HEADER DNA BINDING PROTEIN 31-JAN-19 6QLD
TITLE STRUCTURE OF INNER KINETOCHORE CCAN-CENP-A COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INNER KINETOCHORE SUBUNIT MIF2;
COMPND 3 CHAIN: C;
COMPND 4 SYNONYM: CENP-C HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK
COMPND 5 PROTEIN MIF2,MITOTIC FIDELITY OF CHROMOSOME TRANSMISSION PROTEIN 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (125-MER);
COMPND 9 CHAIN: G;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: INNER KINETOCHORE SUBUNIT MCM16;
COMPND 13 CHAIN: H;
COMPND 14 SYNONYM: CENP-H HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK
COMPND 15 PROTEIN MCM16,MINICHROMOSOME MAINTENANCE PROTEIN 16;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: INNER KINETOCHORE SUBUNIT CTF3;
COMPND 19 CHAIN: I;
COMPND 20 SYNONYM: CENP-I HOMOLOG,CHROMOSOME LOSS PROTEIN 3,CHROMOSOME
COMPND 21 TRANSMISSION FIDELITY PROTEIN 3,CONSTITUTIVE CENTROMERE-ASSOCIATED
COMPND 22 NETWORK PROTEIN CTF3;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: DNA (125-MER);
COMPND 26 CHAIN: J;
COMPND 27 ENGINEERED: YES;
COMPND 28 MOL_ID: 6;
COMPND 29 MOLECULE: INNER KINETOCHORE SUBUNIT MCM22;
COMPND 30 CHAIN: K;
COMPND 31 SYNONYM: CENP-K HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK
COMPND 32 PROTEIN MCM22,MINICHROMOSOME MAINTENANCE PROTEIN 22;
COMPND 33 ENGINEERED: YES;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: INNER KINETOCHORE SUBUNIT IML3;
COMPND 36 CHAIN: L;
COMPND 37 SYNONYM: CENP-L HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK
COMPND 38 PROTEIN IML3,INCREASED MINICHROMOSOME LOSS PROTEIN 3,MINICHROMOSOME
COMPND 39 MAINTENANCE PROTEIN 19;
COMPND 40 ENGINEERED: YES;
COMPND 41 MOL_ID: 8;
COMPND 42 MOLECULE: INNER KINETOCHORE SUBUNIT CHL4;
COMPND 43 CHAIN: N;
COMPND 44 SYNONYM: CENP-N HOMOLOG,CHROMOSOME LOSS PROTEIN 4,CHROMOSOME
COMPND 45 TRANSMISSION FIDELITY PROTEIN 17,CONSTITUTIVE CENTROMERE-ASSOCIATED
COMPND 46 NETWORK PROTEIN CHL4,MINICHROMOSOME MAINTENANCE PROTEIN 17;
COMPND 47 ENGINEERED: YES;
COMPND 48 MOL_ID: 9;
COMPND 49 MOLECULE: INNER KINETOCHORE SUBUNIT MCM21;
COMPND 50 CHAIN: O;
COMPND 51 SYNONYM: CENP-O HOMOLOG,CHROMOSOME TRANSMISSION FIDELITY PROTEIN 5,
COMPND 52 CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK PROTEIN MCM21,
COMPND 53 MINICHROMOSOME MAINTENANCE PROTEIN 21;
COMPND 54 ENGINEERED: YES;
COMPND 55 MOL_ID: 10;
COMPND 56 MOLECULE: INNER KINETOCHORE SUBUNIT CTF19;
COMPND 57 CHAIN: P;
COMPND 58 SYNONYM: CENP-P HOMOLOG,CHROMOSOME TRANSMISSION FIDELITY PROTEIN 19,
COMPND 59 CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK PROTEIN CTF19,
COMPND 60 MINICHROMOSOME MAINTENANCE PROTEIN 18;
COMPND 61 ENGINEERED: YES;
COMPND 62 MOL_ID: 11;
COMPND 63 MOLECULE: INNER KINETOCHORE SUBUNIT OKP1;
COMPND 64 CHAIN: Q;
COMPND 65 SYNONYM: CENP-Q HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK
COMPND 66 PROTEIN OKP1,OUTER KINETOCHORE PROTEIN 1;
COMPND 67 ENGINEERED: YES;
COMPND 68 MOL_ID: 12;
COMPND 69 MOLECULE: INNER KINETOCHORE SUBUNIT AME1;
COMPND 70 CHAIN: U;
COMPND 71 SYNONYM: ASSOCIATED WITH MICROTUBULES AND ESSENTIAL PROTEIN 1,CENP-U
COMPND 72 HOMOLOG,CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK PROTEIN AME1;
COMPND 73 ENGINEERED: YES;
COMPND 74 MOL_ID: 13;
COMPND 75 MOLECULE: INNER KINETOCHORE SUBUNIT NKP1;
COMPND 76 CHAIN: Y;
COMPND 77 SYNONYM: CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK PROTEIN NKP1,NON-
COMPND 78 ESSENTIAL KINETOCHORE PROTEIN 1;
COMPND 79 ENGINEERED: YES;
COMPND 80 MOL_ID: 14;
COMPND 81 MOLECULE: INNER KINETOCHORE SUBUNIT NKP2;
COMPND 82 CHAIN: Z;
COMPND 83 SYNONYM: CONSTITUTIVE CENTROMERE-ASSOCIATED NETWORK PROTEIN NKP2,NON-
COMPND 84 ESSENTIAL KINETOCHORE PROTEIN 2;
COMPND 85 ENGINEERED: YES;
COMPND 86 MOL_ID: 15;
COMPND 87 MOLECULE: HISTONE H3-LIKE CENTROMERIC PROTEIN CSE4;
COMPND 88 CHAIN: a;
COMPND 89 SYNONYM: CENP-A HOMOLOG,CHROMOSOME SEGREGATION PROTEIN 4;
COMPND 90 ENGINEERED: YES;
COMPND 91 MOL_ID: 16;
COMPND 92 MOLECULE: HISTONE H4;
COMPND 93 CHAIN: b, f;
COMPND 94 ENGINEERED: YES;
COMPND 95 MOL_ID: 17;
COMPND 96 MOLECULE: HISTONE H2B.2;
COMPND 97 CHAIN: d;
COMPND 98 ENGINEERED: YES;
COMPND 99 MOL_ID: 18;
COMPND 100 MOLECULE: HISTONE H3-LIKE CENTROMERIC PROTEIN CSE4;
COMPND 101 CHAIN: e;
COMPND 102 SYNONYM: CENP-A HOMOLOG,CHROMOSOME SEGREGATION PROTEIN 4;
COMPND 103 ENGINEERED: YES;
COMPND 104 MOL_ID: 19;
COMPND 105 MOLECULE: HISTONE H2A.1;
COMPND 106 CHAIN: g;
COMPND 107 ENGINEERED: YES;
COMPND 108 MOL_ID: 20;
COMPND 109 MOLECULE: HISTONE H2B.1;
COMPND 110 CHAIN: h;
COMPND 111 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;
COMPND 112 ENGINEERED: YES;
COMPND 113 MOL_ID: 21;
COMPND 114 MOLECULE: HISTONE H2A.1;
COMPND 115 CHAIN: i;
COMPND 116 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: MIF2, YKL089W;
SOURCE 8 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 13 ORGANISM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 18 S288C);
SOURCE 19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 20 ORGANISM_TAXID: 559292;
SOURCE 21 STRAIN: ATCC 204508 / S288C;
SOURCE 22 GENE: MCM16, YPR046W;
SOURCE 23 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 25 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 26 MOL_ID: 4;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 28 S288C);
SOURCE 29 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 30 ORGANISM_TAXID: 559292;
SOURCE 31 STRAIN: ATCC 204508 / S288C;
SOURCE 32 GENE: CTF3, CHL3, YLR381W;
SOURCE 33 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 35 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 36 MOL_ID: 5;
SOURCE 37 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 38 ORGANISM_TAXID: 562;
SOURCE 39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 40 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 41 MOL_ID: 6;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 43 S288C);
SOURCE 44 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 45 ORGANISM_TAXID: 559292;
SOURCE 46 STRAIN: ATCC 204508 / S288C;
SOURCE 47 GENE: MCM22, YJR135C, J2122;
SOURCE 48 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 49 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 50 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 51 MOL_ID: 7;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 53 S288C);
SOURCE 54 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 55 ORGANISM_TAXID: 559292;
SOURCE 56 STRAIN: ATCC 204508 / S288C;
SOURCE 57 GENE: IML3, MCM19, YBR107C, YBR0836;
SOURCE 58 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 59 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 60 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 61 MOL_ID: 8;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 63 S288C);
SOURCE 64 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 65 ORGANISM_TAXID: 559292;
SOURCE 66 STRAIN: ATCC 204508 / S288C;
SOURCE 67 GENE: CHL4, CTF17, MCM17, YDR254W, YD9320A.04;
SOURCE 68 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 69 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 70 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 71 MOL_ID: 9;
SOURCE 72 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 73 S288C);
SOURCE 74 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 75 ORGANISM_TAXID: 559292;
SOURCE 76 STRAIN: ATCC 204508 / S288C;
SOURCE 77 GENE: MCM21, CTF5, YDR318W;
SOURCE 78 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 79 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 80 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 81 MOL_ID: 10;
SOURCE 82 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 83 S288C);
SOURCE 84 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 85 ORGANISM_TAXID: 559292;
SOURCE 86 STRAIN: ATCC 204508 / S288C;
SOURCE 87 GENE: CTF19, MCM18, YPL018W, LPB13W;
SOURCE 88 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 89 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 90 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 91 MOL_ID: 11;
SOURCE 92 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 93 S288C);
SOURCE 94 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 95 ORGANISM_TAXID: 559292;
SOURCE 96 STRAIN: ATCC 204508 / S288C;
SOURCE 97 GENE: OKP1, YGR179C;
SOURCE 98 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 99 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 100 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 101 MOL_ID: 12;
SOURCE 102 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 103 S288C);
SOURCE 104 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 105 ORGANISM_TAXID: 559292;
SOURCE 106 STRAIN: ATCC 204508 / S288C;
SOURCE 107 GENE: AME1, ARP100, YBR211C, YBR1458;
SOURCE 108 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 109 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 110 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 111 MOL_ID: 13;
SOURCE 112 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 113 S288C);
SOURCE 114 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 115 ORGANISM_TAXID: 559292;
SOURCE 116 STRAIN: ATCC 204508 / S288C;
SOURCE 117 GENE: NKP1, YDR383C;
SOURCE 118 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 119 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 120 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 121 MOL_ID: 14;
SOURCE 122 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 123 S288C);
SOURCE 124 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 125 ORGANISM_TAXID: 559292;
SOURCE 126 STRAIN: ATCC 204508 / S288C;
SOURCE 127 GENE: NKP2, YLR315W;
SOURCE 128 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 129 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 130 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 131 MOL_ID: 15;
SOURCE 132 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 133 S288C);
SOURCE 134 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 135 ORGANISM_TAXID: 559292;
SOURCE 136 STRAIN: ATCC 204508 / S288C;
SOURCE 137 GENE: CSE4, CSL2, YKL049C, YKL262;
SOURCE 138 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 139 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 140 MOL_ID: 16;
SOURCE 141 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 142 S288C);
SOURCE 143 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 144 ORGANISM_TAXID: 559292;
SOURCE 145 STRAIN: ATCC 204508 / S288C;
SOURCE 146 GENE: HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752;
SOURCE 147 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 148 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 149 MOL_ID: 17;
SOURCE 150 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 151 S288C);
SOURCE 152 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 153 ORGANISM_TAXID: 559292;
SOURCE 154 STRAIN: ATCC 204508 / S288C;
SOURCE 155 GENE: HTB2, H2B2, YBL002W, YBL0104;
SOURCE 156 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 157 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 158 MOL_ID: 18;
SOURCE 159 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 160 S288C);
SOURCE 161 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 162 ORGANISM_TAXID: 559292;
SOURCE 163 STRAIN: ATCC 204508 / S288C;
SOURCE 164 GENE: CSE4, CSL2, YKL049C, YKL262;
SOURCE 165 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 166 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 167 MOL_ID: 19;
SOURCE 168 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 169 S288C);
SOURCE 170 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 171 ORGANISM_TAXID: 559292;
SOURCE 172 STRAIN: ATCC 204508 / S288C;
SOURCE 173 GENE: HTA1, H2A1, SPT11, YDR225W, YD9934.10;
SOURCE 174 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 175 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 176 MOL_ID: 20;
SOURCE 177 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 178 S288C);
SOURCE 179 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 180 ORGANISM_TAXID: 559292;
SOURCE 181 STRAIN: ATCC 204508 / S288C;
SOURCE 182 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;
SOURCE 183 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 184 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 185 MOL_ID: 21;
SOURCE 186 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 187 S288C);
SOURCE 188 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 189 ORGANISM_TAXID: 559292;
SOURCE 190 STRAIN: ATCC 204508 / S288C;
SOURCE 191 GENE: HTA1, H2A1, SPT11, YDR225W, YD9934.10;
SOURCE 192 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 193 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INNER KINETOCHORE, DNA, NUCLEOSOME, DNA BINDING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR K.YAN,J.YANG,Z.ZHANG,S.H.MCLAUGHLIN,L.CHANG,D.FASCI,A.J.R.HECK,
AUTHOR 2 D.BARFORD
REVDAT 3 27-NOV-19 6QLD 1 JRNL
REVDAT 2 16-OCT-19 6QLD 1 JRNL
REVDAT 1 02-OCT-19 6QLD 0
JRNL AUTH K.YAN,J.YANG,Z.ZHANG,S.H.MCLAUGHLIN,L.CHANG,D.FASCI,
JRNL AUTH 2 A.E.EHRENHOFER-MURRAY,A.J.R.HECK,D.BARFORD
JRNL TITL STRUCTURE OF THE INNER KINETOCHORE CCAN COMPLEX ASSEMBLED
JRNL TITL 2 ONTO A CENTROMERIC NUCLEOSOME.
