HEADER OXIDOREDUCTASE/ELECTRON TRANSPORT 05-OCT-18 6HU9
TITLE III2-IV2 MITOCHONDRIAL RESPIRATORY SUPERCOMPLEX FROM S. CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL;
COMPND 3 CHAIN: A, L;
COMPND 4 SYNONYM: COMPLEX III SUBUNIT 1,CORE PROTEIN I,UBIQUINOL-CYTOCHROME-C
COMPND 5 REDUCTASE COMPLEX CORE PROTEIN 1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL;
COMPND 8 CHAIN: B, M;
COMPND 9 SYNONYM: COMPLEX III SUBUNIT 2,CORE PROTEIN II,UBIQUINOL-CYTOCHROME-C
COMPND 10 REDUCTASE COMPLEX CORE PROTEIN 2;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: CYTOCHROME B;
COMPND 13 CHAIN: C, N;
COMPND 14 SYNONYM: COMPLEX III SUBUNIT 3,COMPLEX III SUBUNIT CYTB,COMPLEX III
COMPND 15 SUBUNIT III,CYTOCHROME B-C1 COMPLEX SUBUNIT 3,CYTOCHROME B-C1 COMPLEX
COMPND 16 SUBUNIT CYTB,UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME B
COMPND 17 SUBUNIT;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL;
COMPND 20 CHAIN: D, O;
COMPND 21 SYNONYM: COMPLEX III SUBUNIT 4,COMPLEX III SUBUNIT IV,CYTOCHROME B-C1
COMPND 22 COMPLEX SUBUNIT 4,UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME
COMPND 23 C1 SUBUNIT,CYTOCHROME C-1;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL;
COMPND 26 CHAIN: E, P;
COMPND 27 SYNONYM: COMPLEX III SUBUNIT 5,RIESKE IRON-SULFUR PROTEIN,RISP,
COMPND 28 UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT;
COMPND 29 EC: 1.10.2.2;
COMPND 30 MOL_ID: 6;
COMPND 31 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 6;
COMPND 32 CHAIN: F, Q;
COMPND 33 SYNONYM: COMPLEX III SUBUNIT 6,COMPLEX III SUBUNIT VI,CYTOCHROME C1
COMPND 34 NON-HEME 17 KDA PROTEIN,MITOCHONDRIAL HINGE PROTEIN,UBIQUINOL-
COMPND 35 CYTOCHROME C REDUCTASE COMPLEX 17 KDA PROTEIN;
COMPND 36 MOL_ID: 7;
COMPND 37 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 7;
COMPND 38 CHAIN: G, R;
COMPND 39 SYNONYM: COMPLEX III SUBUNIT 7,COMPLEX III SUBUNIT VII,UBIQUINOL-
COMPND 40 CYTOCHROME C REDUCTASE C REDUCTASE COMPLEX 14 KDA PROTEIN;
COMPND 41 MOL_ID: 8;
COMPND 42 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 8;
COMPND 43 CHAIN: H, S;
COMPND 44 SYNONYM: COMPLEX III SUBUNIT 8,COMPLEX III SUBUNIT VII,UBIQUINOL-
COMPND 45 CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN,UBIQUINOL-CYTOCHROME C
COMPND 46 REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C;
COMPND 47 MOL_ID: 9;
COMPND 48 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 9;
COMPND 49 CHAIN: I, T;
COMPND 50 SYNONYM: COMPLEX III SUBUNIT 9,COMPLEX III SUBUNIT X,CYTOCHROME C1
COMPND 51 NON-HEME 7.3 KDA PROTEIN,UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3
COMPND 52 KDA PROTEIN;
COMPND 53 MOL_ID: 10;
COMPND 54 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT 10;
COMPND 55 CHAIN: J, U;
COMPND 56 SYNONYM: COMPLEX III SUBUNIT 10,COMPLEX III SUBUNIT XI,UBIQUINOL-
COMPND 57 CYTOCHROME C REDUCTASE COMPLEX 8.5 KDA PROTEIN;
COMPND 58 MOL_ID: 11;
COMPND 59 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;
COMPND 60 CHAIN: a, m;
COMPND 61 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE I, COX1;
COMPND 62 EC: 1.9.3.1;
COMPND 63 MOL_ID: 12;
COMPND 64 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND 65 CHAIN: b, n;
COMPND 66 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE II, COX2;
COMPND 67 EC: 1.9.3.1;
COMPND 68 MOL_ID: 13;
COMPND 69 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 3;
COMPND 70 CHAIN: c, o;
COMPND 71 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III, COX3;
COMPND 72 EC: 1.9.3.1;
COMPND 73 MOL_ID: 14;
COMPND 74 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 4, MITOCHONDRIAL;
COMPND 75 CHAIN: d, p;
COMPND 76 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE IV, COX4;
COMPND 77 EC: 1.9.3.1;
COMPND 78 MOL_ID: 15;
COMPND 79 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 5A, MITOCHONDRIAL;
COMPND 80 CHAIN: e, q;
COMPND 81 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VA, COX5A;
COMPND 82 EC: 1.9.3.1;
COMPND 83 MOL_ID: 16;
COMPND 84 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6, MITOCHONDRIAL;
COMPND 85 CHAIN: f, r;
COMPND 86 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VI, COX6;
COMPND 87 EC: 1.9.3.1;
COMPND 88 MOL_ID: 17;
COMPND 89 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7;
COMPND 90 CHAIN: g, s;
COMPND 91 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VII, COX7;
COMPND 92 EC: 1.9.3.1;
COMPND 93 MOL_ID: 18;
COMPND 94 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIII, MITOCHONDRIAL;
COMPND 95 CHAIN: h, t;
COMPND 96 EC: 1.9.3.1;
COMPND 97 MOL_ID: 19;
COMPND 98 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7A;
COMPND 99 CHAIN: i, u;
COMPND 100 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA, COX9;
COMPND 101 EC: 1.9.3.1;
COMPND 102 MOL_ID: 20;
COMPND 103 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6B;
COMPND 104 CHAIN: j, v;
COMPND 105 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIB, COX12;
COMPND 106 EC: 1.9.3.1;
COMPND 107 MOL_ID: 21;
COMPND 108 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6A, MITOCHONDRIAL;
COMPND 109 CHAIN: k, w;
COMPND 110 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIA, COX13;
COMPND 111 EC: 1.9.3.1;
COMPND 112 ENGINEERED: YES;
COMPND 113 MOL_ID: 22;
COMPND 114 MOLECULE: COX26;
COMPND 115 CHAIN: l, x
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 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 9 S288C);
