HEADER GENE REGULATION 24-JUL-19 6PX3
TITLE SET2 BOUND TO NUCLEOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H4;
COMPND 8 CHAIN: B, F;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: UBIQUITIN-60S RIBOSOMAL PROTEIN L40,HISTONE H2A;
COMPND 12 CHAIN: C, G;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: HISTONE H2B 1.1;
COMPND 16 CHAIN: D, H;
COMPND 17 SYNONYM: H2B1.1;
COMPND 18 ENGINEERED: YES;
COMPND 19 MUTATION: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: DNA (145-MER);
COMPND 22 CHAIN: I;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: DNA (145-MER);
COMPND 26 CHAIN: J;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 7;
COMPND 29 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE;
COMPND 30 CHAIN: S;
COMPND 31 EC: 2.1.1.43;
COMPND 32 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: XELAEV_18002543MG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 10 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 11 ORGANISM_TAXID: 8355;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 16 S288C), XENOPUS LAEVIS;
SOURCE 17 ORGANISM_COMMON: BAKER'S YEAST, AFRICAN CLAWED FROG;
SOURCE 18 ORGANISM_TAXID: 559292, 8355;
SOURCE 19 STRAIN: ATCC 204508 / S288C;
SOURCE 20 GENE: RPL40B, UBI2, YKR094C, HIST1H2AJ, LOC494591,
SOURCE 21 XELAEV_18003602MG;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 MOL_ID: 4;
SOURCE 25 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 26 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 27 ORGANISM_TAXID: 8355;
SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 30 MOL_ID: 5;
SOURCE 31 SYNTHETIC: YES;
SOURCE 32 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 33 ORGANISM_TAXID: 32630;
SOURCE 34 MOL_ID: 6;
SOURCE 35 SYNTHETIC: YES;
SOURCE 36 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 37 ORGANISM_TAXID: 32630;
SOURCE 38 MOL_ID: 7;
SOURCE 39 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS
SOURCE 40 144.50 / IMI 039719);
SOURCE 41 ORGANISM_TAXID: 759272;
SOURCE 42 STRAIN: DSM 1495 / CBS 144.50 / IMI 039719;
SOURCE 43 GENE: CTHT_0025760;
SOURCE 44 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 45 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SET2, NUCLEOSOME, CHROMATIN, KMT, GENE REGULATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.HALIC,S.BILOKAPIC
REVDAT 2 04-SEP-19 6PX3 1 JRNL
REVDAT 1 28-AUG-19 6PX3 0
JRNL AUTH S.BILOKAPIC,M.HALIC
JRNL TITL NUCLEOSOME AND UBIQUITIN POSITION SET2 TO METHYLATE H3K36.
JRNL REF NAT COMMUN V. 10 3795 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31439846
JRNL DOI 10.1038/S41467-019-11726-4
REMARK 2
REMARK 2 RESOLUTION. 4.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
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) : 4.100
REMARK 3 NUMBER OF PARTICLES : 67000
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 6PX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1000243219.
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 : SET2 BOUND TO UBIQUITINATED
REMARK 245 NUCLEOSOME; HISTONE-LYSINE N-
REMARK 245 METHYLTRANSFERASE; DNA; HISTONE
REMARK 245 H3, HISTONE H4, UBIQUITIN-60S
REMARK 245 RIBOSOMAL PROTEIN L40,HISTONE
REMARK 245 H2A, HISTONE H2B 1.1
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 : 7.50
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 BASE (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 : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 75.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
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: UNDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: S
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 MET A 36
REMARK 465 LYS A 37
REMARK 465 ARG A 134
REMARK 465 ALA A 135
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 LYS B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 GLY B 101
REMARK 465 GLY B 102
REMARK 465 MET C -91
REMARK 465 ASP C -90
REMARK 465 SER C -89
REMARK 465 PRO C -88
REMARK 465 ASP C -87
REMARK 465 LEU C -86
REMARK 465 HIS C -85
REMARK 465 HIS C -84
REMARK 465 HIS C -83
REMARK 465 HIS C -82
REMARK 465 HIS C -81
REMARK 465 HIS C -80
REMARK 465 GLY C -79
REMARK 465 THR C -78
REMARK 465 LEU C -77
REMARK 465 VAL C -76
REMARK 465 PRO C -75
REMARK 465 ARG C -74
REMARK 465 GLY C -73
REMARK 465 SER C -72
REMARK 465 THR C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 SER C 9
REMARK 465 GLY C 10
REMARK 465 GLY C 11
REMARK 465 SER C 12
REMARK 465 GLY C 13
REMARK 465 GLY C 14
REMARK 465 SER C 15
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 SER C 123
REMARK 465 LYS C 124
REMARK 465 SER C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 SER C 128
REMARK 465 LYS C 129
REMARK 465 MET 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 THR 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 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 ALA E 135
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 GLY F 102
REMARK 465 MET G -91
REMARK 465 ASP G -90
REMARK 465 SER G -89
REMARK 465 PRO G -88
REMARK 465 ASP G -87
REMARK 465 LEU G -86
REMARK 465 HIS G -85
REMARK 465 HIS G -84
REMARK 465 HIS G -83
REMARK 465 HIS G -82
REMARK 465 HIS G -81
REMARK 465 HIS G -80
REMARK 465 GLY G -79
REMARK 465 THR G -78
REMARK 465 LEU G -77
REMARK 465 VAL G -76
REMARK 465 PRO G -75
REMARK 465 ARG G -74
REMARK 465 GLY G -73
REMARK 465 SER G -72
REMARK 465 MET G -71
REMARK 465 GLN G -70
REMARK 465 ILE G -69
REMARK 465 PHE G -68
REMARK 465 VAL G -67
REMARK 465 LYS G -66
REMARK 465 THR G -65
REMARK 465 LEU G -64
REMARK 465 THR G -63
REMARK 465 GLY G -62