JRNL REF NATURE V. 574 278 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 31578520
JRNL DOI 10.1038/S41586-019-1609-1
REMARK 2
REMARK 2 RESOLUTION. 4.15 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) : 4.150
REMARK 3 NUMBER OF PARTICLES : 145783
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 6QLD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1292100234.
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 : INNER KINETOCHORE CCAN COMPLEX
REMARK 245 ASSEMBLED ONTO A CENTROMERIC
REMARK 245 NUCLEOSOME; KINETOCHORE; DNA;
REMARK 245 HISTONES
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
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 : FEI FALCON III (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) : 32.00
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: 22-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 22-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 109030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 183540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -787.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, H, I, J, K, L, N, O, P,
REMARK 350 AND CHAINS: Q, U, Y, Z, a, b, d, e, f,
REMARK 350 AND CHAINS: g, h, i
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 HIS H 41
REMARK 465 ALA H 42
REMARK 465 VAL H 43
REMARK 465 ILE H 44
REMARK 465 LYS H 75
REMARK 465 PRO H 76
REMARK 465 ASP H 77
REMARK 465 ASN H 78
REMARK 465 MET I 331
REMARK 465 SER I 332
REMARK 465 ARG I 333
REMARK 465 HIS I 452
REMARK 465 ASP I 453
REMARK 465 THR I 526
REMARK 465 LYS I 527
REMARK 465 SER I 528
REMARK 465 ASP I 529
REMARK 465 TYR I 530
REMARK 465 ALA I 531
REMARK 465 LYS I 595A
REMARK 465 VAL I 595B
REMARK 465 LEU I 595C
REMARK 465 SER I 595D
REMARK 465 SER I 595E
REMARK 465 ILE I 620
REMARK 465 PRO I 621
REMARK 465 THR I 622
REMARK 465 ALA I 623
REMARK 465 ASP I 624
REMARK 465 ILE I 633
REMARK 465 THR I 634
REMARK 465 GLY I 635
REMARK 465 ILE I 636
REMARK 465 PRO I 637
REMARK 465 LYS I 657
REMARK 465 ILE I 658
REMARK 465 LYS I 659
REMARK 465 PHE I 660
REMARK 465 THR I 661
REMARK 465 SER I 662
REMARK 465 GLY I 663
REMARK 465 HIS I 677
REMARK 465 HIS I 678
REMARK 465 ASP I 679
REMARK 465 GLU I 680
REMARK 465 ILE I 681
REMARK 465 GLY I 682
REMARK 465 GLN I 683
REMARK 465 HIS I 684
REMARK 465 GLY I 685
REMARK 465 TRP I 686
REMARK 465 ILE I 687
REMARK 465 LYS I 688
REMARK 465 GLY I 689
REMARK 465 ASP K 42
REMARK 465 THR K 43
REMARK 465 GLU K 44
REMARK 465 GLY K 45
REMARK 465 LYS K 46
REMARK 465 PRO K 47
REMARK 465 VAL K 48
REMARK 465 ASN K 49
REMARK 465 MET K 61
REMARK 465 PHE K 62
REMARK 465 PHE K 63
REMARK 465 SER K 64
REMARK 465 GLU K 65
REMARK 465 ARG K 66
REMARK 465 ALA K 67
REMARK 465 ASP K 68
REMARK 465 PHE N 47
REMARK 465 ASP N 48
REMARK 465 GLY N 49
REMARK 465 ASP N 50
REMARK 465 PRO N 81
REMARK 465 ASP N 82
REMARK 465 ASN N 166
REMARK 465 LEU N 167
REMARK 465 PHE N 168
REMARK 465 LEU N 169
REMARK 465 SER N 170
REMARK 465 THR N 171
REMARK 465 PRO N 172
REMARK 465 ASN N 173
REMARK 465 ILE N 174
REMARK 465 GLY N 175
REMARK 465 SER N 176
REMARK 465 ILE N 177
REMARK 465 ASN N 178
REMARK 465 LYS N 179
REMARK 465 GLU N 180
REMARK 465 SER N 181
REMARK 465 LEU N 182
REMARK 465 TYR N 183
REMARK 465 ASN N 184
REMARK 465 LYS N 185
REMARK 465 LEU N 186
REMARK 465 ASP N 187
REMARK 465 LYS N 188
REMARK 465 PHE N 189
REMARK 465 GLN N 190
REMARK 465 GLY N 191
REMARK 465 LYS N 192
REMARK 465 ASP N 310
REMARK 465 GLU N 311
REMARK 465 ASN N 312
REMARK 465 PHE N 313
REMARK 465 TYR N 314
REMARK 465 GLY N 315
REMARK 465 LYS N 316
REMARK 465 ASN N 338
REMARK 465 GLY N 339
REMARK 465 VAL N 340
REMARK 465 MET N 341
REMARK 465 ASP N 342
REMARK 465 GLN N 343
REMARK 465 LYS N 344
REMARK 465 TYR N 345
REMARK 465 ASN N 346
REMARK 465 ASP N 347
REMARK 465 LEU N 348
REMARK 465 LYS N 349
REMARK 465 GLU N 350
REMARK 465 PHE N 351
REMARK 465 ASN N 352
REMARK 465 GLU N 353
REMARK 465 HIS N 354
REMARK 465 VAL N 355
REMARK 465 HIS N 356
REMARK 465 ASN N 357
REMARK 465 ILE N 358
REMARK 465 ARG N 359
REMARK 465 ASN N 360
REMARK 465 GLY N 361
REMARK 465 LYS N 362
REMARK 465 LYS N 363
REMARK 465 ASN N 364
REMARK 465 GLU N 365
REMARK 465 ASP N 366
REMARK 465 SER N 367
REMARK 465 GLY N 368
REMARK 465 GLU N 369
REMARK 465 PRO N 370
REMARK 465 VAL N 371
REMARK 465 TYR N 372
REMARK 465 ILE N 373
REMARK 465 ASP O 332
REMARK 465 ILE O 333
REMARK 465 HIS O 334
REMARK 465 ASP O 335
REMARK 465 PHE O 336
REMARK 465 SER O 337
REMARK 465 GLN O 338
REMARK 465 SER P 111
REMARK 465 SER P 112
REMARK 465 SER P 113
REMARK 465 ASN P 114
REMARK 465 PRO P 115
REMARK 465 ASN P 116
REMARK 465 SER P 117
REMARK 465 ALA P 118
REMARK 465 ILE P 119
REMARK 465 SER P 120
REMARK 465 ASP P 121
REMARK 465 ARG P 122
REMARK 465 LYS P 123
REMARK 465 ASN P 177
REMARK 465 ASP P 178
REMARK 465 ILE P 286
REMARK 465 ARG P 287
REMARK 465 GLU P 288
REMARK 465 GLY P 289
REMARK 465 ARG P 290
REMARK 465 LEU P 291
REMARK 465 THR P 292
REMARK 465 ARG P 308
REMARK 465 GLY P 309
REMARK 465 LYS P 310
REMARK 465 PRO P 311
REMARK 465 ARG P 312
REMARK 465 ASN P 313
REMARK 465 GLY Q 191
REMARK 465 ASP Q 192
REMARK 465 GLN Q 220
REMARK 465 ALA Q 221
REMARK 465 LYS Q 222
REMARK 465 PHE Q 223
REMARK 465 PRO Q 224
REMARK 465 SER Q 225
REMARK 465 ARG Q 226
REMARK 465 ILE Q 227
REMARK 465 SER Q 228
REMARK 465 MET Q 304
REMARK 465 GLU Q 305
REMARK 465 TYR Q 306
REMARK 465 THR Q 307
REMARK 465 TYR Q 308
REMARK 465 GLY Q 309
REMARK 465 LEU Q 310
REMARK 465 GLU Q 311
REMARK 465 SER Q 312
REMARK 465 THR Q 313
REMARK 465 ASN Q 314
REMARK 465 GLY Q 315
REMARK 465 PHE Q 316
REMARK 465 MET Q 317
REMARK 465 HIS Q 318
REMARK 465 PRO Q 319
REMARK 465 ASP U 157
REMARK 465 PHE U 158
REMARK 465 ASN U 159
REMARK 465 LYS U 160
REMARK 465 SER U 161
REMARK 465 ASP U 162
REMARK 465 ASP U 163
REMARK 465 ASP U 164
REMARK 465 GLN U 165
REMARK 465 TYR U 267
REMARK 465 GLU U 268
REMARK 465 GLY U 269
REMARK 465 ASP U 270
REMARK 465 ARG U 271
REMARK 465 LYS U 272
REMARK 465 ILE U 273
REMARK 465 MET U 274
REMARK 465 SER U 275
REMARK 465 GLN U 276
REMARK 465 GLU Y 33
REMARK 465 LEU Y 34
REMARK 465 GLU Y 124
REMARK 465 VAL Y 125
REMARK 465 ALA Y 126
REMARK 465 ASP Y 127
REMARK 465 GLU Y 128
REMARK 465 GLU Y 129
REMARK 465 GLU Y 130
REMARK 465 VAL Y 131
REMARK 465 GLU Y 132
REMARK 465 VAL Y 133
REMARK 465 GLU Y 134
REMARK 465 ASN Y 135
REMARK 465 PHE Z 25
REMARK 465 LYS Z 26
REMARK 465 GLN Z 27
REMARK 465 GLN Z 28
REMARK 465 LEU Z 29
REMARK 465 GLN Z 30
REMARK 465 SER Z 31
REMARK 465 TYR Z 32
REMARK 465 THR Z 33
REMARK 465 SER Z 34
REMARK 465 ASP Z 35
REMARK 465 THR a 171
REMARK 465 LYS a 172
REMARK 465 ASP a 173
REMARK 465 LYS e 131
REMARK 465 TYR e 132
REMARK 465 THR e 133
REMARK 465 PRO e 134
REMARK 465 SER e 135
REMARK 465 GLU e 136
REMARK 465 THR e 171
REMARK 465 LYS e 172
REMARK 465 ASP e 173
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 GLU H 6 CG CD OE1 OE2
REMARK 470 LYS H 7 CG CD CE NZ
REMARK 470 GLN H 8 CG CD OE1 NE2
REMARK 470 GLU H 16 CG CD OE1 OE2
REMARK 470 GLU H 18 CG CD OE1 OE2
REMARK 470 GLU H 21 CG CD OE1 OE2
REMARK 470 GLU H 25 CG CD OE1 OE2
REMARK 470 ASP H 31 CG OD1 OD2
REMARK 470 ARG H 32 CG CD NE CZ NH1 NH2
REMARK 470 ARG H 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 38 CG CD CE NZ
REMARK 470 HIS H 39 CG ND1 CD2 CE1 NE2
REMARK 470 ASN H 40 CG OD1 ND2
REMARK 470 LEU H 45 CG CD1 CD2
REMARK 470 GLU H 64 CG CD OE1 OE2
REMARK 470 GLU H 74 CG CD OE1 OE2
REMARK 470 THR H 79 OG1 CG2
REMARK 470 ASN H 80 CG OD1 ND2
REMARK 470 VAL H 81 CG1 CG2
REMARK 470 LYS H 85 CG CD CE NZ
REMARK 470 GLU H 92 CG CD OE1 OE2
REMARK 470 ASP H 97 CG OD1 OD2