SOURCE 10 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 11 ORGANISM_TAXID: 559292;
SOURCE 12 STRAIN: ATCC 204508 / S288C;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 15 S288C);
SOURCE 16 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 17 ORGANISM_TAXID: 559292;
SOURCE 18 STRAIN: ATCC 204508 / S288C;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 21 S288C);
SOURCE 22 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 23 ORGANISM_TAXID: 559292;
SOURCE 24 STRAIN: ATCC 204508 / S288C;
SOURCE 25 MOL_ID: 5;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 27 S288C);
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 MOL_ID: 6;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 33 S288C);
SOURCE 34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 35 ORGANISM_TAXID: 559292;
SOURCE 36 STRAIN: ATCC 204508 / S288C;
SOURCE 37 MOL_ID: 7;
SOURCE 38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 39 S288C);
SOURCE 40 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 41 ORGANISM_TAXID: 559292;
SOURCE 42 STRAIN: ATCC 204508 / S288C;
SOURCE 43 MOL_ID: 8;
SOURCE 44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 45 S288C);
SOURCE 46 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 47 ORGANISM_TAXID: 559292;
SOURCE 48 STRAIN: ATCC 204508 / S288C;
SOURCE 49 MOL_ID: 9;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 51 S288C);
SOURCE 52 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 53 ORGANISM_TAXID: 559292;
SOURCE 54 STRAIN: ATCC 204508 / S288C;
SOURCE 55 MOL_ID: 10;
SOURCE 56 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 57 S288C);
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 559292;
SOURCE 60 STRAIN: ATCC 204508 / S288C;
SOURCE 61 MOL_ID: 11;
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 MOL_ID: 12;
SOURCE 68 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 69 S288C);
SOURCE 70 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 71 ORGANISM_TAXID: 559292;
SOURCE 72 STRAIN: ATCC 204508 / S288C;
SOURCE 73 MOL_ID: 13;
SOURCE 74 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 75 S288C);
SOURCE 76 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 77 ORGANISM_TAXID: 559292;
SOURCE 78 STRAIN: ATCC 204508 / S288C;
SOURCE 79 MOL_ID: 14;
SOURCE 80 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 81 S288C);
SOURCE 82 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 83 ORGANISM_TAXID: 559292;
SOURCE 84 STRAIN: ATCC 204508 / S288C;
SOURCE 85 MOL_ID: 15;
SOURCE 86 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 87 S288C);
SOURCE 88 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 89 ORGANISM_TAXID: 559292;
SOURCE 90 STRAIN: ATCC 204508 / S288C;
SOURCE 91 MOL_ID: 16;
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 MOL_ID: 17;
SOURCE 98 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 99 S288C);
SOURCE 100 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 101 ORGANISM_TAXID: 559292;
SOURCE 102 STRAIN: ATCC 204508 / S288C;
SOURCE 103 MOL_ID: 18;
SOURCE 104 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 105 S288C);
SOURCE 106 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 107 ORGANISM_TAXID: 559292;
SOURCE 108 STRAIN: ATCC 204508 / S288C;
SOURCE 109 MOL_ID: 19;
SOURCE 110 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 111 S288C);
SOURCE 112 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 113 ORGANISM_TAXID: 559292;
SOURCE 114 STRAIN: ATCC 204508 / S288C;
SOURCE 115 MOL_ID: 20;
SOURCE 116 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 117 S288C);
SOURCE 118 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 119 ORGANISM_TAXID: 559292;
SOURCE 120 STRAIN: ATCC 204508 / S288C;
SOURCE 121 MOL_ID: 21;
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: COX13, YGL191W, G1341;
SOURCE 128 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 129 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 130 EXPRESSION_SYSTEM_STRAIN: W303-1B;
SOURCE 131 MOL_ID: 22;
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
KEYWDS CYTOCHROME C OXIDASE CYTOCHROME BC1 MITOCHONDRIA RESPIRATORY CHAIN
KEYWDS 2 SUPERCOMPLEX, OXIDOREDUCTASE, ELECTRON TRANSPORT, OXIDOREDUCTASE-
KEYWDS 3 ELECTRON TRANSPORT COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.M.HARTLEY,N.PINOTSIS,A.MARECHAL
REVDAT 5 11-DEC-19 6HU9 1 CRYST1 SCALE
REVDAT 4 23-JAN-19 6HU9 1 REMARK SSBOND LINK SITE
REVDAT 3 16-JAN-19 6HU9 1 JRNL
REVDAT 2 09-JAN-19 6HU9 1 JRNL
REVDAT 1 26-DEC-18 6HU9 0
JRNL AUTH A.M.HARTLEY,N.LUKOYANOVA,Y.ZHANG,A.CABRERA-OREFICE,S.ARNOLD,
JRNL AUTH 2 B.MEUNIER,N.PINOTSIS,A.MARECHAL
JRNL TITL STRUCTURE OF YEAST CYTOCHROME C OXIDASE IN A SUPERCOMPLEX
JRNL TITL 2 WITH CYTOCHROME BC1.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 26 78 2019
JRNL REFN ESSN 1545-9985
JRNL PMID 30598554
JRNL DOI 10.1038/S41594-018-0172-Z
REMARK 2
REMARK 2 RESOLUTION. 3.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, EPU, CTFFIND, UCSF CHIMERA,
REMARK 3 PHENIX, RELION, RELION, RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 1KYO
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
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) : 3.350
REMARK 3 NUMBER OF PARTICLES : 44915
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6HU9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012277.