REMARK 465 LYS G -61
REMARK 465 THR G -60
REMARK 465 ILE G -59
REMARK 465 THR G -58
REMARK 465 LEU G -57
REMARK 465 GLU G -56
REMARK 465 VAL G -55
REMARK 465 GLU G -54
REMARK 465 SER G -53
REMARK 465 SER G -52
REMARK 465 ASP G -51
REMARK 465 THR G -50
REMARK 465 ILE G -49
REMARK 465 ASP G -48
REMARK 465 ASN G -47
REMARK 465 VAL G -46
REMARK 465 LYS G -45
REMARK 465 SER G -44
REMARK 465 LYS G -43
REMARK 465 ILE G -42
REMARK 465 GLN G -41
REMARK 465 ASP G -40
REMARK 465 LYS G -39
REMARK 465 GLU G -38
REMARK 465 GLY G -37
REMARK 465 ILE G -36
REMARK 465 PRO G -35
REMARK 465 PRO G -34
REMARK 465 ASP G -33
REMARK 465 GLN G -32
REMARK 465 GLN G -31
REMARK 465 ARG G -30
REMARK 465 LEU G -29
REMARK 465 ILE G -28
REMARK 465 PHE G -27
REMARK 465 ALA G -26
REMARK 465 GLY G -25
REMARK 465 LYS G -24
REMARK 465 GLN G -23
REMARK 465 LEU G -22
REMARK 465 GLU G -21
REMARK 465 ASP G -20
REMARK 465 GLY G -19
REMARK 465 ARG G -18
REMARK 465 THR G -17
REMARK 465 LEU G -16
REMARK 465 SER G -15
REMARK 465 ASP G -14
REMARK 465 TYR G -13
REMARK 465 ASN G -12
REMARK 465 ILE G -11
REMARK 465 GLN G -10
REMARK 465 LYS G -9
REMARK 465 GLU G -8
REMARK 465 SER G -7
REMARK 465 THR G -6
REMARK 465 LEU G -5
REMARK 465 HIS G -4
REMARK 465 LEU G -3
REMARK 465 VAL G -2
REMARK 465 LEU G -1
REMARK 465 ARG G 0
REMARK 465 LEU G 1
REMARK 465 ARG G 2
REMARK 465 GLY G 3
REMARK 465 THR G 4
REMARK 465 SER G 5
REMARK 465 SER G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 SER G 9
REMARK 465 GLY G 10
REMARK 465 GLY G 11
REMARK 465 SER G 12
REMARK 465 GLY G 13
REMARK 465 GLY G 14
REMARK 465 SER G 15
REMARK 465 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 SER G 123
REMARK 465 LYS G 124
REMARK 465 SER G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 SER G 128
REMARK 465 LYS G 129
REMARK 465 MET 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 THR 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 ALA H 121
REMARK 465 LYS H 122
REMARK 465 DC I 1
REMARK 465 DT I 147
REMARK 465 DG I 148
REMARK 465 DC I 149
REMARK 465 DG J -1
REMARK 465 DC J 0
REMARK 465 DA J 1
REMARK 465 DG J 147
REMARK 465 MET S 1
REMARK 465 GLU S 2
REMARK 465 ALA S 3
REMARK 465 SER S 4
REMARK 465 ASP S 5
REMARK 465 ARG S 6
REMARK 465 ALA S 7
REMARK 465 SER S 8
REMARK 465 GLY S 9
REMARK 465 PRO S 10
REMARK 465 THR S 11
REMARK 465 ALA S 12
REMARK 465 GLY S 13
REMARK 465 SER S 14
REMARK 465 LYS S 15
REMARK 465 SER S 16
REMARK 465 GLU S 17
REMARK 465 GLU S 18
REMARK 465 ARG S 19
REMARK 465 THR S 20
REMARK 465 LYS S 21
REMARK 465 GLN S 22
REMARK 465 ASN S 23
REMARK 465 GLY S 24
REMARK 465 PRO S 25
REMARK 465 ARG S 26
REMARK 465 SER S 27
REMARK 465 LYS S 28
REMARK 465 LYS S 29
REMARK 465 GLU S 30
REMARK 465 ASP S 31
REMARK 465 ALA S 32
REMARK 465 SER S 33
REMARK 465 ASP S 34
REMARK 465 SER S 35
REMARK 465 SER S 36
REMARK 465 THR S 37
REMARK 465 SER S 38
REMARK 465 THR S 39
REMARK 465 GLY S 40
REMARK 465 SER S 41
REMARK 465 LYS S 42
REMARK 465 SER S 43
REMARK 465 ALA S 44
REMARK 465 SER S 45
REMARK 465 ARG S 46
REMARK 465 SER S 47
REMARK 465 SER S 48
REMARK 465 SER S 49
REMARK 465 ALA S 50
REMARK 465 THR S 51
REMARK 465 THR S 52
REMARK 465 MET S 53
REMARK 465 SER S 54
REMARK 465 PRO S 55
REMARK 465 ASP S 56
REMARK 465 ASP S 57
REMARK 465 ALA S 58
REMARK 465 LYS S 59
REMARK 465 PRO S 60
REMARK 465 ALA S 61
REMARK 465 ASP S 62
REMARK 465 ASP S 63
REMARK 465 SER S 64
REMARK 465 ALA S 65
REMARK 465 LEU S 66
REMARK 465 ALA S 67
REMARK 465 GLN S 68
REMARK 465 GLU S 69
REMARK 465 ASN S 70
REMARK 465 GLY S 71
REMARK 465 VAL S 72
REMARK 465 ALA S 73
REMARK 465 PRO S 74
REMARK 465 LYS S 75
REMARK 465 PRO S 76
REMARK 465 SER S 77
REMARK 465 ARG S 78
REMARK 465 LYS S 79
REMARK 465 PRO S 85
REMARK 465 ARG S 86
REMARK 465 ASN S 87
REMARK 465 HIS S 94
REMARK 465 LEU S 95
REMARK 465 PRO S 96
REMARK 465 ASP S 97
REMARK 465 ALA S 98
REMARK 465 THR S 99
REMARK 465 GLU S 100
REMARK 465 ASN S 118
REMARK 465 MET S 119
REMARK 465 GLY S 120
REMARK 465 GLU S 326
REMARK 465 ARG S 327
REMARK 465 ALA S 328
REMARK 465 THR S 329
REMARK 465 LYS S 330
REMARK 465 LEU S 331
REMARK 465 PRO S 332
REMARK 465 LEU S 333
REMARK 465 ALA S 334
REMARK 465 THR S 335
REMARK 465 ILE S 336
REMARK 465 GLU S 337
REMARK 465 ALA S 338
REMARK 465 LEU S 339
REMARK 465 GLY S 340
REMARK 465 ILE S 341
REMARK 465 GLU S 342
REMARK 465 ASP S 343
REMARK 465 GLY S 344
REMARK 465 ASP S 345
REMARK 465 SER S 346
REMARK 465 TRP S 347
REMARK 465 ASP S 348
REMARK 465 THR S 349
REMARK 465 THR S 350
REMARK 465 VAL S 351
REMARK 465 ALA S 352
REMARK 465 LYS S 353
REMARK 465 LYS S 354
REMARK 465 PRO S 355
REMARK 465 ARG S 356
REMARK 465 LYS S 357
REMARK 465 LYS S 358
REMARK 465 LYS S 359
REMARK 465 ALA S 360
REMARK 465 SER S 361
REMARK 465 GLU S 362
REMARK 465 THR S 363
REMARK 465 ASP S 364
REMARK 465 GLU S 365
REMARK 465 GLU S 366
REMARK 465 TYR S 367
REMARK 465 VAL S 368
REMARK 465 ASN S 369
REMARK 465 SER S 370
REMARK 465 LEU S 371
REMARK 465 GLN S 372
REMARK 465 PRO S 373
REMARK 465 LYS S 374
REMARK 465 ALA S 375
REMARK 465 LEU S 376
REMARK 465 ASP S 377
REMARK 465 GLU S 378
REMARK 465 ASP S 379
REMARK 465 GLY S 380
REMARK 465 VAL S 381
REMARK 465 ASN S 382
REMARK 465 LYS S 383
REMARK 465 VAL S 384
REMARK 465 MET S 385
REMARK 465 ALA S 386
REMARK 465 THR S 387
REMARK 465 LEU S 388
REMARK 465 MET S 389
REMARK 465 GLN S 390
REMARK 465 CYS S 391
REMARK 465 LYS S 392
REMARK 465 GLU S 393
REMARK 465 LYS S 394
REMARK 465 TRP S 395
REMARK 465 ILE S 396
REMARK 465 ALA S 397
REMARK 465 VAL S 398
REMARK 465 LYS S 399
REMARK 465 LEU S 400
REMARK 465 LEU S 401
REMARK 465 SER S 402
REMARK 465 ARG S 403