REMARK 470 GLU H 99 CG CD OE1 OE2
REMARK 470 GLU H 116 CG CD OE1 OE2
REMARK 470 GLU H 123 CG CD OE1 OE2
REMARK 470 GLU H 130 CG CD OE1 OE2
REMARK 470 PRO H 136 CG CD
REMARK 470 ASN I 321 CG OD1 ND2
REMARK 470 SER I 322 OG
REMARK 470 ASN I 323 CG OD1 ND2
REMARK 470 VAL I 324 CG1 CG2
REMARK 470 LEU I 325 CG CD1 CD2
REMARK 470 LEU I 326 CG CD1 CD2
REMARK 470 PRO I 327 CG CD
REMARK 470 ARG I 328 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 329 CG CD CE NZ
REMARK 470 VAL I 330 CG1 CG2
REMARK 470 ASP I 334 CG OD1 OD2
REMARK 470 LYS I 337 CG CD CE NZ
REMARK 470 LYS I 347 CG CD CE NZ
REMARK 470 ASP I 351 CG OD1 OD2
REMARK 470 GLU I 352 CG CD OE1 OE2
REMARK 470 GLU I 358 CG CD OE1 OE2
REMARK 470 GLU I 373 CG CD OE1 OE2
REMARK 470 GLU I 377 CG CD OE1 OE2
REMARK 470 ASP I 409 CG OD1 OD2
REMARK 470 LYS I 425 CG CD CE NZ
REMARK 470 GLU I 427 CG CD OE1 OE2
REMARK 470 LEU I 428 CG CD1 CD2
REMARK 470 ILE I 429 CG1 CG2 CD1
REMARK 470 ARG I 449 CG CD NE CZ NH1 NH2
REMARK 470 ASP I 450 CG OD1 OD2
REMARK 470 ASN I 454 CG OD1 ND2
REMARK 470 ASN I 455 CG OD1 ND2
REMARK 470 GLU I 460 CG CD OE1 OE2
REMARK 470 ASP I 475 CG OD1 OD2
REMARK 470 ASP I 476 CG OD1 OD2
REMARK 470 ASN I 500 CG OD1 ND2
REMARK 470 ASN I 501 CG OD1 ND2
REMARK 470 THR I 503 OG1 CG2
REMARK 470 ILE I 532 CG1 CG2 CD1
REMARK 470 ASP I 549 CG OD1 OD2
REMARK 470 ASP I 550 CG OD1 OD2
REMARK 470 LYS I 565 CG CD CE NZ
REMARK 470 LYS I 567 CG CD CE NZ
REMARK 470 GLN I 570 CG CD OE1 NE2
REMARK 470 LYS I 576 CG CD CE NZ
REMARK 470 ARG I 579 CG CD NE CZ NH1 NH2
REMARK 470 GLN I 581 CG CD OE1 NE2
REMARK 470 ASP I 587 CG OD1 OD2
REMARK 470 LYS I 596 CG CD CE NZ
REMARK 470 SER I 602 OG
REMARK 470 LEU I 603 CG CD1 CD2
REMARK 470 ASP I 609 CG OD1 OD2
REMARK 470 GLU I 616 CG CD OE1 OE2
REMARK 470 TYR I 619 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE I 625 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS I 626 CG CD CE NZ
REMARK 470 LYS I 629 CG CD CE NZ
REMARK 470 ARG I 648 CG CD NE CZ NH1 NH2
REMARK 470 GLU I 651 CG CD OE1 OE2
REMARK 470 GLU I 654 CG CD OE1 OE2
REMARK 470 ILE I 664 CG1 CG2 CD1
REMARK 470 ILE I 665 CG1 CG2 CD1
REMARK 470 ASN I 666 CG OD1 ND2
REMARK 470 GLU I 667 CG CD OE1 OE2
REMARK 470 GLU I 668 CG CD OE1 OE2
REMARK 470 THR I 669 OG1 CG2
REMARK 470 PHE I 670 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN I 671 CG OD1 ND2
REMARK 470 ASN I 672 CG OD1 ND2
REMARK 470 PHE I 673 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE I 674 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG I 675 CG CD NE CZ NH1 NH2
REMARK 470 VAL I 676 CG1 CG2
REMARK 470 ASP I 695 CG OD1 OD2
REMARK 470 LYS I 699 CG CD CE NZ
REMARK 470 TYR I 728 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP K 9 CG OD1 OD2
REMARK 470 TYR K 11 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS K 13 CG CD CE NZ
REMARK 470 GLU K 16 CG CD OE1 OE2
REMARK 470 ASN K 17 CG OD1 ND2
REMARK 470 GLN K 18 CG CD OE1 NE2
REMARK 470 TYR K 24 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS K 27 CG CD CE NZ
REMARK 470 GLN K 30 CG CD OE1 NE2
REMARK 470 ASP K 34 CG OD1 OD2
REMARK 470 LYS K 38 CG CD CE NZ
REMARK 470 ARG K 39 CG CD NE CZ NH1 NH2
REMARK 470 SER K 40 OG
REMARK 470 LEU K 41 CG CD1 CD2
REMARK 470 GLU K 51 CG CD OE1 OE2
REMARK 470 GLU K 55 CG CD OE1 OE2
REMARK 470 LYS K 59 CG CD CE NZ
REMARK 470 GLU K 88 CG CD OE1 OE2
REMARK 470 LYS K 115 CG CD CE NZ
REMARK 470 GLU K 116 CG CD OE1 OE2
REMARK 470 MET K 128 CG SD CE
REMARK 470 GLU L 138 CG CD OE1 OE2
REMARK 470 ASP N 16 CG OD1 OD2
REMARK 470 ILE N 51 CG1 CG2 CD1
REMARK 470 TYR N 52 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU N 53 CG CD1 CD2
REMARK 470 GLU N 56 CG CD OE1 OE2
REMARK 470 LEU N 61 CG CD1 CD2
REMARK 470 GLU N 63 CG CD OE1 OE2
REMARK 470 LYS N 64 CG CD CE NZ
REMARK 470 TRP N 80 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP N 80 CZ3 CH2
REMARK 470 GLN N 88 CG CD OE1 NE2
REMARK 470 LYS N 117 CG CD CE NZ
REMARK 470 LYS N 127 CG CD CE NZ
REMARK 470 ASP N 218 CG OD1 OD2
REMARK 470 GLU N 301 CG CD OE1 OE2
REMARK 470 ASP N 303 CG OD1 OD2
REMARK 470 ASP N 304 CG OD1 OD2
REMARK 470 ASP N 309 CG OD1 OD2
REMARK 470 GLU N 317 CG CD OE1 OE2
REMARK 470 GLU N 318 CG CD OE1 OE2
REMARK 470 GLU N 320 CG CD OE1 OE2
REMARK 470 GLU N 327 CG CD OE1 OE2
REMARK 470 GLU N 450 CG CD OE1 OE2
REMARK 470 GLN N 451 CG CD OE1 NE2
REMARK 470 ASP O 156 CG OD1 OD2
REMARK 470 ASP O 190 CG OD1 OD2
REMARK 470 ARG O 212 CG CD NE CZ NH1 NH2
REMARK 470 LYS O 229 CG CD CE NZ
REMARK 470 ASP O 331 CG OD1 OD2
REMARK 470 ASP O 354 CG OD1 OD2
REMARK 470 PHE O 363 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN P 97 CG CD OE1 NE2
REMARK 470 ASN P 98 CG OD1 ND2
REMARK 470 ASP P 99 CG OD1 OD2
REMARK 470 ILE P 100 CG1 CG2 CD1
REMARK 470 THR P 101 OG1 CG2
REMARK 470 GLN P 102 CG CD OE1 NE2
REMARK 470 ASP P 103 CG OD1 OD2
REMARK 470 PHE P 104 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU P 105 CG CD1 CD2
REMARK 470 ASN P 106 CG OD1 ND2
REMARK 470 LEU P 107 CG CD1 CD2
REMARK 470 ILE P 108 CG1 CG2 CD1
REMARK 470 SER P 109 OG
REMARK 470 ILE P 110 CG1 CG2 CD1
REMARK 470 ARG P 124 CG CD NE CZ NH1 NH2
REMARK 470 HIS P 176 CG ND1 CD2 CE1 NE2
REMARK 470 GLU P 181 CG CD OE1 OE2
REMARK 470 MET P 194 CG SD CE
REMARK 470 ASN P 195 CG OD1 ND2
REMARK 470 GLU P 198 CG CD OE1 OE2
REMARK 470 LYS P 266 CG CD CE NZ
REMARK 470 ARG P 267 CG CD NE CZ NH1 NH2
REMARK 470 ASP P 278 CG OD1 OD2
REMARK 470 GLU P 283 CG CD OE1 OE2
REMARK 470 ARG P 284 CG CD NE CZ NH1 NH2
REMARK 470 THR P 293 OG1 CG2
REMARK 470 LYS P 295 CG CD CE NZ
REMARK 470 GLU P 307 CG CD OE1 OE2
REMARK 470 LYS P 327 CG CD CE NZ
REMARK 470 GLU P 330 CG CD OE1 OE2
REMARK 470 ASP P 338 CG OD1 OD2
REMARK 470 GLU P 339 CG CD OE1 OE2
REMARK 470 GLU P 356 CG CD OE1 OE2
REMARK 470 PHE P 363 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 PRO P 364 CG CD
REMARK 470 ASP P 365 CG OD1 OD2
REMARK 470 MET P 366 CG SD CE
REMARK 470 SER Q 161 OG
REMARK 470 ILE Q 162 CG1 CG2 CD1
REMARK 470 LEU Q 163 CG CD1 CD2
REMARK 470 ARG Q 164 CG CD NE CZ NH1 NH2
REMARK 470 LEU Q 165 CG CD1 CD2
REMARK 470 LEU Q 166 CG CD1 CD2
REMARK 470 GLU Q 167 CG CD OE1 OE2
REMARK 470 THR Q 168 OG1 CG2
REMARK 470 ASN Q 169 CG OD1 ND2
REMARK 470 THR Q 170 OG1 CG2
REMARK 470 VAL Q 171 CG1 CG2
REMARK 470 SER Q 172 OG
REMARK 470 LEU Q 174 CG CD1 CD2
REMARK 470 ASP Q 175 CG OD1 OD2
REMARK 470 SER Q 176 OG
REMARK 470 VAL Q 177 CG1 CG2
REMARK 470 PHE Q 178 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU Q 179 CG CD OE1 OE2
REMARK 470 LYS Q 180 CG CD CE NZ
REMARK 470 TYR Q 181 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU Q 182 CG CD OE1 OE2
REMARK 470 LYS Q 183 CG CD CE NZ
REMARK 470 GLU Q 184 CG CD OE1 OE2
REMARK 470 MET Q 185 CG SD CE
REMARK 470 ASN Q 186 CG OD1 ND2
REMARK 470 GLN Q 187 CG CD OE1 NE2
REMARK 470 MET Q 188 CG SD CE
REMARK 470 THR Q 189 OG1 CG2
REMARK 470 HIS Q 190 CG ND1 CD2 CE1 NE2
REMARK 470 ASN Q 193 CG OD1 ND2
REMARK 470 ASN Q 194 CG OD1 ND2
REMARK 470 GLU Q 195 CG CD OE1 OE2
REMARK 470 VAL Q 196 CG1 CG2
REMARK 470 LYS Q 197 CG CD CE NZ
REMARK 470 ARG Q 198 CG CD NE CZ NH1 NH2
REMARK 470 ILE Q 199 CG1 CG2 CD1
REMARK 470 TYR Q 200 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER Q 201 OG
REMARK 470 LYS Q 202 CG CD CE NZ
REMARK 470 LYS Q 203 CG CD CE NZ
REMARK 470 GLU Q 204 CG CD OE1 OE2
REMARK 470 ARG Q 205 CG CD NE CZ NH1 NH2
REMARK 470 LEU Q 206 CG CD1 CD2
REMARK 470 LEU Q 207 CG CD1 CD2
REMARK 470 GLU Q 208 CG CD OE1 OE2
REMARK 470 ILE Q 209 CG1 CG2 CD1
REMARK 470 ILE Q 210 CG1 CG2 CD1
REMARK 470 LEU Q 211 CG CD1 CD2
REMARK 470 THR Q 212 OG1 CG2