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 : III2-IV2 MITOCHONDRIAL
REMARK 245 RESPIRATORY SUPERCOMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : 3 MICROL OF SAMPLE APPLIED TO
REMARK 245 NEGATIVELY GLOW DISCHARGED GRID,
REMARK 245 BLOT FORCE -10; BLOTTING TIME
REMARK 245 8.5 SEC
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.20
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 QUANTUM (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) : 1.65
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 130000
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: 44-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: L, M, N, O, P, Q, R, S, T,
REMARK 350 AND CHAINS: U, a, b, c, d, e, f, g, h, i,
REMARK 350 AND CHAINS: j, k, l, m, n, o, p, q, r,
REMARK 350 AND CHAINS: s, t, u, v, w, x
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 LYS D 309
REMARK 465 MET F 1
REMARK 465 GLY F 2
REMARK 465 MET F 3
REMARK 465 LEU F 4
REMARK 465 GLU F 5
REMARK 465 LEU F 6
REMARK 465 VAL F 7
REMARK 465 GLY F 8
REMARK 465 GLU F 9
REMARK 465 TYR F 10
REMARK 465 TRP F 11
REMARK 465 GLU F 12
REMARK 465 GLN F 13
REMARK 465 LEU F 14
REMARK 465 LYS F 15
REMARK 465 ILE F 16
REMARK 465 THR F 17
REMARK 465 VAL F 18
REMARK 465 VAL F 19
REMARK 465 PRO F 20
REMARK 465 VAL F 21
REMARK 465 VAL F 22
REMARK 465 ALA F 23
REMARK 465 ALA F 24
REMARK 465 ALA F 25
REMARK 465 GLU F 26
REMARK 465 ASP F 27
REMARK 465 ASP F 28
REMARK 465 ASP F 29
REMARK 465 ASN F 30
REMARK 465 GLU F 31
REMARK 465 GLN F 32
REMARK 465 HIS F 33
REMARK 465 GLU F 34
REMARK 465 GLU F 35
REMARK 465 LYS F 36
REMARK 465 ALA F 37
REMARK 465 ALA F 38
REMARK 465 GLU F 39
REMARK 465 GLY F 40
REMARK 465 GLU F 41
REMARK 465 GLU F 42
REMARK 465 LYS F 43
REMARK 465 GLU F 44
REMARK 465 GLU F 45
REMARK 465 GLU F 46
REMARK 465 ASN F 47
REMARK 465 GLY F 48
REMARK 465 ASP F 49
REMARK 465 GLU F 50
REMARK 465 ASP F 51
REMARK 465 GLU F 52
REMARK 465 ASP F 53
REMARK 465 GLU F 54
REMARK 465 ASP F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 GLU F 58
REMARK 465 ASP F 59
REMARK 465 ASP F 60
REMARK 465 ASP F 61
REMARK 465 ASP F 62
REMARK 465 ASP F 63
REMARK 465 ASP F 64
REMARK 465 ASP F 65
REMARK 465 GLU F 66
REMARK 465 ASP F 67
REMARK 465 GLU F 68
REMARK 465 GLU F 69
REMARK 465 GLU F 70
REMARK 465 GLU F 71
REMARK 465 GLU F 72
REMARK 465 MET G 1
REMARK 465 MET I 1
REMARK 465 GLY I 59
REMARK 465 ASP I 60
REMARK 465 GLY I 61
REMARK 465 ASP I 62
REMARK 465 ASP I 63
REMARK 465 ASP I 64
REMARK 465 ASP I 65
REMARK 465 GLU I 66
REMARK 465 MET J 1
REMARK 465 LYS O 309
REMARK 465 MET Q 1
REMARK 465 GLY Q 2
REMARK 465 MET Q 3
REMARK 465 LEU Q 4
REMARK 465 GLU Q 5
REMARK 465 LEU Q 6
REMARK 465 VAL Q 7
REMARK 465 GLY Q 8
REMARK 465 GLU Q 9
REMARK 465 TYR Q 10
REMARK 465 TRP Q 11
REMARK 465 GLU Q 12
REMARK 465 GLN Q 13
REMARK 465 LEU Q 14
REMARK 465 LYS Q 15
REMARK 465 ILE Q 16
REMARK 465 THR Q 17
REMARK 465 VAL Q 18
REMARK 465 VAL Q 19
REMARK 465 PRO Q 20
REMARK 465 VAL Q 21
REMARK 465 VAL Q 22
REMARK 465 ALA Q 23
REMARK 465 ALA Q 24
REMARK 465 ALA Q 25
REMARK 465 GLU Q 26
REMARK 465 ASP Q 27
REMARK 465 ASP Q 28
REMARK 465 ASP Q 29
REMARK 465 ASN Q 30
REMARK 465 GLU Q 31
REMARK 465 GLN Q 32
REMARK 465 HIS Q 33
REMARK 465 GLU Q 34
REMARK 465 GLU Q 35
REMARK 465 LYS Q 36
REMARK 465 ALA Q 37
REMARK 465 ALA Q 38
REMARK 465 GLU Q 39
REMARK 465 GLY Q 40
REMARK 465 GLU Q 41
REMARK 465 GLU Q 42
REMARK 465 LYS Q 43
REMARK 465 GLU Q 44
REMARK 465 GLU Q 45
REMARK 465 GLU Q 46
REMARK 465 ASN Q 47
REMARK 465 GLY Q 48
REMARK 465 ASP Q 49
REMARK 465 GLU Q 50
REMARK 465 ASP Q 51
REMARK 465 GLU Q 52
REMARK 465 ASP Q 53
REMARK 465 GLU Q 54
REMARK 465 ASP Q 55
REMARK 465 GLU Q 56
REMARK 465 ASP Q 57
REMARK 465 GLU Q 58
REMARK 465 ASP Q 59
REMARK 465 ASP Q 60
REMARK 465 ASP Q 61
REMARK 465 ASP Q 62
REMARK 465 ASP Q 63
REMARK 465 ASP Q 64
REMARK 465 ASP Q 65
REMARK 465 GLU Q 66
REMARK 465 ASP Q 67
REMARK 465 GLU Q 68
REMARK 465 GLU Q 69
REMARK 465 GLU Q 70
REMARK 465 GLU Q 71
REMARK 465 GLU Q 72
REMARK 465 MET R 1
REMARK 465 MET T 1
REMARK 465 GLY T 59
REMARK 465 ASP T 60
REMARK 465 GLY T 61
REMARK 465 ASP T 62
REMARK 465 ASP T 63
REMARK 465 ASP T 64
REMARK 465 ASP T 65
REMARK 465 GLU T 66
REMARK 465 MET U 1
REMARK 465 GLN d 26
REMARK 465 GLN d 27
REMARK 465 LYS d 28
REMARK 465 ASN d 150
REMARK 465 ASP d 151
REMARK 465 ASP d 152
REMARK 465 HIS d 153
REMARK 465 HIS d 154
REMARK 465 HIS d 155
REMARK 465 SER f 41
REMARK 465 ASP f 42
REMARK 465 ALA f 43
REMARK 465 HIS f 44
REMARK 465 SER f 147
REMARK 465 SER f 148
REMARK 465 ALA j 2
REMARK 465 ASP j 3
REMARK 465 GLN j 4
REMARK 465 GLU j 5
REMARK 465 ASN j 6
REMARK 465 ALA k 10
REMARK 465 SER k 11
REMARK 465 SER k 12
REMARK 465 GLU k 126
REMARK 465 HIS k 127
REMARK 465 ASP k 128
REMARK 465 ASP k 129
REMARK 465 GLY k 130
REMARK 465 ALA k 131
REMARK 465 ARG k 132
REMARK 465 GLY k 133
REMARK 465 SER k 134
REMARK 465 HIS k 135
REMARK 465 HIS k 136
REMARK 465 HIS k 137
REMARK 465 HIS k 138
REMARK 465 HIS k 139
REMARK 465 HIS k 140
REMARK 465 MET l 1
REMARK 465 PHE l 2
REMARK 465 PHE l 3
REMARK 465 SER l 4
REMARK 465 GLN l 5
REMARK 465 VAL l 6
REMARK 465 LEU l 7
REMARK 465 ARG l 8
REMARK 465 SER l 9
REMARK 465 SER l 10
REMARK 465 ALA l 11
REMARK 465 ARG l 12
REMARK 465 ALA l 13
REMARK 465 ALA l 14
REMARK 465 PRO l 15