REMARK 465 LEU S 404
REMARK 465 GLN S 405
REMARK 465 ALA S 406
REMARK 465 THR S 407
REMARK 465 GLN S 408
REMARK 465 ASP S 409
REMARK 465 ASP S 410
REMARK 465 HIS S 411
REMARK 465 LEU S 412
REMARK 465 ARG S 413
REMARK 465 HIS S 414
REMARK 465 ARG S 415
REMARK 465 VAL S 416
REMARK 465 VAL S 417
REMARK 465 ARG S 418
REMARK 465 MET S 419
REMARK 465 HIS S 420
REMARK 465 GLY S 421
REMARK 465 TYR S 422
REMARK 465 GLN S 423
REMARK 465 ILE S 424
REMARK 465 LEU S 425
REMARK 465 LYS S 426
REMARK 465 SER S 427
REMARK 465 THR S 428
REMARK 465 LEU S 429
REMARK 465 ASN S 430
REMARK 465 ALA S 431
REMARK 465 PHE S 432
REMARK 465 LYS S 433
REMARK 465 HIS S 434
REMARK 465 ASP S 435
REMARK 465 ASN S 436
REMARK 465 ASN S 437
REMARK 465 VAL S 438
REMARK 465 VAL S 439
REMARK 465 LEU S 440
REMARK 465 GLN S 441
REMARK 465 VAL S 442
REMARK 465 LEU S 443
REMARK 465 ASP S 444
REMARK 465 ILE S 445
REMARK 465 LEU S 446
REMARK 465 TYR S 447
REMARK 465 ASN S 448
REMARK 465 LEU S 449
REMARK 465 PRO S 450
REMARK 465 ARG S 451
REMARK 465 ILE S 452
REMARK 465 THR S 453
REMARK 465 LYS S 454
REMARK 465 ASN S 455
REMARK 465 LYS S 456
REMARK 465 ILE S 457
REMARK 465 SER S 458
REMARK 465 ASP S 459
REMARK 465 SER S 460
REMARK 465 ASN S 461
REMARK 465 ILE S 462
REMARK 465 GLU S 463
REMARK 465 ALA S 464
REMARK 465 VAL S 465
REMARK 465 VAL S 466
REMARK 465 GLN S 467
REMARK 465 PRO S 468
REMARK 465 LEU S 469
REMARK 465 ALA S 470
REMARK 465 SER S 471
REMARK 465 SER S 472
REMARK 465 SER S 473
REMARK 465 ASP S 474
REMARK 465 GLU S 475
REMARK 465 ARG S 476
REMARK 465 VAL S 477
REMARK 465 ALA S 478
REMARK 465 PHE S 479
REMARK 465 GLU S 480
REMARK 465 ALA S 481
REMARK 465 LYS S 482
REMARK 465 ARG S 483
REMARK 465 LEU S 484
REMARK 465 LEU S 485
REMARK 465 GLU S 486
REMARK 465 GLU S 487
REMARK 465 TRP S 488
REMARK 465 ASP S 489
REMARK 465 LYS S 490
REMARK 465 LEU S 491
REMARK 465 GLU S 492
REMARK 465 THR S 493
REMARK 465 ALA S 494
REMARK 465 TYR S 495
REMARK 465 ARG S 496
REMARK 465 ILE S 497
REMARK 465 PRO S 498
REMARK 465 ARG S 499
REMARK 465 LYS S 500
REMARK 465 LYS S 501
REMARK 465 ASP S 502
REMARK 465 GLY S 503
REMARK 465 ARG S 504
REMARK 465 VAL S 505
REMARK 465 VAL S 506
REMARK 465 SER S 507
REMARK 465 ALA S 508
REMARK 465 ILE S 509
REMARK 465 ALA S 510
REMARK 465 ASN S 511
REMARK 465 SER S 512
REMARK 465 PHE S 513
REMARK 465 GLU S 514
REMARK 465 GLU S 515
REMARK 465 GLU S 516
REMARK 465 ARG S 517
REMARK 465 ARG S 518
REMARK 465 SER S 519
REMARK 465 ASN S 520
REMARK 465 ARG S 521
REMARK 465 GLU S 522
REMARK 465 GLU S 523
REMARK 465 PRO S 524
REMARK 465 THR S 525
REMARK 465 LYS S 526
REMARK 465 PRO S 527
REMARK 465 ALA S 528
REMARK 465 ASP S 529
REMARK 465 PRO S 530
REMARK 465 LEU S 531
REMARK 465 ALA S 532
REMARK 465 ASN S 533
REMARK 465 VAL S 534
REMARK 465 VAL S 535
REMARK 465 ILE S 536
REMARK 465 PRO S 537
REMARK 465 THR S 538
REMARK 465 GLY S 539
REMARK 465 PRO S 540
REMARK 465 ARG S 541
REMARK 465 SER S 542
REMARK 465 ASN S 543
REMARK 465 ILE S 544
REMARK 465 PRO S 545
REMARK 465 GLN S 546
REMARK 465 ARG S 547
REMARK 465 ASN S 548
REMARK 465 ALA S 549
REMARK 465 ASN S 550
REMARK 465 TYR S 551
REMARK 465 TYR S 552
REMARK 465 ASN S 553
REMARK 465 GLY S 554
REMARK 465 VAL S 555
REMARK 465 ARG S 556
REMARK 465 PRO S 557
REMARK 465 ARG S 558
REMARK 465 LYS S 559
REMARK 465 PRO S 560
REMARK 465 PRO S 561
REMARK 465 THR S 562
REMARK 465 ASN S 563
REMARK 465 LEU S 564
REMARK 465 PRO S 565
REMARK 465 GLU S 566
REMARK 465 GLY S 567
REMARK 465 TRP S 568
REMARK 465 PHE S 569
REMARK 465 VAL S 570
REMARK 465 THR S 571
REMARK 465 VAL S 572
REMARK 465 ASP S 573
REMARK 465 LYS S 574
REMARK 465 LYS S 575
REMARK 465 THR S 576
REMARK 465 GLY S 577
REMARK 465 LYS S 578
REMARK 465 TYR S 579
REMARK 465 TYR S 580
REMARK 465 PHE S 581
REMARK 465 TYR S 582
REMARK 465 ASP S 583
REMARK 465 VAL S 584
REMARK 465 ASN S 585
REMARK 465 GLY S 586
REMARK 465 LYS S 587
REMARK 465 VAL S 588
REMARK 465 GLN S 589
REMARK 465 TRP S 590
REMARK 465 GLN S 591
REMARK 465 ARG S 592
REMARK 465 PRO S 593
REMARK 465 THR S 594
REMARK 465 ALA S 595
REMARK 465 PRO S 596
REMARK 465 ALA S 597
REMARK 465 ILE S 598
REMARK 465 THR S 599
REMARK 465 THR S 600
REMARK 465 PRO S 601
REMARK 465 LYS S 602
REMARK 465 PRO S 603
REMARK 465 SER S 604
REMARK 465 VAL S 605
REMARK 465 LYS S 606
REMARK 465 ALA S 607
REMARK 465 GLN S 608
REMARK 465 GLN S 609
REMARK 465 ASP S 610
REMARK 465 GLN S 611
REMARK 465 LYS S 612
REMARK 465 ALA S 613
REMARK 465 LEU S 614
REMARK 465 GLN S 615
REMARK 465 ASP S 616
REMARK 465 ILE S 617
REMARK 465 ILE S 618
REMARK 465 ASP S 619
REMARK 465 SER S 620
REMARK 465 LEU S 621
REMARK 465 THR S 622
REMARK 465 LYS S 623
REMARK 465 GLU S 624
REMARK 465 PRO S 625
REMARK 465 THR S 626
REMARK 465 PRO S 627
REMARK 465 ARG S 628
REMARK 465 GLN S 629
REMARK 465 SER S 630
REMARK 465 ALA S 631
REMARK 465 GLY S 632
REMARK 465 HIS S 633
REMARK 465 THR S 634
REMARK 465 PRO S 635
REMARK 465 GLN S 636
REMARK 465 ARG S 637
REMARK 465 SER S 638
REMARK 465 SER S 639
REMARK 465 THR S 640
REMARK 465 PRO S 641
REMARK 465 ALA S 642
REMARK 465 THR S 643
REMARK 465 GLU S 644
REMARK 465 PRO S 645
REMARK 465 LYS S 646
REMARK 465 LYS S 647
REMARK 465 GLU S 648
REMARK 465 LYS S 649
REMARK 465 TRP S 650
REMARK 465 ARG S 651
REMARK 465 SER S 652
REMARK 465 LEU S 653
REMARK 465 PRO S 654
REMARK 465 ILE S 655
REMARK 465 GLU S 656
REMARK 465 LYS S 657
REMARK 465 GLN S 658
REMARK 465 MET S 659
REMARK 465 LYS S 660
REMARK 465 ILE S 661
REMARK 465 TYR S 662
REMARK 465 GLU S 663
REMARK 465 ASN S 664
REMARK 465 THR S 665
REMARK 465 LEU S 666
REMARK 465 PHE S 667