REMARK 470 LYS Q 213 CG CD CE NZ
REMARK 470 ILE Q 214 CG1 CG2 CD1
REMARK 470 LYS Q 215 CG CD CE NZ
REMARK 470 LYS Q 216 CG CD CE NZ
REMARK 470 LYS Q 217 CG CD CE NZ
REMARK 470 LEU Q 218 CG CD1 CD2
REMARK 470 ARG Q 219 CG CD NE CZ NH1 NH2
REMARK 470 GLU Q 229 CG CD OE1 OE2
REMARK 470 ARG Q 230 CG CD NE CZ NH1 NH2
REMARK 470 ASP Q 231 CG OD1 OD2
REMARK 470 ASP Q 233 CG OD1 OD2
REMARK 470 GLN Q 293 CG CD OE1 NE2
REMARK 470 ASP Q 295 CG OD1 OD2
REMARK 470 HIS Q 297 CG ND1 CD2 CE1 NE2
REMARK 470 LEU Q 300 CG CD1 CD2
REMARK 470 LYS Q 302 CG CD CE NZ
REMARK 470 ASP Q 320 CG OD1 OD2
REMARK 470 ASP Q 349 CG OD1 OD2
REMARK 470 LYS Q 350 CG CD CE NZ
REMARK 470 GLU Q 351 CG CD OE1 OE2
REMARK 470 GLU Q 352 CG CD OE1 OE2
REMARK 470 GLU Q 362 CG CD OE1 OE2
REMARK 470 LYS Q 366 CG CD CE NZ
REMARK 470 ASP Q 380 CG OD1 OD2
REMARK 470 GLU Q 383 CG CD OE1 OE2
REMARK 470 GLU Q 384 CG CD OE1 OE2
REMARK 470 GLU Q 385 CG CD OE1 OE2
REMARK 470 LYS Q 387 CG CD CE NZ
REMARK 470 GLU Q 388 CG CD OE1 OE2
REMARK 470 SER U 131 OG
REMARK 470 VAL U 132 CG1 CG2
REMARK 470 THR U 133 OG1 CG2
REMARK 470 THR U 134 OG1 CG2
REMARK 470 ILE U 135 CG1 CG2 CD1
REMARK 470 ASP U 136 CG OD1 OD2
REMARK 470 VAL U 137 CG1 CG2
REMARK 470 LEU U 138 CG CD1 CD2
REMARK 470 SER U 139 OG
REMARK 470 SER U 140 OG
REMARK 470 LEU U 141 CG CD1 CD2
REMARK 470 PHE U 142 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE U 143 CG1 CG2 CD1
REMARK 470 ASN U 144 CG OD1 ND2
REMARK 470 LEU U 145 CG CD1 CD2
REMARK 470 PHE U 146 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU U 147 CG CD OE1 OE2
REMARK 470 ASN U 148 CG OD1 ND2
REMARK 470 ASP U 149 CG OD1 OD2
REMARK 470 LEU U 150 CG CD1 CD2
REMARK 470 ILE U 151 CG1 CG2 CD1
REMARK 470 PRO U 152 CG CD
REMARK 470 GLN U 153 CG CD OE1 NE2
REMARK 470 LEU U 155 CG CD1 CD2
REMARK 470 LYS U 156 CG CD CE NZ
REMARK 470 PHE U 166 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG U 167 CG CD NE CZ NH1 NH2
REMARK 470 LYS U 168 CG CD CE NZ
REMARK 470 LEU U 169 CG CD1 CD2
REMARK 470 ASP U 174 CG OD1 OD2
REMARK 470 ASP U 183 CG OD1 OD2
REMARK 470 ASP U 188 CG OD1 OD2
REMARK 470 ASP U 194 CG OD1 OD2
REMARK 470 LYS U 207 CG CD CE NZ
REMARK 470 GLU U 214 CG CD OE1 OE2
REMARK 470 GLU U 229 CG CD OE1 OE2
REMARK 470 LYS U 234 CG CD CE NZ
REMARK 470 ASP U 235 CG OD1 OD2
REMARK 470 ASP U 238 CG OD1 OD2
REMARK 470 LYS U 266 CG CD CE NZ
REMARK 470 ASP U 277 CG OD1 OD2
REMARK 470 SER U 278 OG
REMARK 470 GLU U 279 CG CD OE1 OE2
REMARK 470 ASP U 280 CG OD1 OD2
REMARK 470 ASP U 291 CG OD1 OD2
REMARK 470 LYS U 311 CG CD CE NZ
REMARK 470 GLU U 314 CG CD OE1 OE2
REMARK 470 LEU U 316 CG CD1 CD2
REMARK 470 SER U 317 OG
REMARK 470 ASN U 318 CG OD1 ND2
REMARK 470 GLU U 319 CG CD OE1 OE2
REMARK 470 LEU U 320 CG CD1 CD2
REMARK 470 THR Y 2 OG1 CG2
REMARK 470 ASP Y 3 CG OD1 OD2
REMARK 470 ASP Y 23 CG OD1 OD2
REMARK 470 ASP Y 24 CG OD1 OD2
REMARK 470 TYR Y 25 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU Y 26 CG CD1 CD2
REMARK 470 MET Y 27 CG SD CE
REMARK 470 ASP Y 28 CG OD1 OD2
REMARK 470 ASP Y 29 CG OD1 OD2
REMARK 470 LEU Y 30 CG CD1 CD2
REMARK 470 GLU Y 37 CG CD OE1 OE2
REMARK 470 LYS Y 43 CG CD CE NZ
REMARK 470 GLN Y 45 CG CD OE1 NE2
REMARK 470 GLU Y 48 CG CD OE1 OE2
REMARK 470 LYS Y 49 CG CD CE NZ
REMARK 470 LYS Y 51 CG CD CE NZ
REMARK 470 ASP Y 52 CG OD1 OD2
REMARK 470 ASP Y 60 CG OD1 OD2
REMARK 470 GLU Y 65 CG CD OE1 OE2
REMARK 470 ASP Y 68 CG OD1 OD2
REMARK 470 SER Y 71 OG
REMARK 470 GLU Y 72 CG CD OE1 OE2
REMARK 470 GLU Y 83 CG CD OE1 OE2
REMARK 470 ASP Y 87 CG OD1 OD2
REMARK 470 GLN Y 106 CG CD OE1 NE2
REMARK 470 GLU Y 115 CG CD OE1 OE2
REMARK 470 ASP Y 116 CG OD1 OD2
REMARK 470 ASP Y 149 CG OD1 OD2
REMARK 470 GLU Y 161 CG CD OE1 OE2
REMARK 470 ASP Y 166 CG OD1 OD2
REMARK 470 GLU Y 186 CG CD OE1 OE2
REMARK 470 ASP Y 187 CG OD1 OD2
REMARK 470 ASP Y 188 CG OD1 OD2
REMARK 470 ASP Y 189 CG OD1 OD2
REMARK 470 GLU Y 192 CG CD OE1 OE2
REMARK 470 GLU Y 206 CG CD OE1 OE2
REMARK 470 GLU Y 207 CG CD OE1 OE2
REMARK 470 MET Y 208 CG SD CE
REMARK 470 LYS Y 209 CG CD CE NZ
REMARK 470 LEU Y 211 CG CD1 CD2
REMARK 470 LEU Y 212 CG CD1 CD2
REMARK 470 GLU Y 213 CG CD OE1 OE2
REMARK 470 GLU Y 214 CG CD OE1 OE2
REMARK 470 VAL Y 216 CG1 CG2
REMARK 470 LYS Y 217 CG CD CE NZ
REMARK 470 THR Y 218 OG1 CG2
REMARK 470 PHE Y 219 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN Y 221 CG OD1 ND2
REMARK 470 SER Y 222 OG
REMARK 470 PRO Y 223 CG CD
REMARK 470 GLU Y 224 CG CD OE1 OE2
REMARK 470 LYS Y 225 CG CD CE NZ
REMARK 470 ARG Y 226 CG CD NE CZ NH1 NH2
REMARK 470 GLU Y 227 CG CD OE1 OE2
REMARK 470 LYS Y 228 CG CD CE NZ
REMARK 470 ILE Y 229 CG1 CG2 CD1
REMARK 470 LYS Y 230 CG CD CE NZ
REMARK 470 LYS Y 231 CG CD CE NZ
REMARK 470 ILE Y 232 CG1 CG2 CD1
REMARK 470 LEU Y 233 CG CD1 CD2
REMARK 470 SER Y 234 OG
REMARK 470 GLU Y 235 CG CD OE1 OE2
REMARK 470 LEU Y 236 CG CD1 CD2
REMARK 470 LYS Y 237 CG CD CE NZ
REMARK 470 LYS Y 238 CG CD CE NZ
REMARK 470 ASP Z 13 CG OD1 OD2
REMARK 470 PHE Z 22 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU Z 24 CG CD OE1 OE2
REMARK 470 GLU Z 36 CG CD OE1 OE2
REMARK 470 GLN Z 37 CG CD OE1 NE2
REMARK 470 GLN Z 38 CG CD OE1 NE2
REMARK 470 LEU Z 39 CG CD1 CD2
REMARK 470 GLN Z 40 CG CD OE1 NE2
REMARK 470 HIS Z 41 CG ND1 CD2 CE1 NE2
REMARK 470 GLU Z 44 CG CD OE1 OE2
REMARK 470 LEU Z 45 CG CD1 CD2
REMARK 470 ARG Z 49 CG CD NE CZ NH1 NH2
REMARK 470 ASP Z 50 CG OD1 OD2
REMARK 470 GLU Z 56 CG CD OE1 OE2
REMARK 470 GLU Z 77 CG CD OE1 OE2
REMARK 470 GLU Z 79 CG CD OE1 OE2
REMARK 470 SER Z 84 OG
REMARK 470 GLU Z 88 CG CD OE1 OE2
REMARK 470 ASP Z 92 CG OD1 OD2
REMARK 470 ASP Z 99 CG OD1 OD2
REMARK 470 ASP Z 110 CG OD1 OD2
REMARK 470 GLU Z 114 CG CD OE1 OE2
REMARK 470 GLU Z 121 CG CD OE1 OE2
REMARK 470 GLU Z 123 CG CD OE1 OE2
REMARK 470 ASP Z 133 CG OD1 OD2
REMARK 470 ASN Z 134 CG OD1 ND2
REMARK 470 ILE Z 136 CG1 CG2 CD1
REMARK 470 PRO Z 137 CG CD
REMARK 470 LEU Z 139 CG CD1 CD2
REMARK 470 LEU Z 140 CG CD1 CD2
REMARK 470 GLN Z 141 CG CD OE1 NE2
REMARK 470 ILE Z 142 CG1 CG2 CD1
REMARK 470 ILE Z 143 CG1 CG2 CD1
REMARK 470 GLN Z 144 CG CD OE1 NE2
REMARK 470 SER Z 145 OG
REMARK 470 TYR Z 146 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE Z 147 CG1 CG2 CD1
REMARK 470 ASN Z 148 CG OD1 ND2
REMARK 470 LEU Z 149 CG CD1 CD2
REMARK 470 LEU Z 150 CG CD1 CD2
REMARK 470 GLU Z 151 CG CD OE1 OE2
REMARK 470 GLU Z 152 CG CD OE1 OE2
REMARK 470 ASN Z 153 CG OD1 ND2
REMARK 470 LEU a 137 CG CD1 CD2
REMARK 470 LYS a 215 CG CD CE NZ
REMARK 470 VAL b 55 CG1 CG2
REMARK 470 TYR d 44 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL e 112 CG1 CG2
REMARK 470 ARG e 113 CG CD NE CZ NH1 NH2
REMARK 470 GLN e 114 CG CD OE1 NE2
REMARK 470 LYS e 115 CG CD CE NZ
REMARK 470 ARG e 116 CG CD NE CZ NH1 NH2
REMARK 470 ARG e 117 CG CD NE CZ NH1 NH2
REMARK 470 GLU e 118 CG CD OE1 OE2
REMARK 470 LYS e 119 CG CD CE NZ
REMARK 470 GLN e 120 CG CD OE1 NE2
REMARK 470 ARG e 121 CG CD NE CZ NH1 NH2
REMARK 470 LYS e 122 CG CD CE NZ
REMARK 470 GLN e 123 CG CD OE1 NE2
REMARK 470 SER e 124 OG
REMARK 470 LEU e 125 CG CD1 CD2
REMARK 470 LYS e 126 CG CD CE NZ
REMARK 470 ARG e 127 CG CD NE CZ NH1 NH2
REMARK 470 VAL e 128 CG1 CG2
REMARK 470 GLU e 129 CG CD OE1 OE2
REMARK 470 LYS e 130 CG CD CE NZ
REMARK 470 LEU e 137 CG CD1 CD2
REMARK 470 LYS e 215 CG CD CE NZ
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 DG G 4 O3' DA G 5 P -0.149
REMARK 500 DT J -5 O3' DC J -4 P -0.073
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 DA G 5 O3' - P - O5' ANGL. DEV. = 17.0 DEGREES
REMARK 500 DA G 5 O3' - P - OP2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 DA G 5 O3' - P - OP1 ANGL. DEV. = -30.1 DEGREES
