7 ASN F 25 ILE F 29 5 5
HELIX 26 AC8 THR F 30 GLY F 41 1 12
HELIX 27 AC9 LEU F 49 ALA F 76 1 28
HELIX 28 AD1 THR F 82 ARG F 92 1 11
HELIX 29 AD2 SER G 16 GLY G 22 1 7
HELIX 30 AD3 PRO G 26 LYS G 36 1 11
HELIX 31 AD4 GLY G 46 ASN G 73 1 28
HELIX 32 AD5 ILE G 79 ASN G 89 1 11
HELIX 33 AD6 ASP G 90 LEU G 97 1 8
HELIX 34 AD7 GLN G 112 LEU G 116 5 5
HELIX 35 AD8 TYR H 34 HIS H 46 1 13
HELIX 36 AD9 SER H 52 ASN H 81 1 30
HELIX 37 AE1 THR H 87 LEU H 99 1 13
HELIX 38 AE2 GLU H 102 SER H 120 1 19
HELIX 39 AE3 THR M 50 THR M 52 5 3
HELIX 40 AE4 THR N 50 THR N 52 5 3
HELIX 41 AE5 GLU N 84 LYS N 87 5 4
HELIX 42 AE6 GLU N 237 THR N 241 5 5
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 TYR B 98 0
SHEET 2 AA3 2 VAL G 100 ILE G 102 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 ARG C 77 ILE C 78 0
SHEET 2 AA5 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 78
SHEET 1 AA6 2 VAL C 100 ILE C 102 0
SHEET 2 AA6 2 THR F 96 TYR F 98 1 O THR F 96 N THR C 101
SHEET 1 AA7 2 ARG E 83 PHE E 84 0
SHEET 2 AA7 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA8 2 THR E 118 ILE E 119 0
SHEET 2 AA8 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA9 2 ARG G 42 VAL G 43 0
SHEET 2 AA9 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 AB1 2 ARG G 77 ILE G 78 0
SHEET 2 AB1 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
SHEET 1 AB2 4 GLN M 25 GLN M 28 0
SHEET 2 AB2 4 VAL M 40 SER M 47 -1 O SER M 47 N GLN M 25
SHEET 3 AB2 4 THR M 100 LEU M 105 -1 O MET M 103 N MET M 42
SHEET 4 AB2 4 ALA M 90 ASP M 95 -1 N THR M 93 O TYR M 102
SHEET 1 AB3 6 GLU M 32 VAL M 34 0
SHEET 2 AB3 6 THR M 136 VAL M 140 1 O THR M 139 N VAL M 34
SHEET 3 AB3 6 ALA M 114 SER M 122 -1 N ALA M 114 O VAL M 138
SHEET 4 AB3 6 TYR M 54 THR M 62 -1 N VAL M 59 O TYR M 117
SHEET 5 AB3 6 GLY M 66 TYR M 74 -1 O ILE M 70 N TRP M 58
SHEET 6 AB3 6 GLY M 79 TYR M 82 -1 O GLY M 79 N TYR M 74
SHEET 1 AB4 4 GLU M 32 VAL M 34 0
SHEET 2 AB4 4 THR M 136 VAL M 140 1 O THR M 139 N VAL M 34
SHEET 3 AB4 4 ALA M 114 SER M 122 -1 N ALA M 114 O VAL M 138
SHEET 4 AB4 4 LEU M 129 TRP M 132 -1 O TYR M 131 N ARG M 120
SHEET 1 AB5 4 THR M 163 GLN M 164 0
SHEET 2 AB5 4 VAL M 177 LYS M 182 -1 O LYS M 182 N THR M 163
SHEET 3 AB5 4 PHE M 229 ILE M 233 -1 O LEU M 231 N ILE M 179
SHEET 4 AB5 4 PHE M 220 GLY M 224 -1 N SER M 223 O SER M 230
SHEET 1 AB6 2 SER M 168 ALA M 171 0
SHEET 2 AB6 2 LYS M 261 ILE M 264 1 O LYS M 261 N MET M 169
SHEET 1 AB7 4 SER M 211 LEU M 212 0
SHEET 2 AB7 4 LYS M 203 TYR M 207 -1 N TYR M 207 O SER M 211
SHEET 3 AB7 4 LEU M 191 GLN M 196 -1 N GLN M 195 O LYS M 203
SHEET 4 AB7 4 THR M 243 GLN M 248 -1 O LEU M 247 N SER M 192
SHEET 1 AB8 2 GLN N 25 LEU N 26 0
SHEET 2 AB8 2 ALA N 46 SER N 47 -1 O SER N 47 N GLN N 25
SHEET 1 AB9 6 GLU N 32 LEU N 33 0
SHEET 2 AB9 6 THR N 136 THR N 139 1 O SER N 137 N GLU N 32
SHEET 3 AB9 6 VAL N 115 SER N 122 -1 N TYR N 116 O THR N 136
SHEET 4 AB9 6 TYR N 54 THR N 62 -1 N GLN N 57 O ALA N 119
SHEET 5 AB9 6 GLY N 66 TYR N 74 -1 O GLU N 68 N LYS N 60
SHEET 6 AB9 6 GLY N 79 TYR N 82 -1 O LYS N 81 N TYR N 72
SHEET 1 AC1 4 GLU N 32 LEU N 33 0
SHEET 2 AC1 4 THR N 136 THR N 139 1 O SER N 137 N GLU N 32
SHEET 3 AC1 4 VAL N 115 SER N 122 -1 N TYR N 116 O THR N 136
SHEET 4 AC1 4 LEU N 129 TRP N 132 -1 O TYR N 131 N ARG N 120
SHEET 1 AC2 3 VAL N 40 PRO N 43 0
SHEET 2 AC2 3 THR N 100 LEU N 105 -1 O MET N 103 N MET N 42
SHEET 3 AC2 3 ALA N 90 ASP N 95 -1 N THR N 91 O GLU N 104
SHEET 1 AC3 4 THR N 163 GLN N 164 0
SHEET 2 AC3 4 VAL N 177 LYS N 182 -1 O LYS N 182 N THR N 163
SHEET 3 AC3 4 ASP N 228 ILE N 233 -1 O LEU N 231 N ILE N 179
SHEET 4 AC3 4 SER N 221 SER N 225 -1 N SER N 221 O THR N 232
SHEET 1 AC4 2 SER N 168 ALA N 171 0
SHEET 2 AC4 2 LYS N 261 ILE N 264 1 O GLU N 263 N MET N 169
SHEET 1 AC5 5 SER N 211 LEU N 212 0
SHEET 2 AC5 5 LYS N 203 TYR N 207 -1 N TYR N 207 O SER N 211
SHEET 3 AC5 5 LEU N 191 GLN N 196 -1 N TRP N 193 O LEU N 205
SHEET 4 AC5 5 THR N 243 GLN N 248 -1 O LEU N 247 N SER N 192
SHEET 5 AC5 5 THR N 255 PHE N 256 -1 O THR N 255 N GLN N 248
SSBOND 1 CYS M 44 CYS M 118 1555 1555 2.02
SSBOND 2 CYS M 181 CYS M 246 1555 1555 2.03
SSBOND 3 CYS N 44 CYS N 118 1555 1555 2.03
SSBOND 4 CYS N 181 CYS N 246 1555 1555 2.03
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