REMARK 465 ILE l 16
REMARK 465 LYS l 17
REMARK 465 ARG l 18
REMARK 465 TYR l 19
REMARK 465 THR l 20
REMARK 465 GLY l 21
REMARK 465 GLN p 26
REMARK 465 GLN p 27
REMARK 465 LYS p 28
REMARK 465 ASN p 150
REMARK 465 ASP p 151
REMARK 465 ASP p 152
REMARK 465 HIS p 153
REMARK 465 HIS p 154
REMARK 465 HIS p 155
REMARK 465 SER r 41
REMARK 465 ASP r 42
REMARK 465 ALA r 43
REMARK 465 HIS r 44
REMARK 465 SER r 147
REMARK 465 SER r 148
REMARK 465 ALA v 2
REMARK 465 ASP v 3
REMARK 465 GLN v 4
REMARK 465 GLU v 5
REMARK 465 ASN v 6
REMARK 465 ALA w 10
REMARK 465 SER w 11
REMARK 465 SER w 12
REMARK 465 GLU w 126
REMARK 465 HIS w 127
REMARK 465 ASP w 128
REMARK 465 ASP w 129
REMARK 465 GLY w 130
REMARK 465 ALA w 131
REMARK 465 ARG w 132
REMARK 465 GLY w 133
REMARK 465 SER w 134
REMARK 465 HIS w 135
REMARK 465 HIS w 136
REMARK 465 HIS w 137
REMARK 465 HIS w 138
REMARK 465 HIS w 139
REMARK 465 HIS w 140
REMARK 465 MET x 1
REMARK 465 PHE x 2
REMARK 465 PHE x 3
REMARK 465 SER x 4
REMARK 465 GLN x 5
REMARK 465 VAL x 6
REMARK 465 LEU x 7
REMARK 465 ARG x 8
REMARK 465 SER x 9
REMARK 465 SER x 10
REMARK 465 ALA x 11
REMARK 465 ARG x 12
REMARK 465 ALA x 13
REMARK 465 ALA x 14
REMARK 465 PRO x 15
REMARK 465 ILE x 16
REMARK 465 LYS x 17
REMARK 465 ARG x 18
REMARK 465 TYR x 19
REMARK 465 THR x 20
REMARK 465 GLY x 21
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 NE2 HIS m 241 CE2 TYR m 245 1.34
REMARK 500 NE2 HIS a 241 CE2 TYR a 245 1.34
REMARK 500 SG CYS D 101 CBB HEC D 401 1.48
REMARK 500 SG CYS O 101 CBB HEC O 401 1.51
REMARK 500 SG CYS O 104 CBC HEC O 401 1.77
REMARK 500 NE2 HIS m 62 NA HEA m 602 1.92
REMARK 500 CE1 HIS a 62 FE HEA a 602 2.11
REMARK 500 NE2 HIS a 62 NA HEA a 602 2.13
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 LEU E 65 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 LEU c 4 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 ASN A 61 37.17 -99.58
REMARK 500 LEU A 78 35.33 -99.15
REMARK 500 LEU A 251 59.58 -93.33
REMARK 500 ASN A 274 30.31 -99.66
REMARK 500 SER A 357 47.56 -141.60
REMARK 500 MET A 455 47.81 -93.23
REMARK 500 PRO B 25 57.60 -92.28
REMARK 500 PHE B 56 34.78 -95.46
REMARK 500 ARG B 152 -62.94 -94.08
REMARK 500 SER B 262 -179.87 -69.85
REMARK 500 GLU B 337 65.64 60.15
REMARK 500 LEU C 216 -60.62 -90.27
REMARK 500 SER C 223 -5.90 74.35
REMARK 500 ALA C 267 -5.65 69.08
REMARK 500 VAL D 100 -59.25 -123.15
REMARK 500 ASP D 139 -168.88 -76.51
REMARK 500 THR D 297 41.78 -107.56
REMARK 500 GLU F 118 -0.91 65.14
REMARK 500 CYS F 123 32.67 -99.50
REMARK 500 PRO J 72 43.65 -80.78
REMARK 500 LEU L 78 30.98 -96.83
REMARK 500 ILE L 125 -60.75 -92.13
REMARK 500 LEU L 251 55.15 -98.05
REMARK 500 SER L 357 48.56 -141.35
REMARK 500 MET L 455 47.64 -93.59
REMARK 500 THR M 26 -166.88 -125.07
REMARK 500 PHE M 56 32.54 -92.98
REMARK 500 LYS M 222 68.80 62.32
REMARK 500 SER N 223 -5.49 73.44
REMARK 500 ALA N 267 -5.43 69.18
REMARK 500 PRO N 286 49.80 -86.99
REMARK 500 ASP O 108 0.76 -67.75
REMARK 500 ASP O 139 -169.20 -76.71
REMARK 500 THR O 297 42.33 -108.27
REMARK 500 TYR S 9 30.40 -98.91
REMARK 500 ASN T 44 73.51 -102.85
REMARK 500 PRO U 72 44.29 -83.01
REMARK 500 TYR a 7 34.75 -96.06
REMARK 500 LEU a 40 32.81 -93.80
REMARK 500 GLN a 46 -62.15 -97.01
REMARK 500 ASN a 51 62.49 62.03
REMARK 500 PHE a 95 75.13 52.46
REMARK 500 VAL a 129 44.72 -109.25
REMARK 500 ASN a 217 16.52 59.87
REMARK 500 PHE a 497 45.74 -82.77
REMARK 500 VAL a 498 -10.04 -146.31
REMARK 500 ASN a 507 48.00 -141.77
REMARK 500 PRO a 521 126.47 -27.26
REMARK 500 ALA b 29 11.08 -141.05
REMARK 500 HIS b 77 -63.96 -95.53
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL a 119 GLU a 120 -147.99
REMARK 500 SER a 520 PRO a 521 -109.36
REMARK 500 SER m 520 PRO m 521 -107.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEF A 501
REMARK 610 CDL C 604
REMARK 610 PEF C 605
REMARK 610 PEF C 606
REMARK 610 PCF C 607
REMARK 610 PEF D 402
REMARK 610 CDL E 302
REMARK 610 PEF E 303
REMARK 610 CDL H 601
REMARK 610 CDL H 602
REMARK 610 PEF H 603
REMARK 610 PCF H 604
REMARK 610 PCF I 101
REMARK 610 CDL L 501
REMARK 610 PEF N 603
REMARK 610 PEF N 604
REMARK 610 PEF N 605
REMARK 610 CDL O 402
REMARK 610 PEF O 403
REMARK 610 CDL P 302
REMARK 610 PEF P 303
REMARK 610 CDL S 601
REMARK 610 PEF S 602
REMARK 610 PCF S 603
REMARK 610 PCF T 101
REMARK 610 PEF a 607
REMARK 610 PEF a 608
REMARK 610 PEF b 303
REMARK 610 PEF c 301
REMARK 610 PEF c 302
REMARK 610 PCF e 202
REMARK 610 PEF m 607
REMARK 610 PEF n 303
REMARK 610 PEF n 304
REMARK 610 PEF o 301
REMARK 610 PEF o 302
REMARK 610 PCF q 202
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 HEM C 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 82 NE2
REMARK 620 2 HEM C 601 NA 97.9
REMARK 620 3 HEM C 601 NB 87.7 87.2
REMARK 620 4 HEM C 601 NC 80.5 173.7 86.7
REMARK 620 5 HEM C 601 ND 91.5 93.8 178.8 92.4
REMARK 620 6 HIS C 183 NE2 160.7 100.0 100.3 82.4 80.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 96 NE2
REMARK 620 2 HEM C 602 NA 91.4
REMARK 620 3 HEM C 602 NB 99.8 87.2
REMARK 620 4 HEM C 602 NC 94.6 171.9 86.4
REMARK 620 5 HEM C 602 ND 81.8 93.2 178.3 93.0
REMARK 620 6 HIS C 197 NE2 166.1 87.7 94.0 87.8 84.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 105 NE2
REMARK 620 2 HEC D 401 NA 82.2
REMARK 620 3 HEC D 401 NB 85.2 89.4
REMARK 620 4 HEC D 401 NC 96.0 178.2 90.4