REMARK 500 DT G 46 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC G 47 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT G 48 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT G 105 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC G 109 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DC G 110 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC G 111 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 LEU H 82 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU I 478 CA - CB - CG ANGL. DEV. = 16.9 DEGREES
REMARK 500 DA J -48 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT J -5 C3' - O3' - P ANGL. DEV. = -13.0 DEGREES
REMARK 500 DC J -4 O3' - P - O5' ANGL. DEV. = -13.1 DEGREES
REMARK 500 LEU Q 296 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR C 297 -160.32 -125.00
REMARK 500 TRP C 298 -1.81 70.37
REMARK 500 ARG I 328 32.02 -96.44
REMARK 500 ARG I 350 -108.39 23.55
REMARK 500 ASP I 351 -23.41 69.97
REMARK 500 GLU I 352 -145.24 -147.91
REMARK 500 ASP I 389 70.31 61.74
REMARK 500 PHE I 400 -37.87 -131.10
REMARK 500 LYS I 425 73.79 48.93
REMARK 500 GLN I 533 24.85 48.78
REMARK 500 ASP I 549 51.77 -94.22
REMARK 500 ASN I 575 14.24 55.96
REMARK 500 LEU I 722 70.14 57.70
REMARK 500 PRO L 41 65.37 16.66
REMARK 500 SER L 42 -7.35 -46.56
REMARK 500 ASP L 45 49.69 -91.70
REMARK 500 ASN L 64 33.04 -93.74
REMARK 500 THR L 196 -31.13 -131.08
REMARK 500 LEU N 84 -64.72 -93.41
REMARK 500 GLU N 234 -10.57 65.66
REMARK 500 MET N 267 -8.57 66.89
REMARK 500 GLU N 318 75.09 57.94
REMARK 500 LYS N 334 -156.82 -149.06
REMARK 500 ARG N 375 -12.57 72.80
REMARK 500 SER N 378 -169.19 -79.04
REMARK 500 ASN N 394 50.55 39.80
REMARK 500 ASN N 435 60.07 36.46
REMARK 500 ASP O 185 37.25 -99.27
REMARK 500 LYS O 229 20.77 -141.15
REMARK 500 ILE O 259 -63.93 -108.37
REMARK 500 LYS O 320 -159.58 -91.44
REMARK 500 GLN O 321 93.13 -67.39
REMARK 500 THR P 144 51.71 -93.68
REMARK 500 ASN P 195 80.93 -151.58
REMARK 500 PHE P 207 -9.65 72.85
REMARK 500 MET P 274 -156.08 -148.01
REMARK 500 SER P 277 10.19 -146.37
REMARK 500 LEU U 155 32.57 -95.06
REMARK 500 MET U 299 32.80 -96.85
REMARK 500 SER Y 22 -62.04 -93.92
REMARK 500 LYS Y 49 48.12 -91.75
REMARK 500 LYS Y 51 47.96 -83.06
REMARK 500 ILE Y 88 76.28 53.48
REMARK 500 LYS Y 90 -169.37 -76.99
REMARK 500 TYR Y 91 25.46 48.38
REMARK 500 GLU Y 104 72.29 39.81
REMARK 500 ALA Z 131 40.06 -102.85
REMARK 500 MET a 218 45.11 -93.33
REMARK 500 GLN b 28 40.94 -109.44
REMARK 500 SER d 128 57.83 -95.47
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-4579 RELATED DB: EMDB
REMARK 900 STRUCTURE OF INNER KINETOCHORE CCAN-CENP-A COMPLEX
DBREF 6QLD C 284 305 UNP P35201 CENPC_YEAST 284 305
DBREF 6QLD G 2 125 PDB 6QLD 6QLD 2 125
DBREF 6QLD H 4 136 UNP Q12262 CENPH_YEAST 4 136
DBREF 6QLD I 321 728 UNP Q12748 CENPI_YEAST 321 728
DBREF 6QLD J -125 -2 PDB 6QLD 6QLD -125 -2
DBREF 6QLD K 7 128 UNP P47167 CENPK_YEAST 7 128
DBREF 6QLD L 2 242 UNP P38265 CENPL_YEAST 2 242
DBREF 6QLD N 5 451 UNP P38907 CENPN_YEAST 5 451
DBREF 6QLD O 153 364 UNP Q06675 CENPO_YEAST 153 364
DBREF 6QLD P 97 366 UNP Q02732 CENPP_YEAST 97 366
DBREF 6QLD Q 161 391 UNP P53298 CENPQ_YEAST 161 391
DBREF 6QLD U 131 320 UNP P38313 CENPU_YEAST 131 320
DBREF 6QLD Y 2 238 UNP Q12493 NKP1_YEAST 2 238
DBREF 6QLD Z 3 153 UNP Q06162 NKP2_YEAST 3 153
DBREF 6QLD a 137 226 UNP P36012 CENPA_YEAST 137 226
DBREF 6QLD b 25 103 UNP P02309 H4_YEAST 25 103
DBREF 6QLD d 37 129 UNP P02294 H2B2_YEAST 37 129
DBREF 6QLD e 112 226 UNP P36012 CENPA_YEAST 112 226
DBREF 6QLD f 25 103 UNP P02309 H4_YEAST 25 103
DBREF 6QLD g 17 121 UNP P04911 H2A1_YEAST 17 121
DBREF 6QLD h 36 129 UNP P02293 H2B1_YEAST 36 129
DBREF 6QLD i 17 118 UNP P04911 H2A1_YEAST 17 118
SEQRES 1 C 22 LEU ARG LYS SER THR ARG VAL LYS VAL ALA PRO LEU GLN
SEQRES 2 C 22 TYR TRP ARG ASN GLU LYS ILE VAL TYR
SEQRES 1 G 124 DT DC DG DA DG DA DA DT DC DC DC DG DG
SEQRES 2 G 124 DT DG DC DC DG DA DG DG DC DC DG DC DT
SEQRES 3 G 124 DC DA DA DT DT DG DG DT DC DG DT DA DG
SEQRES 4 G 124 DA DC DA DG DC DT DC DT DA DG DC DA DC
SEQRES 5 G 124 DC DG DC DT DT DA DA DA DC DG DC DA DC
SEQRES 6 G 124 DG DT DA DC DG DC DG DC DT DG DT DC DC
SEQRES 7 G 124 DC DC DC DG DC DG DT DT DT DT DA DA DC
SEQRES 8 G 124 DC DG DC DC DA DA DG DG DG DG DA DT DT
SEQRES 9 G 124 DA DC DT DC DC DC DT DA DG DT DC DT DC
SEQRES 10 G 124 DC DA DG DG DC DA DC
SEQRES 1 H 133 SER SER GLU LYS GLN TRP GLU ARG ILE GLN GLN LEU GLU
SEQRES 2 H 133 LYS GLU HIS VAL GLU VAL TYR ARG GLU LEU LEU ILE THR
SEQRES 3 H 133 LEU ASP ARG LEU TYR LEU ILE ARG LYS HIS ASN HIS ALA
SEQRES 4 H 133 VAL ILE LEU SER HIS THR GLN GLN ARG LEU LEU GLU ILE
SEQRES 5 H 133 ARG HIS GLN LEU GLN ILE ASN LEU GLU LYS THR ALA LEU
SEQRES 6 H 133 LEU ILE ARG LEU LEU GLU LYS PRO ASP ASN THR ASN VAL
SEQRES 7 H 133 LEU PHE THR LYS LEU GLN ASN LEU LEU GLU GLU SER ASN
SEQRES 8 H 133 SER LEU ASP TYR GLU LEU LEU GLN SER LEU GLY ALA GLN
SEQRES 9 H 133 SER SER LEU HIS LYS GLN LEU ILE GLU SER ARG ALA GLU
SEQRES 10 H 133 ARG ASP GLU LEU MET SER LYS LEU ILE GLU LEU SER SER
SEQRES 11 H 133 LYS PHE PRO
SEQRES 1 I 408 ASN SER ASN VAL LEU LEU PRO ARG LYS VAL MET SER ARG
SEQRES 2 I 408 ASP SER LEU LYS HIS LEU TYR SER SER ILE ILE LEU ILE
SEQRES 3 I 408 LYS ASN SER ARG ASP GLU SER SER SER PRO TYR GLU TRP
SEQRES 4 I 408 CYS ILE TRP GLN LEU LYS ARG CYS PHE ALA HIS GLN ILE
SEQRES 5 I 408 GLU THR PRO GLN GLU VAL ILE PRO ILE ILE ILE SER VAL
SEQRES 6 I 408 SER SER MET ASP ASN LYS LEU SER SER ARG ILE ILE GLN
SEQRES 7 I 408 THR PHE CYS ASN LEU LYS TYR LEU LYS LEU ASP GLU LEU
SEQRES 8 I 408 THR LEU LYS LYS VAL CYS GLY GLY ILE LEU PRO LEU TRP
SEQRES 9 I 408 LYS PRO GLU LEU ILE SER GLY THR ARG GLU PHE PHE VAL
SEQRES 10 I 408 LYS PHE MET ALA SER ILE PHE MET TRP SER THR ARG ASP
SEQRES 11 I 408 GLY HIS ASP ASN ASN CYS THR PHE SER GLU THR CYS PHE
SEQRES 12 I 408 TYR VAL LEU GLN MET ILE THR ASN TRP VAL LEU ASP ASP
SEQRES 13 I 408 LYS LEU ILE ALA LEU GLY LEU THR LEU LEU HIS ASP MET
SEQRES 14 I 408 GLN SER LEU LEU THR LEU ASP LYS ILE PHE ASN ASN ALA
SEQRES 15 I 408 THR SER ASN ARG PHE SER THR MET ALA PHE ILE SER SER
SEQRES 16 I 408 LEU ASP ILE LEU THR GLN LEU SER LYS GLN THR LYS SER
SEQRES 17 I 408 ASP TYR ALA ILE GLN TYR LEU ILE VAL GLY PRO ASP ILE
SEQRES 18 I 408 MET ASN LYS VAL PHE SER SER ASP ASP PRO LEU LEU LEU
SEQRES 19 I 408 SER ALA ALA CYS ARG TYR LEU VAL ALA THR LYS ASN LYS
SEQRES 20 I 408 LEU MET GLN TYR PRO SER THR ASN LYS PHE VAL ARG MET
SEQRES 21 I 408 GLN ASN GLN TYR ILE MET ASP LEU THR ASN TYR LEU TYR
SEQRES 22 I 408 ARG ASN LYS VAL LEU SER SER LYS SER LEU PHE GLY VAL
SEQRES 23 I 408 SER PRO ASP PHE PHE LYS GLN ILE LEU GLU ASN LEU TYR
SEQRES 24 I 408 ILE PRO THR ALA ASP PHE LYS ASN ALA LYS PHE PHE THR
SEQRES 25 I 408 ILE THR GLY ILE PRO ALA LEU SER TYR ILE CYS ILE ILE
SEQRES 26 I 408 ILE LEU ARG ARG LEU GLU THR ALA GLU ASN THR LYS ILE
SEQRES 27 I 408 LYS PHE THR SER GLY ILE ILE ASN GLU GLU THR PHE ASN
SEQRES 28 I 408 ASN PHE PHE ARG VAL HIS HIS ASP GLU ILE GLY GLN HIS
SEQRES 29 I 408 GLY TRP ILE LYS GLY VAL ASN ASN ILE HIS ASP LEU ARG
SEQRES 30 I 408 VAL LYS ILE LEU MET HIS LEU SER ASN THR ALA ASN PRO
SEQRES 31 I 408 TYR ARG ASP ILE ALA ALA PHE LEU PHE THR TYR LEU LYS
SEQRES 32 I 408 SER LEU SER LYS TYR
SEQRES 1 J 124 DG DT DG DC DC DT DG DG DA DG DA DC DT
SEQRES 2 J 124 DA DG DG DG DA DG DT DA DA DT DC DC DC
SEQRES 3 J 124 DC DT DT DG DG DC DG DG DT DT DA DA DA
SEQRES 4 J 124 DA DC DG DC DG DG DG DG DG DA DC DA DG
SEQRES 5 J 124 DC DG DC DG DT DA DC DG DT DG DC DG DT
SEQRES 6 J 124 DT DT DA DA DG DC DG DG DT DG DC DT DA
SEQRES 7 J 124 DG DA DG DC DT DG DT DC DT DA DC DG DA