REMARK 465 PRO S 668
REMARK 465 HIS S 669
REMARK 465 VAL S 670
REMARK 465 LYS S 671
REMARK 465 TYR S 672
REMARK 465 VAL S 673
REMARK 465 MET S 674
REMARK 465 ASP S 675
REMARK 465 LYS S 676
REMARK 465 PHE S 677
REMARK 465 HIS S 678
REMARK 465 GLY S 679
REMARK 465 LYS S 680
REMARK 465 LEU S 681
REMARK 465 PRO S 682
REMARK 465 ARG S 683
REMARK 465 GLU S 684
REMARK 465 ASP S 685
REMARK 465 LEU S 686
REMARK 465 LYS S 687
REMARK 465 LYS S 688
REMARK 465 PHE S 689
REMARK 465 ALA S 690
REMARK 465 ARG S 691
REMARK 465 ASP S 692
REMARK 465 VAL S 693
REMARK 465 ASN S 694
REMARK 465 LYS S 695
REMARK 465 LYS S 696
REMARK 465 LEU S 697
REMARK 465 VAL S 698
REMARK 465 ALA S 699
REMARK 465 SER S 700
REMARK 465 ASP S 701
REMARK 465 TYR S 702
REMARK 465 LYS S 703
REMARK 465 HIS S 704
REMARK 465 ASN S 705
REMARK 465 ARG S 706
REMARK 465 VAL S 707
REMARK 465 GLN S 708
REMARK 465 ASP S 709
REMARK 465 PRO S 710
REMARK 465 THR S 711
REMARK 465 VAL S 712
REMARK 465 PRO S 713
REMARK 465 LEU S 714
REMARK 465 SER S 715
REMARK 465 SER S 716
REMARK 465 LYS S 717
REMARK 465 GLN S 718
REMARK 465 ALA S 719
REMARK 465 LYS S 720
REMARK 465 LYS S 721
REMARK 465 VAL S 722
REMARK 465 ARG S 723
REMARK 465 LYS S 724
REMARK 465 TYR S 725
REMARK 465 VAL S 726
REMARK 465 TYR S 727
REMARK 465 ASP S 728
REMARK 465 PHE S 729
REMARK 465 PHE S 730
REMARK 465 ASP S 731
REMARK 465 ARG S 732
REMARK 465 ALA S 733
REMARK 465 LEU S 734
REMARK 465 GLN S 735
REMARK 465 LYS S 736
REMARK 465 TYR S 737
REMARK 465 LEU S 738
REMARK 465 GLU S 739
REMARK 465 TYR S 740
REMARK 465 GLN S 741
REMARK 465 LYS S 742
REMARK 465 ARG S 743
REMARK 465 LYS S 744
REMARK 465 ALA S 745
REMARK 465 GLN S 746
REMARK 465 TYR S 747
REMARK 465 THR S 748
REMARK 465 SER S 749
REMARK 465 LYS S 750
REMARK 465 GLU S 751
REMARK 465 GLY S 752
REMARK 465 MET S 753
REMARK 465 GLN S 754
REMARK 465 SER S 755
REMARK 465 SER S 756
REMARK 465 GLN S 757
REMARK 465 THR S 758
REMARK 465 GLU S 759
REMARK 465 GLN S 760
REMARK 465 ASN S 761
REMARK 465 THR S 762
REMARK 465 ALA S 763
REMARK 465 THR S 764
REMARK 465 PRO S 765
REMARK 465 THR S 766
REMARK 465 GLY S 767
REMARK 465 THR S 768
REMARK 465 LEU S 769
REMARK 465 GLY S 770
REMARK 465 LYS S 771
REMARK 465 ASP S 772
REMARK 465 VAL S 773
REMARK 465 ASP S 774
REMARK 465 GLU S 775
REMARK 465 VAL S 776
REMARK 465 MET S 777
REMARK 465 SER S 778
REMARK 465 ASP S 779
REMARK 465 VAL S 780
REMARK 465 GLU S 781
REMARK 465 ALA S 782
REMARK 465 PRO S 783
REMARK 465 ASN S 784
REMARK 465 SER S 785
REMARK 465 SER S 786
REMARK 465 PRO S 787
REMARK 465 GLN S 788
REMARK 465 SER S 789
REMARK 465 THR S 790
REMARK 465 SER S 791
REMARK 465 SER S 792
REMARK 465 ALA S 793
REMARK 465 GLY S 794
REMARK 465 ARG S 795
REMARK 465 LYS S 796
REMARK 465 ARG S 797
REMARK 465 LYS S 798
REMARK 465 ARG S 799
REMARK 465 ASP S 800
REMARK 465 ASP S 801
REMARK 465 ASP S 802
REMARK 465 GLN S 803
REMARK 465 ASP S 804
REMARK 465 GLY S 805
REMARK 465 ASP S 806
REMARK 465 HIS S 807
REMARK 465 ASP S 808
REMARK 465 MET S 809
REMARK 465 ARG S 810
REMARK 465 SER S 811
REMARK 465 PRO S 812
REMARK 465 ALA S 813
REMARK 465 ASP S 814
REMARK 465 GLU S 815
REMARK 465 ASP S 816
REMARK 465 ALA S 817
REMARK 465 ALA S 818
REMARK 465 THR S 819
REMARK 465 SER S 820
REMARK 465 SER S 821
REMARK 465 ASP S 822
REMARK 465 PRO S 823
REMARK 465 PRO S 824
REMARK 465 SER S 825
REMARK 465 VAL S 826
REMARK 465 LYS S 827
REMARK 465 ARG S 828
REMARK 465 ILE S 829
REMARK 465 LYS S 830
REMARK 465 GLU S 831
REMARK 465 ASP S 832
REMARK 465 ASP S 833
REMARK 465 GLY S 834
REMARK 465 THR S 835
REMARK 465 GLY S 836
REMARK 465 ASN S 837
REMARK 465 ASP S 838
REMARK 465 VAL S 839
REMARK 465 ILE S 840
REMARK 465 PRO S 841
REMARK 465 SER S 842
REMARK 465 PRO S 843
REMARK 465 PRO S 844
REMARK 465 PRO S 845
REMARK 465 PRO S 846
REMARK 465 PRO S 847
REMARK 465 PRO S 848
REMARK 465 PRO S 849
REMARK 465 PRO S 850
REMARK 465 ALA S 851
REMARK 465 GLU S 852
REMARK 465 ILE S 853
REMARK 465 PRO S 854
REMARK 465 MET S 855
REMARK 465 THR S 856
REMARK 465 GLU S 857
REMARK 465 GLU S 858
REMARK 465 GLU S 859
REMARK 465 ARG S 860
REMARK 465 SER S 861
REMARK 465 MET S 862
REMARK 465 ARG S 863
REMARK 465 GLU S 864
REMARK 465 GLN S 865
REMARK 465 GLU S 866
REMARK 465 GLU S 867
REMARK 465 ALA S 868
REMARK 465 LEU S 869
REMARK 465 MET S 870
REMARK 465 ARG S 871
REMARK 465 GLU S 872
REMARK 465 ASN S 873
REMARK 465 GLU S 874
REMARK 465 GLU S 875
REMARK 465 ALA S 876
REMARK 465 GLN S 877
REMARK 465 ARG S 878
REMARK 465 LEU S 879
REMARK 465 GLU S 880
REMARK 465 ASP S 881
REMARK 465 GLU S 882
REMARK 465 ALA S 883
REMARK 465 LYS S 884
REMARK 465 ARG S 885
REMARK 465 LYS S 886
REMARK 465 GLN S 887
REMARK 465 LEU S 888
REMARK 465 GLU S 889
REMARK 465 LEU S 890
REMARK 465 GLN S 891
REMARK 465 ASN S 892
REMARK 465 GLY S 893
REMARK 465 LEU S 894
REMARK 465 ALA S 895
REMARK 465 ALA S 896
REMARK 465 ALA S 897
REMARK 465 LYS S 898
REMARK 465 ASN S 899
REMARK 465 ALA S 900
REMARK 465 GLY S 901
REMARK 465 ILE S 902
REMARK 465 GLU S 903
REMARK 465 LEU S 904
REMARK 465 GLY S 905
REMARK 465 SER S 906
REMARK 465 ALA S 907
REMARK 465 SER S 908
REMARK 465 PHE S 909
REMARK 465 THR S 910
REMARK 465 VAL S 911
REMARK 465 SER S 912
REMARK 465 GLY S 913
REMARK 465 GLU S 914
REMARK 465 PRO S 915
REMARK 465 MET S 916
REMARK 465 ASP S 917
REMARK 465 VAL S 918
REMARK 465 ASP S 919
REMARK 465 ASN S 920
REMARK 465 ASP S 921
REMARK 465 GLY S 922
REMARK 465 PRO S 923
REMARK 465 PRO S 924
REMARK 465 PRO S 925
REMARK 465 GLN S 926
REMARK 465 GLU S 927
REMARK 465 GLN S 928
REMARK 465 ALA S 929
REMARK 465 GLN S 930
REMARK 465 GLN S 931