REMARK 620 5 HEC D 401 ND 92.8 90.0 178.0 90.1
REMARK 620 6 MET D 225 SD 169.8 94.3 85.2 87.5 96.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 159 SG
REMARK 620 2 FES E 301 S1 109.9
REMARK 620 3 FES E 301 S2 140.7 89.5
REMARK 620 4 CYS E 178 SG 107.0 67.2 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 161 ND1
REMARK 620 2 FES E 301 S1 123.1
REMARK 620 3 FES E 301 S2 132.0 89.4
REMARK 620 4 HIS E 181 ND1 91.1 107.4 113.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM N 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 82 NE2
REMARK 620 2 HEM N 601 NA 96.8
REMARK 620 3 HEM N 601 NB 96.3 88.4
REMARK 620 4 HEM N 601 NC 84.4 173.8 85.3
REMARK 620 5 HEM N 601 ND 84.7 95.3 176.0 90.9
REMARK 620 6 HIS N 183 NE2 161.7 98.7 93.8 81.2 84.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM N 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 96 NE2
REMARK 620 2 HEM N 602 NA 90.1
REMARK 620 3 HEM N 602 NB 98.8 86.9
REMARK 620 4 HEM N 602 NC 95.2 172.2 86.7
REMARK 620 5 HEM N 602 ND 82.6 93.7 178.5 92.6
REMARK 620 6 HIS N 197 NE2 164.3 88.6 96.7 87.9 82.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC O 401 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 105 NE2
REMARK 620 2 HEC O 401 NA 92.0
REMARK 620 3 HEC O 401 NB 100.5 90.2
REMARK 620 4 HEC O 401 NC 84.2 176.2 90.1
REMARK 620 5 HEC O 401 ND 75.6 89.1 176.1 90.4
REMARK 620 6 MET O 225 SD 155.4 93.1 103.4 90.5 80.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES P 301 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS P 159 SG
REMARK 620 2 FES P 301 S1 117.8
REMARK 620 3 FES P 301 S2 140.7 89.2
REMARK 620 4 CYS P 178 SG 103.2 79.3 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES P 301 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 161 ND1
REMARK 620 2 FES P 301 S1 124.7
REMARK 620 3 FES P 301 S2 132.1 89.0
REMARK 620 4 HIS P 181 ND1 87.5 107.5 116.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA a 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU a 39 O
REMARK 620 2 GLU a 39 OE1 61.0
REMARK 620 3 ALA a 42 O 98.7 148.7
REMARK 620 4 GLY a 44 O 118.7 89.2 80.1
REMARK 620 5 PRO a 441 O 103.4 64.9 146.4 110.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA a 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 62 NE2
REMARK 620 2 HEA a 602 NA 65.4
REMARK 620 3 HEA a 602 NB 111.9 92.8
REMARK 620 4 HEA a 602 NC 107.3 172.5 88.6
REMARK 620 5 HEA a 602 ND 69.4 89.1 178.1 89.7
REMARK 620 6 HIS a 378 NE2 163.6 115.2 84.5 72.3 94.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU a 601 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 241 ND1
REMARK 620 2 HIS a 290 NE2 106.4
REMARK 620 3 HIS a 291 NE2 133.2 91.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG a 605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP a 369 OD1
REMARK 620 2 GLU b 223 OE1 110.8
REMARK 620 3 GLU b 223 OE2 116.7 55.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA a 603 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS a 376 NE2
REMARK 620 2 HEA a 603 NA 79.2
REMARK 620 3 HEA a 603 NB 90.5 90.5
REMARK 620 4 HEA a 603 NC 97.0 176.2 89.5
REMARK 620 5 HEA a 603 ND 93.6 91.6 175.7 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA b 301 CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS b 186 ND1
REMARK 620 2 CYS b 221 SG 125.6
REMARK 620 3 CYS b 225 SG 82.1 81.2
REMARK 620 4 MET b 232 SD 99.9 128.4 132.9
REMARK 620 5 CUA b 302 CU2 132.1 52.3 50.2 114.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA b 302 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS b 221 SG
REMARK 620 2 GLU b 223 O 83.3
REMARK 620 3 CYS b 225 SG 84.9 76.3
REMARK 620 4 HIS b 229 ND1 151.7 82.1 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN d 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS d 111 SG
REMARK 620 2 CYS d 134 SG 85.0
REMARK 620 3 CYS d 137 SG 150.3 93.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA m 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU m 39 O
REMARK 620 2 ALA m 42 O 99.6
REMARK 620 3 GLY m 44 O 107.7 71.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA m 602 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS m 62 NE2
REMARK 620 2 HEA m 602 NA 58.1
REMARK 620 3 HEA m 602 NB 90.6 92.0
REMARK 620 4 HEA m 602 NC 117.1 175.2 88.3
REMARK 620 5 HEA m 602 ND 92.5 90.6 176.7 89.3
REMARK 620 6 HIS m 378 NE2 161.8 106.8 79.1 77.9 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU m 601 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS m 241 ND1
REMARK 620 2 HIS m 290 NE2 98.8
REMARK 620 3 HIS m 291 NE2 128.8 90.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG m 605 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP m 369 OD1
REMARK 620 2 GLU n 223 OE1 123.8
REMARK 620 3 GLU n 223 OE2 105.7 53.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEA m 603 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS m 376 NE2
REMARK 620 2 HEA m 603 NA 74.7
REMARK 620 3 HEA m 603 NB 100.1 90.8
REMARK 620 4 HEA m 603 NC 101.1 175.8 89.4
REMARK 620 5 HEA m 603 ND 83.6 91.6 176.1 88.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA n 301 CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS n 186 ND1
REMARK 620 2 CYS n 221 SG 122.7
REMARK 620 3 CYS n 225 SG 78.4 78.4
REMARK 620 4 MET n 232 SD 111.9 112.2 153.3