SEQRES 8 J 124 DC DC DA DA DT DT DG DA DG DC DG DG DC
SEQRES 9 J 124 DC DT DC DG DG DC DA DC DC DG DG DG DA
SEQRES 10 J 124 DT DT DC DT DC DG DA
SEQRES 1 K 122 VAL LEU ASP VAL TYR ILE LYS ASN LEU GLU ASN GLN ILE
SEQRES 2 K 122 GLY ASN LYS ARG TYR PHE LEU LYS GLN ALA GLN GLY ALA
SEQRES 3 K 122 ILE ASP GLU ILE THR LYS ARG SER LEU ASP THR GLU GLY
SEQRES 4 K 122 LYS PRO VAL ASN SER GLU VAL PHE THR GLU LEU LEU ARG
SEQRES 5 K 122 LYS PRO MET PHE PHE SER GLU ARG ALA ASP PRO ILE GLY
SEQRES 6 K 122 PHE SER LEU THR SER ASN PHE LEU SER LEU ARG ALA GLN
SEQRES 7 K 122 SER SER SER GLU TRP LEU SER LEU MET ASN ASP GLN SER
SEQRES 8 K 122 VAL ASP GLN LYS ALA MET LEU LEU LEU GLN ASN ASN ILE
SEQRES 9 K 122 ASN SER ASP LEU LYS GLU LEU LEU ARG LYS LEU GLN HIS
SEQRES 10 K 122 GLN MET THR ILE MET
SEQRES 1 L 241 PRO TYR THR TRP LYS PHE LEU GLY ILE SER LYS GLN LEU
SEQRES 2 L 241 SER LEU GLU ASN GLY ILE ALA LYS LEU ASN GLN LEU LEU
SEQRES 3 L 241 ASN LEU GLU VAL ASP LEU ASP ILE GLN THR ILE ARG VAL
SEQRES 4 L 241 PRO SER ASP PRO ASP GLY GLY THR ALA ALA ASP GLU TYR
SEQRES 5 L 241 ILE ARG TYR GLU MET ARG LEU ASP ILE SER ASN LEU ASP
SEQRES 6 L 241 GLU GLY THR TYR SER LYS PHE ILE PHE LEU GLY ASN SER
SEQRES 7 L 241 LYS MET GLU VAL PRO MET PHE LEU CYS TYR CYS GLY THR
SEQRES 8 L 241 ASP ASN ARG ASN GLU VAL VAL LEU GLN TRP LEU LYS ALA
SEQRES 9 L 241 GLU TYR GLY VAL ILE MET TRP PRO ILE LYS PHE GLU GLN
SEQRES 10 L 241 LYS THR MET ILE LYS LEU ALA ASP ALA SER ILE VAL HIS
SEQRES 11 L 241 VAL THR LYS GLU ASN ILE GLU GLN ILE THR TRP PHE SER
SEQRES 12 L 241 SER LYS LEU TYR PHE GLU PRO GLU THR GLN ASP LYS ASN
SEQRES 13 L 241 LEU ARG GLN PHE SER ILE GLU ILE PRO ARG GLU SER CYS
SEQRES 14 L 241 GLU GLY LEU ALA LEU GLY TYR GLY ASN THR MET HIS PRO
SEQRES 15 L 241 TYR ASN ASP ALA ILE VAL PRO TYR ILE TYR ASN GLU THR
SEQRES 16 L 241 GLY MET ALA VAL GLU ARG LEU PRO LEU THR SER VAL ILE
SEQRES 17 L 241 LEU ALA GLY HIS THR LYS ILE MET ARG GLU SER ILE VAL
SEQRES 18 L 241 THR SER THR ARG SER LEU ARG ASN ARG VAL LEU ALA VAL
SEQRES 19 L 241 VAL LEU GLN SER ILE GLN PHE
SEQRES 1 N 447 LEU ARG LEU GLU ASP ASN TYR VAL PRO THR SER ASP THR
SEQRES 2 N 447 LEU VAL VAL PHE LYS GLN LEU MET LYS LEU PRO VAL THR
SEQRES 3 N 447 VAL LEU TYR ASP LEU THR LEU SER TRP PHE ALA LYS PHE
SEQRES 4 N 447 GLY GLY SER PHE ASP GLY ASP ILE TYR LEU LEU THR GLU
SEQRES 5 N 447 THR LEU ASP LEU LEU ILE GLU LYS GLY VAL ARG ARG ASN
SEQRES 6 N 447 VAL ILE VAL ASN ARG ILE LEU TYR VAL TYR TRP PRO ASP
SEQRES 7 N 447 GLY LEU ASN VAL PHE GLN LEU ALA GLU ILE ASP CYS HIS
SEQRES 8 N 447 LEU MET ILE SER LYS PRO GLU LYS PHE LYS TRP LEU PRO
SEQRES 9 N 447 SER LYS ALA LEU ARG GLY ASP GLY LYS PRO TYR VAL VAL
SEQRES 10 N 447 LYS LEU GLN PRO ALA LYS PHE ILE GLU ASN LEU GLN THR
SEQRES 11 N 447 ASP LEU ALA LYS ILE TYR HIS CYS HIS VAL TYR MET PHE
SEQRES 12 N 447 LYS HIS PRO SER LEU PRO VAL LEU ILE THR ARG ILE GLN
SEQRES 13 N 447 LEU PHE ASP SER ASN ASN LEU PHE LEU SER THR PRO ASN
SEQRES 14 N 447 ILE GLY SER ILE ASN LYS GLU SER LEU TYR ASN LYS LEU
SEQRES 15 N 447 ASP LYS PHE GLN GLY LYS PRO LEU ILE SER ARG ARG PRO
SEQRES 16 N 447 TYR TYR VAL ALA PHE PRO LEU ASN SER PRO ILE ILE PHE
SEQRES 17 N 447 HIS SER VAL ASP LYS ASP ILE TYR ALA ARG LEU VAL LEU
SEQRES 18 N 447 GLN SER ILE SER ARG THR ILE SER GLU ARG GLU THR ILE
SEQRES 19 N 447 ILE PHE LYS PRO VAL GLN LYS ILE PRO VAL LYS SER ILE
SEQRES 20 N 447 HIS ASN ILE MET THR LEU LEU GLY PRO SER ARG PHE ALA
SEQRES 21 N 447 GLU SER MET GLY PRO TRP GLU CYS TYR ALA SER ALA ASN
SEQRES 22 N 447 PHE GLU ARG SER PRO LEU HIS ASP TYR LYS LYS HIS GLN
SEQRES 23 N 447 GLY LEU THR GLY LYS LYS VAL MET VAL ARG GLU PHE ASP
SEQRES 24 N 447 ASP SER PHE LEU ASN ASP ASP GLU ASN PHE TYR GLY LYS
SEQRES 25 N 447 GLU GLU PRO GLU ILE ARG ARG LEU ARG LEU GLU LYS ASN
SEQRES 26 N 447 MET ILE LYS PHE LYS GLY SER ALA ASN GLY VAL MET ASP
SEQRES 27 N 447 GLN LYS TYR ASN ASP LEU LYS GLU PHE ASN GLU HIS VAL
SEQRES 28 N 447 HIS ASN ILE ARG ASN GLY LYS LYS ASN GLU ASP SER GLY
SEQRES 29 N 447 GLU PRO VAL TYR ILE SER ARG TYR SER SER LEU VAL PRO
SEQRES 30 N 447 ILE GLU LYS VAL GLY PHE THR LEU LYS ASN GLU ILE ASN
SEQRES 31 N 447 SER ARG ILE ILE THR ILE LYS LEU LYS PHE ASN GLY ASN
SEQRES 32 N 447 ASP ILE PHE GLY GLY LEU HIS GLU LEU CYS ASP LYS ASN
SEQRES 33 N 447 LEU ILE ASN ILE ASP LYS VAL PRO GLY TRP LEU ALA GLY
SEQRES 34 N 447 GLU ASN GLY SER PHE SER GLY THR ILE MET ASN GLY ASP
SEQRES 35 N 447 PHE GLN ARG GLU GLN
SEQRES 1 O 212 SER THR SER ASP ARG SER GLU LEU GLU ASP TYR ILE VAL
SEQRES 2 O 212 LEU GLU ASN VAL TYR ARG MET PHE GLY ILE THR PHE PHE
SEQRES 3 O 212 PRO LEU VAL ASP PRO ILE ASP LEU LYS ILE LYS ASP ALA
SEQRES 4 O 212 SER GLY GLU ILE PHE VAL ASP ARG GLU MET LEU GLY ILE
SEQRES 5 O 212 ARG LEU GLU VAL PHE SER GLU ARG THR SER GLN PHE GLU
SEQRES 6 O 212 LYS PRO HIS TYR VAL LEU LEU LYS LYS ARG ILE LYS SER
SEQRES 7 O 212 ASN SER TRP PHE LEU PHE LYS HIS THR ILE PRO SER PHE
SEQRES 8 O 212 ILE ASP VAL GLN GLY ILE PHE ASP ASP THR ASN GLY GLY
SEQRES 9 O 212 LEU VAL ILE SER HIS ASP ASP ALA TYR LEU PHE ALA LYS
SEQRES 10 O 212 ARG VAL PHE LEU GLN LEU VAL GLU VAL GLN LYS ARG ARG
SEQRES 11 O 212 GLN ILE PHE LYS ASP LEU GLU ALA LYS LYS ILE ILE HIS
SEQRES 12 O 212 ASP LEU ASP LEU ASP LEU GLU SER SER MET VAL SER PHE
SEQRES 13 O 212 PHE VAL LYS ASP ILE LYS VAL GLU LEU PHE VAL LYS GLN
SEQRES 14 O 212 ASN GLU ILE VAL SER CYS SER ILE LEU ASP ASP ILE HIS
SEQRES 15 O 212 ASP PHE SER GLN ASN ASN LYS SER LYS TRP GLU ILE ALA
SEQRES 16 O 212 LEU LEU GLY SER LEU ASP ASP LEU GLU LEU LYS LEU ASN
SEQRES 17 O 212 HIS SER PHE ALA
SEQRES 1 P 270 GLN ASN ASP ILE THR GLN ASP PHE LEU ASN LEU ILE SER
SEQRES 2 P 270 ILE SER SER SER ASN PRO ASN SER ALA ILE SER ASP ARG
SEQRES 3 P 270 LYS ARG VAL GLU ARG ILE ASN GLY LEU THR ASN LEU GLN
SEQRES 4 P 270 LYS GLU LEU VAL THR LYS TYR ASP THR LEU PRO LEU LEU
SEQRES 5 P 270 ASN MET ASN LEU ARG LEU SER TYR LEU ARG ASP HIS THR
SEQRES 6 P 270 TYR PRO HIS LEU GLN VAL SER VAL GLN SER ARG ASP ARG
SEQRES 7 P 270 VAL HIS ASN ASP GLY ILE GLU VAL LEU VAL VAL ASN TYR
SEQRES 8 P 270 LYS PHE CYS ARG ASN THR MET ASN PRO PHE GLU ILE GLN
SEQRES 9 P 270 PHE LYS MET PHE TYR LYS PHE GLU ASP SER THR LEU LEU
SEQRES 10 P 270 LYS TRP GLU ILE LEU ARG ILE SER THR ASN VAL ARG LEU
SEQRES 11 P 270 LYS ALA LYS GLN LEU LEU ALA THR ARG ASN PHE GLN LYS
SEQRES 12 P 270 CYS LEU LEU SER LEU TYR GLU PHE ASP LYS ILE LYS SER
SEQRES 13 P 270 LYS LYS THR GLY ILE PHE GLN ASN LEU ILE ASN LEU LEU
SEQRES 14 P 270 LYS ARG LYS THR ARG CYS TYR LEU MET ASN ASN SER ASP
SEQRES 15 P 270 SER LEU ILE VAL GLU ARG VAL ILE ARG GLU GLY ARG LEU
SEQRES 16 P 270 THR THR ILE LYS LEU GLN ILE ASN PHE ILE ILE THR MET
SEQRES 17 P 270 PRO GLY GLU ARG GLY LYS PRO ARG ASN CYS PHE LEU PRO
SEQRES 18 P 270 MET SER LYS ILE SER ILE ALA LEU TRP LYS GLY GLY GLU
SEQRES 19 P 270 ARG PHE ASN GLN ILE ASP LEU ASP GLU ILE CYS TYR GLY
SEQRES 20 P 270 LEU ILE LYS GLU TYR GLY VAL LYS THR GLY LEU LYS GLU
SEQRES 21 P 270 ILE CYS ASN VAL CYS LEU PHE PRO ASP MET
SEQRES 1 Q 231 SER ILE LEU ARG LEU LEU GLU THR ASN THR VAL SER ALA
SEQRES 2 Q 231 LEU ASP SER VAL PHE GLU LYS TYR GLU LYS GLU MET ASN
SEQRES 3 Q 231 GLN MET THR HIS GLY ASP ASN ASN GLU VAL LYS ARG ILE
SEQRES 4 Q 231 TYR SER LYS LYS GLU ARG LEU LEU GLU ILE ILE LEU THR
SEQRES 5 Q 231 LYS ILE LYS LYS LYS LEU ARG GLN ALA LYS PHE PRO SER
SEQRES 6 Q 231 ARG ILE SER GLU ARG ASP LEU ASP ILE GLU TYR ILE TYR
SEQRES 7 Q 231 SER LYS ARG GLN PHE ILE GLN ASN ARG TYR SER GLN GLU
SEQRES 8 Q 231 LEU GLN ASN ASN GLU ARG LEU GLU ALA ILE LEU SER ARG
SEQRES 9 Q 231 GLU GLN ASN LEU LEU GLU GLU THR ARG LYS LEU CYS MET