REMARK 465 GLN S 932
REMARK 465 LYS S 933
REMARK 465 GLN S 934
REMARK 465 ALA S 935
REMARK 465 VAL S 936
REMARK 465 MET S 937
REMARK 465 SER S 938
REMARK 465 HIS S 939
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS C 36 CG CD CE NZ
REMARK 470 SER S 80 OG
REMARK 470 SER S 81 OG
REMARK 470 LYS S 82 CG CD CE NZ
REMARK 470 LEU S 83 CG CD1 CD2
REMARK 470 PRO S 84 CG CD
REMARK 470 PRO S 88 CG CD
REMARK 470 PRO S 89 CG CD
REMARK 470 GLN S 90 CG CD OE1 NE2
REMARK 470 LEU S 91 CG CD1 CD2
REMARK 470 PHE S 92 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN S 93 CG OD1 ND2
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 O GLN C -23 OE2 GLU D 102 0.86
REMARK 500 O GLN C -23 CD GLU D 102 1.59
REMARK 500 O GLY C -25 OD1 ASP C 90 1.74
REMARK 500 C GLN C -23 OE2 GLU D 102 1.79
REMARK 500 NE2 GLN C -23 CE1 HIS D 106 2.01
REMARK 500 NE2 GLN C -23 ND1 HIS D 106 2.11
REMARK 500 O ASN C -47 OG SER C -44 2.11
REMARK 500 OD1 ASP C -48 CB ASP C -20 2.17
REMARK 500 O GLN C -23 OE1 GLU D 102 2.18
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 DC I 82 O3' DC I 82 C3' -0.037
REMARK 500 DC I 84 O3' DC I 84 C3' -0.044
REMARK 500 DT J 28 O3' DT J 28 C3' -0.044
REMARK 500 DG J 29 O3' DG J 29 C3' -0.049
REMARK 500 DG J 68 O3' DG J 68 C3' -0.040
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 40 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA I 49 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC I 107 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I 118 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT I 138 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG J 29 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA J 40 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC J 49 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG J 69 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA J 90 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG J 101 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT J 109 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC J 111 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG J 122 O4' - C1' - N9 ANGL. DEV. = 2.1 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 PRO A 43 86.98 -63.62
REMARK 500 ASP A 81 60.24 60.07
REMARK 500 ASP B 24 30.42 -92.70
REMARK 500 HIS D 46 88.38 -151.40
REMARK 500 ALA E 114 20.06 -78.04
REMARK 500 PRO G 109 77.15 -65.94
REMARK 500 LEU S 83 52.36 -95.01
REMARK 500 SER S 110 -0.66 -141.02
REMARK 500 SER S 116 -53.43 -120.45
REMARK 500 ASP S 123 19.62 50.26
REMARK 500 ASP S 130 40.88 -99.71
REMARK 500 ARG S 136 -36.26 -130.00
REMARK 500 ASP S 146 12.22 -141.83
REMARK 500 GLN S 172 13.64 -141.35
REMARK 500 LYS S 177 66.16 60.65
REMARK 500 GLN S 178 52.25 -94.48
REMARK 500 ILE S 206 -62.60 -108.50
REMARK 500 PHE S 236 56.53 -96.97
REMARK 500 PHE S 294 -169.26 -124.90
REMARK 500 GLN S 324 54.63 -95.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S1002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 129 SG
REMARK 620 2 CYS S 131 SG 90.7
REMARK 620 3 CYS S 143 SG 134.9 115.9
REMARK 620 4 CYS S 149 SG 143.1 65.8 82.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 143 SG
REMARK 620 2 CYS S 158 SG 117.6
REMARK 620 3 CYS S 163 SG 118.8 116.7
REMARK 620 4 CYS S 169 SG 73.1 89.8 132.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN S1003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 261 SG
REMARK 620 2 CYS S 308 SG 126.5
REMARK 620 3 CYS S 310 SG 145.9 61.9
REMARK 620 4 CYS S 315 SG 126.7 85.1 84.5
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-0559 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-20517 RELATED DB: EMDB
REMARK 900 SET2 BOUND TO NUCLEOSOME
DBREF1 6PX3 A 0 135 UNP A0A310TTQ1_XENLA
DBREF2 6PX3 A A0A310TTQ1 1 136
DBREF 6PX3 B 0 102 UNP P62799 H4_XENLA 1 103
DBREF 6PX3 C -71 3 UNP P0CH09 RL40B_YEAST 1 75
DBREF 6PX3 C 17 129 UNP Q6AZJ8 Q6AZJ8_XENLA 18 130
DBREF 6PX3 D 1 122 UNP P02281 H2B11_XENLA 5 126
DBREF1 6PX3 E 0 135 UNP A0A310TTQ1_XENLA
DBREF2 6PX3 E A0A310TTQ1 1 136
DBREF 6PX3 F 0 102 UNP P62799 H4_XENLA 1 103
DBREF 6PX3 G -71 3 UNP P0CH09 RL40B_YEAST 1 75
DBREF 6PX3 G 17 129 UNP Q6AZJ8 Q6AZJ8_XENLA 18 130
DBREF 6PX3 H 1 122 UNP P02281 H2B11_XENLA 5 126
DBREF 6PX3 I 1 149 PDB 6PX3 6PX3 1 149
DBREF 6PX3 J -1 147 PDB 6PX3 6PX3 -1 147
DBREF 6PX3 S 1 939 UNP G0S676 G0S676_CHATD 1 939
SEQADV 6PX3 MET A 36 UNP A0A310TTQ LYS 37 ENGINEERED MUTATION
SEQADV 6PX3 MET C -91 UNP P0CH09 INITIATING METHIONINE
SEQADV 6PX3 ASP C -90 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 SER C -89 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 PRO C -88 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 ASP C -87 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 LEU C -86 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -85 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -84 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -83 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -82 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -81 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS C -80 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 GLY C -79 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 THR C -78 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 LEU C -77 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 VAL C -76 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 PRO C -75 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 ARG C -74 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 GLY C -73 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 SER C -72 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 THR C 4 UNP P0CH09 LINKER