REMARK 620 5 CUA n 302 CU2 134.1 54.5 55.8 109.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CUA n 302 CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS n 221 SG
REMARK 620 2 GLU n 223 O 80.2
REMARK 620 3 CYS n 225 SG 75.2 87.6
REMARK 620 4 HIS n 229 ND1 117.9 70.8 151.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN p 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS p 111 SG
REMARK 620 2 CYS p 134 SG 81.3
REMARK 620 3 CYS p 137 SG 135.5 91.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UQ6 C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL C 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF C 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF C 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEC D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FES E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL E 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF E 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL H 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL H 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF H 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF H 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF I 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM N 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM N 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF N 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF N 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF N 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF N 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEC O 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL O 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF O 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FES P 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL P 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF P 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL S 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF S 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF S 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF T 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU a 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA a 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA a 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA a 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG a 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF a 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF a 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF a 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA b 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA b 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF b 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF c 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF c 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN d 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF e 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF e 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF h 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CU m 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA m 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEA m 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA m 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG m 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF m 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF m 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA n 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CUA n 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF n 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF n 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF o 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF o 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN p 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF q 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PCF q 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEF t 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-0262 RELATED DB: EMDB
REMARK 900 BC1 (CHAINS A,B,C,D,E,F,G,H,I,J,L,M,N,O,P,Q,R,S,T,U)
REMARK 900 RELATED ID: EMD-0269 RELATED DB: EMDB
REMARK 900 CIV 1 (CHAINS A,B,C,D,E,F,G,H,I,J,K,L,Y)
REMARK 900 RELATED ID: EMD-0268 RELATED DB: EMDB
REMARK 900 CIV 2 (CHAINS M,N,O,P,Q,R,S,T,U,V,W,Z)
DBREF 6HU9 A 27 457 UNP P07256 QCR1_YEAST 27 457
DBREF 6HU9 B 17 368 UNP P07257 QCR2_YEAST 17 368
DBREF 6HU9 C 1 385 UNP P00163 CYB_YEAST 1 385
DBREF 6HU9 D 62 309 UNP P07143 CY1_YEAST 62 309
DBREF 6HU9 E 31 215 UNP P08067 UCRI_YEAST 31 215
DBREF 6HU9 F 1 147 UNP P00127 QCR6_YEAST 1 147
DBREF 6HU9 G 1 127 UNP P00128 QCR7_YEAST 1 127
DBREF 6HU9 H 2 94 UNP P08525 QCR8_YEAST 2 94
DBREF 6HU9 I 1 66 UNP P22289 QCR9_YEAST 1 66
DBREF 6HU9 J 1 77 UNP P37299 QCR10_YEAST 1 77
DBREF 6HU9 L 27 457 UNP P07256 QCR1_YEAST 27 457
DBREF 6HU9 M 17 368 UNP P07257 QCR2_YEAST 17 368
DBREF 6HU9 N 1 385 UNP P00163 CYB_YEAST 1 385
DBREF 6HU9 O 62 309 UNP P07143 CY1_YEAST 62 309
DBREF 6HU9 P 31 215 UNP P08067 UCRI_YEAST 31 215
DBREF 6HU9 Q 1 147 UNP P00127 QCR6_YEAST 1 147
DBREF 6HU9 R 1 127 UNP P00128 QCR7_YEAST 1 127
DBREF 6HU9 S 2 94 UNP P08525 QCR8_YEAST 2 94