SEQRES 10 Q 231 ASN LEU LYS THR ASN ASN LYS LYS ARG LEU THR GLU LYS
SEQRES 11 Q 231 LEU ILE GLN LYS ASP LEU HIS PRO VAL LEU ASN LYS ALA
SEQRES 12 Q 231 MET GLU TYR THR TYR GLY LEU GLU SER THR ASN GLY PHE
SEQRES 13 Q 231 MET HIS PRO ASP GLY PRO VAL THR PHE ARG ASN ASP SER
SEQRES 14 Q 231 HIS GLU LEU ASN LEU MET LEU ASN ASP PRO ILE LYS SER
SEQRES 15 Q 231 THR ALA ASP VAL ARG LEU ASP LYS GLU GLU VAL LEU SER
SEQRES 16 Q 231 LEU LEU PRO SER LEU LYS GLU TYR THR LYS LYS SER LYS
SEQRES 17 Q 231 GLU LEU LYS GLU THR MET GLY GLN MET ILE SER ASP SER
SEQRES 18 Q 231 HIS GLU GLU GLU ILE LYS GLU VAL PHE VAL
SEQRES 1 U 190 SER VAL THR THR ILE ASP VAL LEU SER SER LEU PHE ILE
SEQRES 2 U 190 ASN LEU PHE GLU ASN ASP LEU ILE PRO GLN ALA LEU LYS
SEQRES 3 U 190 ASP PHE ASN LYS SER ASP ASP ASP GLN PHE ARG LYS LEU
SEQRES 4 U 190 LEU TYR LYS LEU ASP LEU ARG LEU PHE GLN THR ILE SER
SEQRES 5 U 190 ASP GLN MET THR ARG ASP LEU LYS ASP ILE LEU ASP ILE
SEQRES 6 U 190 ASN VAL SER ASN ASN GLU LEU CYS TYR GLN LEU LYS GLN
SEQRES 7 U 190 VAL LEU ALA ARG LYS GLU ASP LEU ASN GLN GLN ILE ILE
SEQRES 8 U 190 SER VAL ARG ASN GLU ILE GLN GLU LEU LYS ALA GLY LYS
SEQRES 9 U 190 ASP TRP HIS ASP LEU GLN ASN GLU GLN ALA LYS LEU ASN
SEQRES 10 U 190 ASP LYS VAL LYS LEU ASN LYS ARG LEU ASN ASP LEU THR
SEQRES 11 U 190 SER THR LEU LEU GLY LYS TYR GLU GLY ASP ARG LYS ILE
SEQRES 12 U 190 MET SER GLN ASP SER GLU ASP ASP SER ILE ARG ASP ASP
SEQRES 13 U 190 SER ASN ILE LEU ASP ILE ALA HIS PHE VAL ASP LEU MET
SEQRES 14 U 190 ASP PRO TYR ASN GLY LEU LEU LYS LYS ILE ASN LYS ILE
SEQRES 15 U 190 ASN GLU ASN LEU SER ASN GLU LEU
SEQRES 1 Y 237 THR ASP THR TYR ASN SER ILE SER ASN PHE ILE GLU ASN
SEQRES 2 Y 237 GLU LEU THR ALA LEU LEU SER SER ASP ASP TYR LEU MET
SEQRES 3 Y 237 ASP ASP LEU ALA GLY GLU LEU PRO ASN GLU VAL CYS ARG
SEQRES 4 Y 237 LEU LEU LYS ALA GLN VAL ILE GLU LYS ARG LYS ASP ALA
SEQRES 5 Y 237 MET SER ARG GLY LYS GLN ASP LEU LEU SER LYS GLU ILE
SEQRES 6 Y 237 TYR ASP ASN GLU SER GLU LEU ARG ALA SER GLN SER GLN
SEQRES 7 Y 237 GLN ILE MET GLU LEU VAL GLY ASP ILE PRO LYS TYR SER
SEQRES 8 Y 237 LEU GLY SER GLU LEU ARG ASN ARG VAL GLU GLY GLU PRO
SEQRES 9 Y 237 GLN SER THR SER ILE GLU ARG LEU ILE GLU ASP VAL LEU
SEQRES 10 Y 237 LYS LEU PRO GLN MET GLU VAL ALA ASP GLU GLU GLU VAL
SEQRES 11 Y 237 GLU VAL GLU ASN ASP LEU LYS VAL LEU SER GLU TYR SER
SEQRES 12 Y 237 ASN LEU ARG LYS ASP LEU ILE LEU LYS CYS GLN ALA LEU
SEQRES 13 Y 237 GLN ILE GLY GLU SER LYS LEU SER ASP ILE LEU SER GLN
SEQRES 14 Y 237 THR ASN SER ILE ASN SER LEU THR THR SER ILE LYS GLU
SEQRES 15 Y 237 ALA SER GLU ASP ASP ASP ILE SER GLU TYR PHE ALA THR
SEQRES 16 Y 237 TYR ASN GLY LYS LEU VAL VAL ALA LEU GLU GLU MET LYS
SEQRES 17 Y 237 LEU LEU LEU GLU GLU ALA VAL LYS THR PHE GLY ASN SER
SEQRES 18 Y 237 PRO GLU LYS ARG GLU LYS ILE LYS LYS ILE LEU SER GLU
SEQRES 19 Y 237 LEU LYS LYS
SEQRES 1 Z 151 SER GLU GLN LEU LEU HIS ASN TYR VAL SER ASP SER LEU
SEQRES 2 Z 151 LEU THR THR LEU ILE SER PHE GLN GLU PHE LYS GLN GLN
SEQRES 3 Z 151 LEU GLN SER TYR THR SER ASP GLU GLN GLN LEU GLN HIS
SEQRES 4 Z 151 TRP TYR GLU LEU LEU GLN ALA ARG ASP ALA ARG VAL THR
SEQRES 5 Z 151 SER GLU LEU GLU ALA ARG ILE LYS GLN PHE PHE ILE THR
SEQRES 6 Z 151 LEU ARG SER ARG LEU LEU ARG PHE LEU GLU SER GLU GLN
SEQRES 7 Z 151 LEU SER HIS SER LEU SER LEU GLU THR LEU ILE ASP ALA
SEQRES 8 Z 151 LEU TYR LYS ILE ASN ASP LEU LEU GLN GLN ARG LEU GLN
SEQRES 9 Z 151 ILE LEU ASP ASP ALA ILE GLN GLU LYS THR SER GLU LEU
SEQRES 10 Z 151 ALA GLU PHE GLU ASN MET VAL ARG SER PRO SER ALA GLY
SEQRES 11 Z 151 ASP ASN ALA ILE PRO GLY LEU LEU GLN ILE ILE GLN SER
SEQRES 12 Z 151 TYR ILE ASN LEU LEU GLU GLU ASN
SEQRES 1 a 90 LEU ALA LEU TYR GLU ILE ARG LYS TYR GLN ARG SER THR
SEQRES 2 a 90 ASP LEU LEU ILE SER LYS ILE PRO PHE ALA ARG LEU VAL
SEQRES 3 a 90 LYS GLU VAL THR ASP GLU PHE THR THR LYS ASP GLN ASP
SEQRES 4 a 90 LEU ARG TRP GLN SER MET ALA ILE MET ALA LEU GLN GLU
SEQRES 5 a 90 ALA SER GLU ALA TYR LEU VAL GLY LEU LEU GLU HIS THR
SEQRES 6 a 90 ASN LEU LEU ALA LEU HIS ALA LYS ARG ILE THR ILE MET
SEQRES 7 a 90 LYS LYS ASP MET GLN LEU ALA ARG ARG ILE ARG GLY
SEQRES 1 b 79 ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG
SEQRES 2 b 79 LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU
SEQRES 3 b 79 ILE TYR GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU
SEQRES 4 b 79 GLU SER VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS
SEQRES 5 b 79 ALA LYS ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR
SEQRES 6 b 79 ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY
SEQRES 7 b 79 GLY
SEQRES 1 d 93 ARG LYS GLU THR TYR SER SER TYR ILE TYR LYS VAL LEU
SEQRES 2 d 93 LYS GLN THR HIS PRO ASP THR GLY ILE SER GLN LYS SER
SEQRES 3 d 93 MET SER ILE LEU ASN SER PHE VAL ASN ASP ILE PHE GLU
SEQRES 4 d 93 ARG ILE ALA THR GLU ALA SER LYS LEU ALA ALA TYR ASN
SEQRES 5 d 93 LYS LYS SER THR ILE SER ALA ARG GLU ILE GLN THR ALA
SEQRES 6 d 93 VAL ARG LEU ILE LEU PRO GLY GLU LEU ALA LYS HIS ALA
SEQRES 7 d 93 VAL SER GLU GLY THR ARG ALA VAL THR LYS TYR SER SER
SEQRES 8 d 93 SER THR
SEQRES 1 e 115 VAL ARG GLN LYS ARG ARG GLU LYS GLN ARG LYS GLN SER
SEQRES 2 e 115 LEU LYS ARG VAL GLU LYS LYS TYR THR PRO SER GLU LEU
SEQRES 3 e 115 ALA LEU TYR GLU ILE ARG LYS TYR GLN ARG SER THR ASP
SEQRES 4 e 115 LEU LEU ILE SER LYS ILE PRO PHE ALA ARG LEU VAL LYS
SEQRES 5 e 115 GLU VAL THR ASP GLU PHE THR THR LYS ASP GLN ASP LEU
SEQRES 6 e 115 ARG TRP GLN SER MET ALA ILE MET ALA LEU GLN GLU ALA
SEQRES 7 e 115 SER GLU ALA TYR LEU VAL GLY LEU LEU GLU HIS THR ASN
SEQRES 8 e 115 LEU LEU ALA LEU HIS ALA LYS ARG ILE THR ILE MET LYS
SEQRES 9 e 115 LYS ASP MET GLN LEU ALA ARG ARG ILE ARG GLY
SEQRES 1 f 79 ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG
SEQRES 2 f 79 LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU
SEQRES 3 f 79 ILE TYR GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU
SEQRES 4 f 79 GLU SER VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS
SEQRES 5 f 79 ALA LYS ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR
SEQRES 6 f 79 ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY
SEQRES 7 f 79 GLY
SEQRES 1 g 105 GLN SER ARG SER ALA LYS ALA GLY LEU THR PHE PRO VAL
SEQRES 2 g 105 GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY ASN TYR ALA
SEQRES 3 g 105 GLN ARG ILE GLY SER GLY ALA PRO VAL TYR LEU THR ALA
SEQRES 4 g 105 VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU GLU LEU ALA
SEQRES 5 g 105 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 g 105 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP ASP GLU
SEQRES 7 g 105 LEU ASN LYS LEU LEU GLY ASN VAL THR ILE ALA GLN GLY
SEQRES 8 g 105 GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU LEU PRO LYS
SEQRES 9 g 105 LYS
SEQRES 1 h 94 ALA ARG LYS GLU THR TYR SER SER TYR ILE TYR LYS VAL
SEQRES 2 h 94 LEU LYS GLN THR HIS PRO ASP THR GLY ILE SER GLN LYS
SEQRES 3 h 94 SER MET SER ILE LEU ASN SER PHE VAL ASN ASP ILE PHE
SEQRES 4 h 94 GLU ARG ILE ALA THR GLU ALA SER LYS LEU ALA ALA TYR
SEQRES 5 h 94 ASN LYS LYS SER THR ILE SER ALA ARG GLU ILE GLN THR
SEQRES 6 h 94 ALA VAL ARG LEU ILE LEU PRO GLY GLU LEU ALA LYS HIS
SEQRES 7 h 94 ALA VAL SER GLU GLY THR ARG ALA VAL THR LYS TYR SER
SEQRES 8 h 94 SER SER THR
SEQRES 1 i 102 GLN SER ARG SER ALA LYS ALA GLY LEU THR PHE PRO VAL
SEQRES 2 i 102 GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY ASN TYR ALA
SEQRES 3 i 102 GLN ARG ILE GLY SER GLY ALA PRO VAL TYR LEU THR ALA
SEQRES 4 i 102 VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU GLU LEU ALA
SEQRES 5 i 102 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 i 102 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP ASP GLU