SEQADV 6PX3 SER C 5 UNP P0CH09 LINKER
SEQADV 6PX3 SER C 6 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 7 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 8 UNP P0CH09 LINKER
SEQADV 6PX3 SER C 9 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 10 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 11 UNP P0CH09 LINKER
SEQADV 6PX3 SER C 12 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 13 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 14 UNP P0CH09 LINKER
SEQADV 6PX3 SER C 15 UNP P0CH09 LINKER
SEQADV 6PX3 GLY C 16 UNP P0CH09 LINKER
SEQADV 6PX3 MET D 0 UNP P02281 INITIATING METHIONINE
SEQADV 6PX3 THR D 29 UNP P02281 SER 33 ENGINEERED MUTATION
SEQADV 6PX3 MET E 36 UNP A0A310TTQ LYS 37 ENGINEERED MUTATION
SEQADV 6PX3 MET G -91 UNP P0CH09 INITIATING METHIONINE
SEQADV 6PX3 ASP G -90 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 SER G -89 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 PRO G -88 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 ASP G -87 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 LEU G -86 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -85 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -84 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -83 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -82 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -81 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 HIS G -80 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 GLY G -79 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 THR G -78 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 LEU G -77 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 VAL G -76 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 PRO G -75 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 ARG G -74 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 GLY G -73 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 SER G -72 UNP P0CH09 EXPRESSION TAG
SEQADV 6PX3 THR G 4 UNP P0CH09 LINKER
SEQADV 6PX3 SER G 5 UNP P0CH09 LINKER
SEQADV 6PX3 SER G 6 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 7 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 8 UNP P0CH09 LINKER
SEQADV 6PX3 SER G 9 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 10 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 11 UNP P0CH09 LINKER
SEQADV 6PX3 SER G 12 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 13 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 14 UNP P0CH09 LINKER
SEQADV 6PX3 SER G 15 UNP P0CH09 LINKER
SEQADV 6PX3 GLY G 16 UNP P0CH09 LINKER
SEQADV 6PX3 MET H 0 UNP P02281 INITIATING METHIONINE
SEQADV 6PX3 THR H 29 UNP P02281 SER 33 ENGINEERED MUTATION
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 MET 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 ALA 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 221 MET ASP SER PRO ASP LEU HIS HIS HIS HIS HIS HIS GLY
SEQRES 2 C 221 THR LEU VAL PRO ARG GLY SER MET GLN ILE PHE VAL LYS
SEQRES 3 C 221 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU SER
SEQRES 4 C 221 SER ASP THR ILE ASP ASN VAL LYS SER LYS ILE GLN ASP
SEQRES 5 C 221 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 6 C 221 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 7 C 221 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 8 C 221 ARG LEU ARG GLY THR SER SER GLY GLY SER GLY GLY SER
SEQRES 9 C 221 GLY GLY SER GLY ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 10 C 221 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 11 C 221 TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 12 C 221 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 13 C 221 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 14 C 221 ILE ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP
SEQRES 15 C 221 GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA
SEQRES 16 C 221 GLN GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU
SEQRES 17 C 221 PRO LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 D 123 MET ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS
SEQRES 2 D 123 LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS
SEQRES 3 D 123 ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL
SEQRES 4 D 123 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 5 D 123 SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN
SEQRES 6 D 123 ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 7 D 123 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 8 D 123 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 9 D 123 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 10 D 123 LYS TYR THR SER ALA 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 MET 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 ALA 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 221 MET ASP SER PRO ASP LEU HIS HIS HIS HIS HIS HIS GLY
SEQRES 2 G 221 THR LEU VAL PRO ARG GLY SER MET GLN ILE PHE VAL LYS
SEQRES 3 G 221 THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU SER
SEQRES 4 G 221 SER ASP THR ILE ASP ASN VAL LYS SER LYS ILE GLN ASP
SEQRES 5 G 221 LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE
SEQRES 6 G 221 ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP
SEQRES 7 G 221 TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU
SEQRES 8 G 221 ARG LEU ARG GLY THR SER SER GLY GLY SER GLY GLY SER