DBREF 6HU9 T 1 66 UNP P22289 QCR9_YEAST 1 66
DBREF 6HU9 U 1 77 UNP P37299 QCR10_YEAST 1 77
DBREF 6HU9 a 1 534 UNP P00401 COX1_YEAST 1 534
DBREF 6HU9 b 16 251 UNP P00410 COX2_YEAST 16 251
DBREF 6HU9 c 1 269 UNP P00420 COX3_YEAST 1 269
DBREF 6HU9 d 26 155 UNP P04037 COX4_YEAST 26 155
DBREF 6HU9 e 21 153 UNP P00424 COX5A_YEAST 21 153
DBREF 6HU9 f 41 148 UNP P00427 COX6_YEAST 41 148
DBREF 6HU9 g 2 60 UNP P10174 COX7_YEAST 2 60
DBREF 6HU9 h 28 74 UNP P04039 COX8_YEAST 28 74
DBREF 6HU9 i 2 56 UNP P07255 COX9_YEAST 2 56
DBREF 6HU9 j 2 83 UNP Q01519 COX12_YEAST 2 83
DBREF 6HU9 k 10 129 UNP P32799 COX13_YEAST 10 129
DBREF 6HU9 l 1 66 UNP Q2V2P9 YD19A_YEAST 1 66
DBREF 6HU9 m 1 534 UNP P00401 COX1_YEAST 1 534
DBREF 6HU9 n 16 251 UNP P00410 COX2_YEAST 16 251
DBREF 6HU9 o 1 269 UNP P00420 COX3_YEAST 1 269
DBREF 6HU9 p 26 155 UNP P04037 COX4_YEAST 26 155
DBREF 6HU9 q 21 153 UNP P00424 COX5A_YEAST 21 153
DBREF 6HU9 r 41 148 UNP P00427 COX6_YEAST 41 148
DBREF 6HU9 s 2 60 UNP P10174 COX7_YEAST 2 60
DBREF 6HU9 t 28 74 UNP P04039 COX8_YEAST 28 74
DBREF 6HU9 u 2 56 UNP P07255 COX9_YEAST 2 56
DBREF 6HU9 v 2 83 UNP Q01519 COX12_YEAST 2 83
DBREF 6HU9 w 10 129 UNP P32799 COX13_YEAST 10 129
DBREF 6HU9 x 1 66 UNP Q2V2P9 YD19A_YEAST 1 66
SEQADV 6HU9 GLY k 130 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 ALA k 131 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 ARG k 132 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 GLY k 133 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 SER k 134 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 135 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 136 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 137 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 138 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 139 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS k 140 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 GLY w 130 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 ALA w 131 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 ARG w 132 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 GLY w 133 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 SER w 134 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 135 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 136 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 137 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 138 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 139 UNP P32799 EXPRESSION TAG
SEQADV 6HU9 HIS w 140 UNP P32799 EXPRESSION TAG
SEQRES 1 A 431 ALA GLU VAL THR GLN LEU SER ASN GLY ILE VAL VAL ALA
SEQRES 2 A 431 THR GLU HIS ASN PRO SER ALA HIS THR ALA SER VAL GLY
SEQRES 3 A 431 VAL VAL PHE GLY SER GLY ALA ALA ASN GLU ASN PRO TYR
SEQRES 4 A 431 ASN ASN GLY VAL SER ASN LEU TRP LYS ASN ILE PHE LEU
SEQRES 5 A 431 SER LYS GLU ASN SER ALA VAL ALA ALA LYS GLU GLY LEU
SEQRES 6 A 431 ALA LEU SER SER ASN ILE SER ARG ASP PHE GLN SER TYR
SEQRES 7 A 431 ILE VAL SER SER LEU PRO GLY SER THR ASP LYS SER LEU
SEQRES 8 A 431 ASP PHE LEU ASN GLN SER PHE ILE GLN GLN LYS ALA ASN
SEQRES 9 A 431 LEU LEU SER SER SER ASN PHE GLU ALA THR LYS LYS SER
SEQRES 10 A 431 VAL LEU LYS GLN VAL GLN ASP PHE GLU GLU ASN ASP HIS
SEQRES 11 A 431 PRO ASN ARG VAL LEU GLU HIS LEU HIS SER THR ALA PHE
SEQRES 12 A 431 GLN ASN THR PRO LEU SER LEU PRO THR ARG GLY THR LEU
SEQRES 13 A 431 GLU SER LEU GLU ASN LEU VAL VAL ALA ASP LEU GLU SER
SEQRES 14 A 431 PHE ALA ASN ASN HIS PHE LEU ASN SER ASN ALA VAL VAL
SEQRES 15 A 431 VAL GLY THR GLY ASN ILE LYS HIS GLU ASP LEU VAL ASN
SEQRES 16 A 431 SER ILE GLU SER LYS ASN LEU SER LEU GLN THR GLY THR
SEQRES 17 A 431 LYS PRO VAL LEU LYS LYS LYS ALA ALA PHE LEU GLY SER
SEQRES 18 A 431 GLU VAL ARG LEU ARG ASP ASP THR LEU PRO LYS ALA TRP
SEQRES 19 A 431 ILE SER LEU ALA VAL GLU GLY GLU PRO VAL ASN SER PRO
SEQRES 20 A 431 ASN TYR PHE VAL ALA LYS LEU ALA ALA GLN ILE PHE GLY
SEQRES 21 A 431 SER TYR ASN ALA PHE GLU PRO ALA SER ARG LEU GLN GLY
SEQRES 22 A 431 ILE LYS LEU LEU ASP ASN ILE GLN GLU TYR GLN LEU CYS
SEQRES 23 A 431 ASP ASN PHE ASN HIS PHE SER LEU SER TYR LYS ASP SER
SEQRES 24 A 431 GLY LEU TRP GLY PHE SER THR ALA THR ARG ASN VAL THR
SEQRES 25 A 431 MET ILE ASP ASP LEU ILE HIS PHE THR LEU LYS GLN TRP
SEQRES 26 A 431 ASN ARG LEU THR ILE SER VAL THR ASP THR GLU VAL GLU
SEQRES 27 A 431 ARG ALA LYS SER LEU LEU LYS LEU GLN LEU GLY GLN LEU
SEQRES 28 A 431 TYR GLU SER GLY ASN PRO VAL ASN ASP ALA ASN LEU LEU
SEQRES 29 A 431 GLY ALA GLU VAL LEU ILE LYS GLY SER LYS LEU SER LEU
SEQRES 30 A 431 GLY GLU ALA PHE LYS LYS ILE ASP ALA ILE THR VAL LYS
SEQRES 31 A 431 ASP VAL LYS ALA TRP ALA GLY LYS ARG LEU TRP ASP GLN
SEQRES 32 A 431 ASP ILE ALA ILE ALA GLY THR GLY GLN ILE GLU GLY LEU
SEQRES 33 A 431 LEU ASP TYR MET ARG ILE ARG SER ASP MET SER MET MET
SEQRES 34 A 431 ARG TRP
SEQRES 1 B 352 LEU THR VAL SER ALA ARG ASP ALA PRO THR LYS ILE SER
SEQRES 2 B 352 THR LEU ALA VAL LYS VAL HIS GLY GLY SER ARG TYR ALA
SEQRES 3 B 352 THR LYS ASP GLY VAL ALA HIS LEU LEU ASN ARG PHE ASN
SEQRES 4 B 352 PHE GLN ASN THR ASN THR ARG SER ALA LEU LYS LEU VAL
SEQRES 5 B 352 ARG GLU SER GLU LEU LEU GLY GLY THR PHE LYS SER THR
SEQRES 6 B 352 LEU ASP ARG GLU TYR ILE THR LEU LYS ALA THR PHE LEU
SEQRES 7 B 352 LYS ASP ASP LEU PRO TYR TYR VAL ASN ALA LEU ALA ASP