SEQRES 7 i 102 LEU ASN LYS LEU LEU GLY ASN VAL THR ILE ALA GLN GLY
SEQRES 8 i 102 GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU LEU
HELIX 1 AA1 SER H 5 LYS H 38 1 34
HELIX 2 AA2 SER H 46 LEU H 73 1 28
HELIX 3 AA3 PHE H 83 SER H 93 1 11
HELIX 4 AA4 LEU H 96 PHE H 135 1 40
HELIX 5 AA5 ASP I 334 HIS I 338 5 5
HELIX 6 AA6 LEU I 339 SER I 349 1 11
HELIX 7 AA7 SER I 354 ALA I 369 1 16
HELIX 8 AA8 VAL I 378 SER I 387 1 10
HELIX 9 AA9 ASP I 389 THR I 399 1 11
HELIX 10 AB1 ASN I 402 LYS I 407 1 6
HELIX 11 AB2 ASP I 409 LEU I 421 1 13
HELIX 12 AB3 THR I 432 ASP I 450 1 19
HELIX 13 AB4 THR I 457 VAL I 473 1 17
HELIX 14 AB5 ILE I 479 LEU I 493 1 15
HELIX 15 AB6 ARG I 506 LYS I 524 1 19
HELIX 16 AB7 GLY I 538 SER I 548 1 11
HELIX 17 AB8 ASP I 550 MET I 569 1 20
HELIX 18 AB9 PHE I 577 LEU I 592 1 16
HELIX 19 AC1 SER I 607 TYR I 619 1 13
HELIX 20 AC2 LEU I 639 GLU I 651 1 13
HELIX 21 AC3 ASN I 666 ARG I 675 1 10
HELIX 22 AC4 ASP I 695 THR I 707 1 13
HELIX 23 AC5 ARG I 712 TYR I 721 1 10
HELIX 24 AC6 LEU I 722 SER I 726 5 5
HELIX 25 AC7 LEU K 8 SER K 40 1 33
HELIX 26 AC8 GLU K 51 ARG K 58 1 8
HELIX 27 AC9 ILE K 70 ILE K 127 1 58
HELIX 28 AD1 GLY L 19 ASN L 28 1 10
HELIX 29 AD2 ASN L 94 GLU L 106 1 13
HELIX 30 AD3 GLN L 118 SER L 128 1 11
HELIX 31 AD4 THR L 153 ASN L 157 5 5
HELIX 32 AD5 PRO L 166 GLY L 178 1 13
HELIX 33 AD6 HIS L 182 ALA L 187 1 6
HELIX 34 AD7 ALA L 187 THR L 196 1 10
HELIX 35 AD8 ARG L 229 ILE L 240 1 12
HELIX 36 AD9 ASP N 16 MET N 25 1 10
HELIX 37 AE1 PRO N 28 PHE N 43 1 16
HELIX 38 AE2 LEU N 54 LYS N 64 1 11
HELIX 39 AE3 ARG N 67 TYR N 77 1 11
HELIX 40 AE4 ASN N 85 LYS N 100 1 16
HELIX 41 AE5 GLN N 124 ALA N 137 1 14
HELIX 42 AE6 ASP N 218 ILE N 232 1 15
HELIX 43 AE7 SER N 250 GLY N 259 1 10
HELIX 44 AE8 SER N 261 GLU N 265 5 5
HELIX 45 AE9 GLY N 268 TYR N 273 5 6
HELIX 46 AF1 HIS N 289 GLY N 294 1 6
HELIX 47 AF2 GLU N 318 LYS N 334 1 17
HELIX 48 AF3 ASP N 408 LYS N 419 1 12
HELIX 49 AF4 ASN N 423 VAL N 427 5 5
HELIX 50 AF5 PRO N 428 GLY N 433 1 6
HELIX 51 AF6 THR O 154 MET O 172 1 19
HELIX 52 AF7 VAL O 246 THR O 253 1 8
HELIX 53 AF8 ASN O 254 LEU O 257 5 4
HELIX 54 AF9 SER O 260 LYS O 291 1 32
HELIX 55 AG1 ASN O 340 LEU O 348 1 9
HELIX 56 AG2 LEU O 352 PHE O 363 1 12
HELIX 57 AG3 ASN P 98 ILE P 110 1 13
HELIX 58 AG4 ASN P 133 THR P 140 1 8
HELIX 59 AG5 ASN P 149 ASP P 159 1 11
HELIX 60 AG6 VAL P 224 LEU P 232 1 9
HELIX 61 AG7 ASN P 236 LYS P 266 1 31
HELIX 62 AG8 ASN P 333 TYR P 348 1 16
HELIX 63 AG9 THR P 352 PHE P 363 1 12
HELIX 64 AH1 ILE Q 162 GLU Q 184 1 23
HELIX 65 AH2 LYS Q 197 ARG Q 219 1 23
HELIX 66 AH3 ILE Q 234 GLN Q 293 1 60
HELIX 67 AH4 PRO Q 322 ASN Q 333 1 12
HELIX 68 AH5 ASP Q 349 LEU Q 357 1 9
HELIX 69 AH6 PRO Q 358 HIS Q 382 1 25
HELIX 70 AH7 HIS Q 382 VAL Q 391 1 10
HELIX 71 AH8 VAL U 132 LEU U 155 1 24
HELIX 72 AH9 ARG U 167 LYS U 231 1 65
HELIX 73 AI1 GLY U 233 GLY U 265 1 33
HELIX 74 AI2 ASN U 288 MET U 299 1 12
HELIX 75 AI3 LEU U 305 ASN U 318 1 14
HELIX 76 AI4 ASP Y 3 LEU Y 16 1 14
HELIX 77 AI5 LEU Y 16 SER Y 22 1 7
HELIX 78 AI6 ASN Y 36 LYS Y 49 1 14
HELIX 79 AI7 GLY Y 57 GLU Y 83 1 27
HELIX 80 AI8 GLY Y 94 GLY Y 103 1 10
HELIX 81 AI9 SER Y 109 LEU Y 118 1 10
HELIX 82 AJ1 LEU Y 137 GLU Y 186 1 50
HELIX 83 AJ2 ASP Y 189 THR Y 196 1 8
HELIX 84 AJ3 THR Y 196 PHE Y 219 1 24
HELIX 85 AJ4 PRO Y 223 LYS Y 238 1 16
HELIX 86 AJ5 GLU Z 4 SER Z 14 1 11
HELIX 87 AJ6 LEU Z 19 GLN Z 23 5 5
HELIX 88 AJ7 GLN Z 38 TYR Z 43 1 6
HELIX 89 AJ8 TYR Z 43 SER Z 82 1 40
HELIX 90 AJ9 GLU Z 88 ASN Z 124 1 37
HELIX 91 AK1 ALA Z 131 GLU Z 152 1 22
HELIX 92 AK2 ALA a 138 GLN a 146 1 9
HELIX 93 AK3 LYS a 155 THR a 170 1 16
HELIX 94 AK4 GLN a 179 ALA a 208 1 30
HELIX 95 AK5 LYS a 216 ALA a 221 1 6
HELIX 96 AK6 ARG a 222 ARG a 225 5 4
HELIX 97 AK7 THR b 31 GLY b 43 1 13
HELIX 98 AK8 GLY b 49 ALA b 77 1 29
HELIX 99 AK9 THR b 83 GLY b 95 1 13
HELIX 100 AL1 TYR d 41 HIS d 53 1 13
HELIX 101 AL2 SER d 59 ASN d 88 1 30
HELIX 102 AL3 SER d 94 LEU d 106 1 13
HELIX 103 AL4 PRO d 107 SER d 128 1 22
HELIX 104 AL5 ARG e 113 VAL e 128 1 16
HELIX 105 AL6 LEU e 139 GLN e 146 1 8
HELIX 106 AL7 SER e 154 ASP e 167 1 14
HELIX 107 AL8 GLN e 179 ALA e 208 1 30
HELIX 108 AL9 LYS e 216 ILE e 224 1 9
HELIX 109 AM1 ASN f 26 ILE f 30 5 5
HELIX 110 AM2 THR f 31 GLY f 42 1 12
HELIX 111 AM3 LEU f 50 ALA f 77 1 28
HELIX 112 AM4 THR f 83 GLN f 94 1 12
HELIX 113 AM5 PRO g 28 ASN g 40 1 13
HELIX 114 AM6 SER g 47 ASN g 75 1 29
HELIX 115 AM7 ILE g 81 ARG g 90 1 10
HELIX 116 AM8 ASP g 92 LEU g 99 1 8
HELIX 117 AM9 TYR h 41 HIS h 53 1 13
HELIX 118 AN1 SER h 59 ASN h 88 1 30
HELIX 119 AN2 SER h 94 LEU h 106 1 13
HELIX 120 AN3 PRO h 107 SER h 126 1 20
HELIX 121 AN4 PRO i 28 ARG i 38 1 11
HELIX 122 AN5 GLY i 48 ASP i 74 1 27
HELIX 123 AN6 ILE i 81 ASN i 91 1 11
HELIX 124 AN7 ASP i 92 GLY i 100 1 9
SHEET 1 AA1 6 PHE L 73 LEU L 76 0
SHEET 2 AA1 6 MET L 85 TYR L 89 -1 O CYS L 88 N ILE L 74
SHEET 3 AA1 6 TYR L 3 ILE L 10 -1 N LYS L 6 O TYR L 89
SHEET 4 AA1 6 SER L 220 THR L 223 -1 O ILE L 221 N TRP L 5
SHEET 5 AA1 6 THR L 214 ILE L 216 -1 N LYS L 215 O VAL L 222
SHEET 6 AA1 6 VAL L 208 ILE L 209 -1 N VAL L 208 O ILE L 216
SHEET 1 AA2 2 LEU L 33 GLN L 36 0
SHEET 2 AA2 2 ARG L 55 MET L 58 -1 O ARG L 55 N GLN L 36
SHEET 1 AA3 2 VAL L 130 VAL L 132 0
SHEET 2 AA3 2 GLU L 138 ILE L 140 -1 O GLN L 139 N HIS L 131
SHEET 1 AA4 4 SER L 162 GLU L 164 0
SHEET 2 AA4 4 ARG N 396 LYS N 403 -1 O LYS N 401 N GLU L 164
SHEET 3 AA4 4 THR N 388 ILE N 393 -1 N ILE N 393 O ARG N 396
SHEET 4 AA4 4 THR N 441 MET N 443 1 O ILE N 442 N LYS N 390
SHEET 1 AA5 5 TRP N 106 LYS N 110 0
SHEET 2 AA5 5 ILE N 210 SER N 214 -1 O ILE N 211 N SER N 109
SHEET 3 AA5 5 TYR N 200 PRO N 205 -1 N TYR N 201 O SER N 214
SHEET 4 AA5 5 VAL N 154 ASP N 163 -1 N LEU N 155 O PHE N 204
SHEET 5 AA5 5 CYS N 142 LYS N 148 -1 N TYR N 145 O ARG N 158
SHEET 1 AA6 5 TRP N 106 LYS N 110 0
SHEET 2 AA6 5 ILE N 210 SER N 214 -1 O ILE N 211 N SER N 109
SHEET 3 AA6 5 TYR N 200 PRO N 205 -1 N TYR N 201 O SER N 214
SHEET 4 AA6 5 VAL N 154 ASP N 163 -1 N LEU N 155 O PHE N 204
SHEET 5 AA6 5 ILE N 195 SER N 196 -1 O ILE N 195 N ASP N 163
SHEET 1 AA7 2 LEU N 112 ARG N 113 0
SHEET 2 AA7 2 LYS N 117 PRO N 118 -1 O LYS N 117 N ARG N 113
SHEET 1 AA8 4 ILE O 175 LEU O 180 0
SHEET 2 AA8 4 MET O 201 LEU O 206 -1 O ARG O 205 N THR O 176
SHEET 3 AA8 4 HIS O 220 LYS O 226 -1 O VAL O 222 N ILE O 204
SHEET 4 AA8 4 TRP O 233 LEU O 235 -1 O PHE O 234 N LYS O 225
SHEET 1 AA9 4 MET O 305 PHE O 309 0
SHEET 2 AA9 4 LYS O 314 LYS O 320 -1 O LEU O 317 N VAL O 306
SHEET 3 AA9 4 GLU O 323 LEU O 330 -1 O SER O 326 N PHE O 318
SHEET 4 AA9 4 GLY O 350 SER O 351 -1 O GLY O 350 N ILE O 324
SHEET 1 AB1 4 LEU P 165 VAL P 175 0
SHEET 2 AB1 4 ILE P 180 PHE P 189 -1 O VAL P 182 N ASP P 173
SHEET 3 AB1 4 PHE P 197 TYR P 205 -1 O PHE P 201 N VAL P 185
SHEET 4 AB1 4 LEU P 212 ILE P 220 -1 O LEU P 218 N GLN P 200
SHEET 1 AB2 5 ARG P 270 LEU P 273 0
SHEET 2 AB2 5 SER P 279 ARG P 284 -1 O ILE P 281 N TYR P 272
SHEET 3 AB2 5 ILE P 294 THR P 303 -1 O ILE P 294 N ARG P 284
SHEET 4 AB2 5 MET P 318 TRP P 326 -1 O SER P 322 N ASN P 299
SHEET 5 AB2 5 LEU Q 334 LEU Q 336 1 O MET Q 335 N SER P 319
SHEET 1 AB3 2 THR b 97 TYR b 99 0
SHEET 2 AB3 2 VAL g 102 ILE g 104 1 O THR g 103 N THR b 97
SHEET 1 AB4 2 GLY d 57 ILE d 58 0
SHEET 2 AB4 2 ARG i 79 ILE i 80 1 O ILE i 80 N GLY d 57
SHEET 1 AB5 2 THR d 92 ILE d 93 0
SHEET 2 AB5 2 ARG i 44 ILE i 45 1 O ARG i 44 N ILE d 93
SHEET 1 AB6 2 ARG e 177 TRP e 178 0
SHEET 2 AB6 2 THR f 81 VAL f 82 1 O VAL f 82 N ARG e 177
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