SEQRES 9 G 221 GLY GLY SER GLY ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 10 G 221 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 11 G 221 TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 12 G 221 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 13 G 221 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 14 G 221 ILE ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP
SEQRES 15 G 221 GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA
SEQRES 16 G 221 GLN GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU
SEQRES 17 G 221 PRO LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 H 123 MET ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS
SEQRES 2 H 123 LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS
SEQRES 3 H 123 ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL
SEQRES 4 H 123 TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE
SEQRES 5 H 123 SER SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN
SEQRES 6 H 123 ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU
SEQRES 7 H 123 ALA HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU
SEQRES 8 H 123 ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU
SEQRES 9 H 123 ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR
SEQRES 10 H 123 LYS TYR THR SER ALA LYS
SEQRES 1 I 149 DC DT DG DG DA DG DA DA DT DC DC DC DG
SEQRES 2 I 149 DG DT DG DC DC DG DA DG DG DC DC DG DC
SEQRES 3 I 149 DT DC DA DA DT DT DG DG DT DC DG DT DA
SEQRES 4 I 149 DG DA DC DA DG DC DT DC DT DA DG DC DA
SEQRES 5 I 149 DC DC DG DC DT DT DA DA DA DC DG DC DA
SEQRES 6 I 149 DC DG DT DA DC DG DC DG DC DT DG DT DC
SEQRES 7 I 149 DC DC DC DC DG DC DG DT DT DT DT DA DA
SEQRES 8 I 149 DC DC DG DC DC DA DA DG DG DG DG DA DT
SEQRES 9 I 149 DT DA DC DT DC DC DC DT DA DG DT DC DT
SEQRES 10 I 149 DC DC DA DG DG DC DA DC DG DT DG DT DC
SEQRES 11 I 149 DA DG DA DT DA DT DA DT DA DC DA DT DC
SEQRES 12 I 149 DC DT DG DT DG DC
SEQRES 1 J 149 DG DC DA DC DA DG DG DA DT DG DT DA DT
SEQRES 2 J 149 DA DT DA DT DC DT DG DA DC DA DC DG DT
SEQRES 3 J 149 DG DC DC DT DG DG DA DG DA DC DT DA DG
SEQRES 4 J 149 DG DG DA DG DT DA DA DT DC DC DC DC DT
SEQRES 5 J 149 DT DG DG DC DG DG DT DT DA DA DA DA DC
SEQRES 6 J 149 DG DC DG DG DG DG DG DA DC DA DG DC DG
SEQRES 7 J 149 DC DG DT DA DC DG DT DG DC DG DT DT DT
SEQRES 8 J 149 DA DA DG DC DG DG DT DG DC DT DA DG DA
SEQRES 9 J 149 DG DC DT DG DT DC DT DA DC DG DA DC DC
SEQRES 10 J 149 DA DA DT DT DG DA DG DC DG DG DC DC DT
SEQRES 11 J 149 DC DG DG DC DA DC DC DG DG DG DA DT DT
SEQRES 12 J 149 DC DT DC DC DA DG
SEQRES 1 S 939 MET GLU ALA SER ASP ARG ALA SER GLY PRO THR ALA GLY
SEQRES 2 S 939 SER LYS SER GLU GLU ARG THR LYS GLN ASN GLY PRO ARG
SEQRES 3 S 939 SER LYS LYS GLU ASP ALA SER ASP SER SER THR SER THR
SEQRES 4 S 939 GLY SER LYS SER ALA SER ARG SER SER SER ALA THR THR
SEQRES 5 S 939 MET SER PRO ASP ASP ALA LYS PRO ALA ASP ASP SER ALA
SEQRES 6 S 939 LEU ALA GLN GLU ASN GLY VAL ALA PRO LYS PRO SER ARG
SEQRES 7 S 939 LYS SER SER LYS LEU PRO PRO ARG ASN PRO PRO GLN LEU
SEQRES 8 S 939 PHE ASN HIS LEU PRO ASP ALA THR GLU GLU ALA CYS ARG
SEQRES 9 S 939 THR PHE GLN VAL ILE SER ASP CYS LEU TYR GLY SER ARG
SEQRES 10 S 939 ASN MET GLY SER SER ASP HIS ASP ALA LEU ASP CYS ASP
SEQRES 11 S 939 CYS ALA GLU ASP TRP ARG ASP GLY LYS ASN HIS ALA CYS
SEQRES 12 S 939 GLY GLU ASP SER ASP CYS ILE ASN ARG ALA THR LYS ILE
SEQRES 13 S 939 GLU CYS VAL ILE GLY ASP CYS ASN CYS GLY GLU GLY CYS
SEQRES 14 S 939 GLN ASN GLN ARG PHE GLN ARG LYS GLN TYR ALA LYS VAL
SEQRES 15 S 939 SER VAL ILE LYS THR GLU LYS LYS GLY TYR GLY LEU ARG
SEQRES 16 S 939 ALA ASP THR ASP LEU GLN PRO ASN ASP PHE ILE TYR GLU
SEQRES 17 S 939 TYR VAL GLY GLU VAL ILE ASN GLU PRO THR PHE ARG SER
SEQRES 18 S 939 ARG MET LEU LYS TYR ASP LYS GLU GLY ILE LYS HIS PHE
SEQRES 19 S 939 TYR PHE MET SER LEU THR LYS ASN GLU PHE VAL ASP ALA
SEQRES 20 S 939 THR LYS LYS GLY ASN LEU GLY ARG PHE CYS ASN HIS SER
SEQRES 21 S 939 CYS ASN PRO ASN CYS TYR VAL ASP LYS TRP VAL VAL GLY
SEQRES 22 S 939 ASP LYS LEU ARG MET GLY ILE PHE ALA ALA ARG TYR ILE
SEQRES 23 S 939 LYS ALA GLY GLU GLU LEU VAL PHE ASN TYR ASN VAL ASP
SEQRES 24 S 939 ARG TYR GLY ALA ASP PRO GLN PRO CYS TYR CYS GLY GLU
SEQRES 25 S 939 PRO ASN CYS VAL GLY PHE ILE GLY GLY LYS THR GLN THR
SEQRES 26 S 939 GLU ARG ALA THR LYS LEU PRO LEU ALA THR ILE GLU ALA
SEQRES 27 S 939 LEU GLY ILE GLU ASP GLY ASP SER TRP ASP THR THR VAL
SEQRES 28 S 939 ALA LYS LYS PRO ARG LYS LYS LYS ALA SER GLU THR ASP
SEQRES 29 S 939 GLU GLU TYR VAL ASN SER LEU GLN PRO LYS ALA LEU ASP
SEQRES 30 S 939 GLU ASP GLY VAL ASN LYS VAL MET ALA THR LEU MET GLN
SEQRES 31 S 939 CYS LYS GLU LYS TRP ILE ALA VAL LYS LEU LEU SER ARG
SEQRES 32 S 939 LEU GLN ALA THR GLN ASP ASP HIS LEU ARG HIS ARG VAL
SEQRES 33 S 939 VAL ARG MET HIS GLY TYR GLN ILE LEU LYS SER THR LEU
SEQRES 34 S 939 ASN ALA PHE LYS HIS ASP ASN ASN VAL VAL LEU GLN VAL
SEQRES 35 S 939 LEU ASP ILE LEU TYR ASN LEU PRO ARG ILE THR LYS ASN
SEQRES 36 S 939 LYS ILE SER ASP SER ASN ILE GLU ALA VAL VAL GLN PRO
SEQRES 37 S 939 LEU ALA SER SER SER ASP GLU ARG VAL ALA PHE GLU ALA
SEQRES 38 S 939 LYS ARG LEU LEU GLU GLU TRP ASP LYS LEU GLU THR ALA
SEQRES 39 S 939 TYR ARG ILE PRO ARG LYS LYS ASP GLY ARG VAL VAL SER
SEQRES 40 S 939 ALA ILE ALA ASN SER PHE GLU GLU GLU ARG ARG SER ASN
SEQRES 41 S 939 ARG GLU GLU PRO THR LYS PRO ALA ASP PRO LEU ALA ASN
SEQRES 42 S 939 VAL VAL ILE PRO THR GLY PRO ARG SER ASN ILE PRO GLN
SEQRES 43 S 939 ARG ASN ALA ASN TYR TYR ASN GLY VAL ARG PRO ARG LYS
SEQRES 44 S 939 PRO PRO THR ASN LEU PRO GLU GLY TRP PHE VAL THR VAL
SEQRES 45 S 939 ASP LYS LYS THR GLY LYS TYR TYR PHE TYR ASP VAL ASN
SEQRES 46 S 939 GLY LYS VAL GLN TRP GLN ARG PRO THR ALA PRO ALA ILE
SEQRES 47 S 939 THR THR PRO LYS PRO SER VAL LYS ALA GLN GLN ASP GLN
SEQRES 48 S 939 LYS ALA LEU GLN ASP ILE ILE ASP SER LEU THR LYS GLU
SEQRES 49 S 939 PRO THR PRO ARG GLN SER ALA GLY HIS THR PRO GLN ARG
SEQRES 50 S 939 SER SER THR PRO ALA THR GLU PRO LYS LYS GLU LYS TRP
SEQRES 51 S 939 ARG SER LEU PRO ILE GLU LYS GLN MET LYS ILE TYR GLU
SEQRES 52 S 939 ASN THR LEU PHE PRO HIS VAL LYS TYR VAL MET ASP LYS
SEQRES 53 S 939 PHE HIS GLY LYS LEU PRO ARG GLU ASP LEU LYS LYS PHE
SEQRES 54 S 939 ALA ARG ASP VAL ASN LYS LYS LEU VAL ALA SER ASP TYR
SEQRES 55 S 939 LYS HIS ASN ARG VAL GLN ASP PRO THR VAL PRO LEU SER
SEQRES 56 S 939 SER LYS GLN ALA LYS LYS VAL ARG LYS TYR VAL TYR ASP
SEQRES 57 S 939 PHE PHE ASP ARG ALA LEU GLN LYS TYR LEU GLU TYR GLN
SEQRES 58 S 939 LYS ARG LYS ALA GLN TYR THR SER LYS GLU GLY MET GLN
SEQRES 59 S 939 SER SER GLN THR GLU GLN ASN THR ALA THR PRO THR GLY
SEQRES 60 S 939 THR LEU GLY LYS ASP VAL ASP GLU VAL MET SER ASP VAL
SEQRES 61 S 939 GLU ALA PRO ASN SER SER PRO GLN SER THR SER SER ALA
SEQRES 62 S 939 GLY ARG LYS ARG LYS ARG ASP ASP ASP GLN ASP GLY ASP
SEQRES 63 S 939 HIS ASP MET ARG SER PRO ALA ASP GLU ASP ALA ALA THR
SEQRES 64 S 939 SER SER ASP PRO PRO SER VAL LYS ARG ILE LYS GLU ASP
SEQRES 65 S 939 ASP GLY THR GLY ASN ASP VAL ILE PRO SER PRO PRO PRO
SEQRES 66 S 939 PRO PRO PRO PRO PRO ALA GLU ILE PRO MET THR GLU GLU
SEQRES 67 S 939 GLU ARG SER MET ARG GLU GLN GLU GLU ALA LEU MET ARG
SEQRES 68 S 939 GLU ASN GLU GLU ALA GLN ARG LEU GLU ASP GLU ALA LYS
SEQRES 69 S 939 ARG LYS GLN LEU GLU LEU GLN ASN GLY LEU ALA ALA ALA
SEQRES 70 S 939 LYS ASN ALA GLY ILE GLU LEU GLY SER ALA SER PHE THR
SEQRES 71 S 939 VAL SER GLY GLU PRO MET ASP VAL ASP ASN ASP GLY PRO
SEQRES 72 S 939 PRO PRO GLN GLU GLN ALA GLN GLN GLN LYS GLN ALA VAL
SEQRES 73 S 939 MET SER HIS
HET ZN S1001 1
HET ZN S1002 1
HET ZN S1003 1
HETNAM ZN ZINC ION
FORMUL 12 ZN 3(ZN 2+)
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 ASP A 77 1 15
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 ASP B 24 ILE B 29 5 6
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 GLN B 93 1 12
HELIX 9 AA9 THR C -50 GLY C -37 1 14
HELIX 10 AB1 PRO C -35 ASP C -33 5 3
HELIX 11 AB2 THR C -17 ASN C -12 5 6
HELIX 12 AB3 ARG C 17 ALA C 21 1 5
HELIX 13 AB4 PRO C 26 LYS C 36 1 11
HELIX 14 AB5 ALA C 45 ASN C 73 1 29
HELIX 15 AB6 ILE C 79 ASP C 90 1 12
HELIX 16 AB7 ASP C 90 LEU C 97 1 8
HELIX 17 AB8 GLN C 112 LEU C 116 5 5
HELIX 18 AB9 TYR D 34 HIS D 46 1 13
HELIX 19 AC1 SER D 52 ASN D 81 1 30
HELIX 20 AC2 THR D 87 LEU D 99 1 13
HELIX 21 AC3 GLY D 101 SER D 120 1 20
HELIX 22 AC4 GLY E 44 SER E 57 1 14
HELIX 23 AC5 ARG E 63 ASP E 77 1 15
HELIX 24 AC6 GLN E 85 ALA E 114 1 30
HELIX 25 AC7 MET E 120 GLY E 132 1 13
HELIX 26 AC8 ASN F 25 ILE F 29 5 5
HELIX 27 AC9 THR F 30 GLY F 41 1 12
HELIX 28 AD1 LEU F 49 LYS F 77 1 29
HELIX 29 AD2 THR F 82 GLN F 93 1 12
HELIX 30 AD3 ARG G 17 GLY G 22 1 6
HELIX 31 AD4 PRO G 26 LYS G 36 1 11
HELIX 32 AD5 ALA G 45 ASP G 72 1 28
HELIX 33 AD6 ILE G 79 ASN G 89 1 11
HELIX 34 AD7 ASP G 90 LEU G 97 1 8
HELIX 35 AD8 GLN G 112 LEU G 116 5 5
HELIX 36 AD9 TYR H 34 HIS H 46 1 13
HELIX 37 AE1 SER H 52 ASN H 81 1 30
HELIX 38 AE2 THR H 87 LEU H 99 1 13
HELIX 39 AE3 PRO H 100 SER H 120 1 21
HELIX 40 AE4 ASN S 151 LYS S 155 5 5
HELIX 41 AE5 ASN S 215 GLY S 230 1 16
HELIX 42 AE6 ASN S 252 PHE S 256 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 TYR B 98
SHEET 1 AA4 5 THR C -60 GLU C -56 0
SHEET 2 AA4 5 GLN C -70 LYS C -66 -1 N ILE C -69 O LEU C -57
SHEET 3 AA4 5 THR C -6 LEU C -1 1 O LEU C -3 N LYS C -66
SHEET 4 AA4 5 GLN C -31 PHE C -27 -1 N ARG C -30 O VAL C -2
SHEET 5 AA4 5 LYS C -24 GLN C -23 -1 O LYS C -24 N PHE C -27
SHEET 1 AA5 2 ARG C 42 VAL C 43 0
SHEET 2 AA5 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 AA6 2 ARG C 77 ILE C 78 0
SHEET 2 AA6 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 78
SHEET 1 AA7 2 VAL C 100 ILE C 102 0
SHEET 2 AA7 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 AA8 2 VAL E 35 MET E 36 0
SHEET 2 AA8 2 VAL S 298 ASP S 299 -1 O ASP S 299 N VAL E 35
SHEET 1 AA9 2 ARG E 83 PHE E 84 0
SHEET 2 AA9 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AB1 2 THR E 118 ILE E 119 0
SHEET 2 AB1 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AB2 2 ARG G 42 VAL G 43 0
SHEET 2 AB2 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 AB3 2 ARG G 77 ILE G 78 0
SHEET 2 AB3 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
SHEET 1 AB4 2 VAL S 182 THR S 187 0
SHEET 2 AB4 2 GLY S 191 ALA S 196 -1 O GLY S 191 N THR S 187
SHEET 1 AB5 3 PHE S 205 GLU S 208 0
SHEET 2 AB5 3 LYS S 275 ALA S 282 -1 O ILE S 280 N TYR S 207
SHEET 3 AB5 3 CYS S 265 VAL S 272 -1 N TRP S 270 O ARG S 277
SHEET 1 AB6 2 GLU S 212 ILE S 214 0
SHEET 2 AB6 2 PHE S 244 ASP S 246 -1 O ASP S 246 N GLU S 212
SSBOND 1 CYS S 131 CYS S 149 1555 1555 2.63
SSBOND 2 CYS S 143 CYS S 169 1555 1555 2.85
SSBOND 3 CYS S 308 CYS S 310 1555 1555 2.37
LINK SG CYS S 129 ZN ZN S1002 1555 1555 2.26
LINK SG CYS S 131 ZN ZN S1002 1555 1555 2.50
LINK SG CYS S 143 ZN ZN S1002 1555 1555 2.36
LINK SG CYS S 143 ZN ZN S1001 1555 1555 2.40
LINK SG CYS S 149 ZN ZN S1002 1555 1555 2.34
LINK SG CYS S 158 ZN ZN S1001 1555 1555 2.45
LINK SG CYS S 163 ZN ZN S1001 1555 1555 2.46
LINK SG CYS S 169 ZN ZN S1001 1555 1555 2.38
LINK SG CYS S 261 ZN ZN S1003 1555 1555 2.33
LINK SG CYS S 308 ZN ZN S1003 1555 1555 2.28
LINK SG CYS S 310 ZN ZN S1003 1555 1555 2.33
LINK SG CYS S 315 ZN ZN S1003 1555 1555 2.31
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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