SEQRES 8 B 352 VAL LEU TYR LYS THR ALA PHE LYS PRO HIS GLU LEU THR
SEQRES 9 B 352 GLU SER VAL LEU PRO ALA ALA ARG TYR ASP TYR ALA VAL
SEQRES 10 B 352 ALA GLU GLN CYS PRO VAL LYS SER ALA GLU ASP GLN LEU
SEQRES 11 B 352 TYR ALA ILE THR PHE ARG LYS GLY LEU GLY ASN PRO LEU
SEQRES 12 B 352 LEU TYR ASP GLY VAL GLU ARG VAL SER LEU GLN ASP ILE
SEQRES 13 B 352 LYS ASP PHE ALA ASP LYS VAL TYR THR LYS GLU ASN LEU
SEQRES 14 B 352 GLU VAL SER GLY GLU ASN VAL VAL GLU ALA ASP LEU LYS
SEQRES 15 B 352 ARG PHE VAL ASP GLU SER LEU LEU SER THR LEU PRO ALA
SEQRES 16 B 352 GLY LYS SER LEU VAL SER LYS SER GLU PRO LYS PHE PHE
SEQRES 17 B 352 LEU GLY GLU GLU ASN ARG VAL ARG PHE ILE GLY ASP SER
SEQRES 18 B 352 VAL ALA ALA ILE GLY ILE PRO VAL ASN LYS ALA SER LEU
SEQRES 19 B 352 ALA GLN TYR GLU VAL LEU ALA ASN TYR LEU THR SER ALA
SEQRES 20 B 352 LEU SER GLU LEU SER GLY LEU ILE SER SER ALA LYS LEU
SEQRES 21 B 352 ASP LYS PHE THR ASP GLY GLY LEU PHE THR LEU PHE VAL
SEQRES 22 B 352 ARG ASP GLN ASP SER ALA VAL VAL SER SER ASN ILE LYS
SEQRES 23 B 352 LYS ILE VAL ALA ASP LEU LYS LYS GLY LYS ASP LEU SER
SEQRES 24 B 352 PRO ALA ILE ASN TYR THR LYS LEU LYS ASN ALA VAL GLN
SEQRES 25 B 352 ASN GLU SER VAL SER SER PRO ILE GLU LEU ASN PHE ASP
SEQRES 26 B 352 ALA VAL LYS ASP PHE LYS LEU GLY LYS PHE ASN TYR VAL
SEQRES 27 B 352 ALA VAL GLY ASP VAL SER ASN LEU PRO TYR LEU ASP GLU
SEQRES 28 B 352 LEU
SEQRES 1 C 385 MET ALA PHE ARG LYS SER ASN VAL TYR LEU SER LEU VAL
SEQRES 2 C 385 ASN SER TYR ILE ILE ASP SER PRO GLN PRO SER SER ILE
SEQRES 3 C 385 ASN TYR TRP TRP ASN MET GLY SER LEU LEU GLY LEU CYS
SEQRES 4 C 385 LEU VAL ILE GLN ILE VAL THR GLY ILE PHE MET ALA MET
SEQRES 5 C 385 HIS TYR SER SER ASN ILE GLU LEU ALA PHE SER SER VAL
SEQRES 6 C 385 GLU HIS ILE MET ARG ASP VAL HIS ASN GLY TYR ILE LEU
SEQRES 7 C 385 ARG TYR LEU HIS ALA ASN GLY ALA SER PHE PHE PHE MET
SEQRES 8 C 385 VAL MET PHE MET HIS MET ALA LYS GLY LEU TYR TYR GLY
SEQRES 9 C 385 SER TYR ARG SER PRO ARG VAL THR LEU TRP ASN VAL GLY
SEQRES 10 C 385 VAL ILE ILE PHE ILE LEU THR ILE ALA THR ALA PHE LEU
SEQRES 11 C 385 GLY TYR CYS CYS VAL TYR GLY GLN MET SER HIS TRP GLY
SEQRES 12 C 385 ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO PHE
SEQRES 13 C 385 VAL GLY ASN ASP ILE VAL SER TRP LEU TRP GLY GLY PHE
SEQRES 14 C 385 SER VAL SER ASN PRO THR ILE GLN ARG PHE PHE ALA LEU
SEQRES 15 C 385 HIS TYR LEU VAL PRO PHE ILE ILE ALA ALA MET VAL ILE
SEQRES 16 C 385 MET HIS LEU MET ALA LEU HIS ILE HIS GLY SER SER ASN
SEQRES 17 C 385 PRO LEU GLY ILE THR GLY ASN LEU ASP ARG ILE PRO MET
SEQRES 18 C 385 HIS SER TYR PHE ILE PHE LYS ASP LEU VAL THR VAL PHE
SEQRES 19 C 385 LEU PHE MET LEU ILE LEU ALA LEU PHE VAL PHE TYR SER
SEQRES 20 C 385 PRO ASN THR LEU GLY HIS PRO ASP ASN TYR ILE PRO GLY
SEQRES 21 C 385 ASN PRO LEU VAL THR PRO ALA SER ILE VAL PRO GLU TRP
SEQRES 22 C 385 TYR LEU LEU PRO PHE TYR ALA ILE LEU ARG SER ILE PRO
SEQRES 23 C 385 ASP LYS LEU LEU GLY VAL ILE THR MET PHE ALA ALA ILE
SEQRES 24 C 385 LEU VAL LEU LEU VAL LEU PRO PHE THR ASP ARG SER VAL
SEQRES 25 C 385 VAL ARG GLY ASN THR PHE LYS VAL LEU SER LYS PHE PHE
SEQRES 26 C 385 PHE PHE ILE PHE VAL PHE ASN PHE VAL LEU LEU GLY GLN
SEQRES 27 C 385 ILE GLY ALA CYS HIS VAL GLU VAL PRO TYR VAL LEU MET
SEQRES 28 C 385 GLY GLN ILE ALA THR PHE ILE TYR PHE ALA TYR PHE LEU
SEQRES 29 C 385 ILE ILE VAL PRO VAL ILE SER THR ILE GLU ASN VAL LEU
SEQRES 30 C 385 PHE TYR ILE GLY ARG VAL ASN LYS
SEQRES 1 D 248 MET THR ALA ALA GLU HIS GLY LEU HIS ALA PRO ALA TYR
SEQRES 2 D 248 ALA TRP SER HIS ASN GLY PRO PHE GLU THR PHE ASP HIS
SEQRES 3 D 248 ALA SER ILE ARG ARG GLY TYR GLN VAL TYR ARG GLU VAL
SEQRES 4 D 248 CYS ALA ALA CYS HIS SER LEU ASP ARG VAL ALA TRP ARG
SEQRES 5 D 248 THR LEU VAL GLY VAL SER HIS THR ASN GLU GLU VAL ARG
SEQRES 6 D 248 ASN MET ALA GLU GLU PHE GLU TYR ASP ASP GLU PRO ASP
SEQRES 7 D 248 GLU GLN GLY ASN PRO LYS LYS ARG PRO GLY LYS LEU SER
SEQRES 8 D 248 ASP TYR ILE PRO GLY PRO TYR PRO ASN GLU GLN ALA ALA
SEQRES 9 D 248 ARG ALA ALA ASN GLN GLY ALA LEU PRO PRO ASP LEU SER
SEQRES 10 D 248 LEU ILE VAL LYS ALA ARG HIS GLY GLY CYS ASP TYR ILE
SEQRES 11 D 248 PHE SER LEU LEU THR GLY TYR PRO ASP GLU PRO PRO ALA
SEQRES 12 D 248 GLY VAL ALA LEU PRO PRO GLY SER ASN TYR ASN PRO TYR
SEQRES 13 D 248 PHE PRO GLY GLY SER ILE ALA MET ALA ARG VAL LEU PHE
SEQRES 14 D 248 ASP ASP MET VAL GLU TYR GLU ASP GLY THR PRO ALA THR
SEQRES 15 D 248 THR SER GLN MET ALA LYS ASP VAL THR THR PHE LEU ASN
SEQRES 16 D 248 TRP CYS ALA GLU PRO GLU HIS ASP GLU ARG LYS ARG LEU
SEQRES 17 D 248 GLY LEU LYS THR VAL ILE ILE LEU SER SER LEU TYR LEU
SEQRES 18 D 248 LEU SER ILE TRP VAL LYS LYS PHE LYS TRP ALA GLY ILE
SEQRES 19 D 248 LYS THR ARG LYS PHE VAL PHE ASN PRO PRO LYS PRO ARG
SEQRES 20 D 248 LYS
SEQRES 1 E 185 LYS SER THR TYR ARG THR PRO ASN PHE ASP ASP VAL LEU
SEQRES 2 E 185 LYS GLU ASN ASN ASP ALA ASP LYS GLY ARG SER TYR ALA
SEQRES 3 E 185 TYR PHE MET VAL GLY ALA MET GLY LEU LEU SER SER ALA
SEQRES 4 E 185 GLY ALA LYS SER THR VAL GLU THR PHE ILE SER SER MET
SEQRES 5 E 185 THR ALA THR ALA ASP VAL LEU ALA MET ALA LYS VAL GLU
SEQRES 6 E 185 VAL ASN LEU ALA ALA ILE PRO LEU GLY LYS ASN VAL VAL
SEQRES 7 E 185 VAL LYS TRP GLN GLY LYS PRO VAL PHE ILE ARG HIS ARG
SEQRES 8 E 185 THR PRO HIS GLU ILE GLN GLU ALA ASN SER VAL ASP MET
SEQRES 9 E 185 SER ALA LEU LYS ASP PRO GLN THR ASP ALA ASP ARG VAL
SEQRES 10 E 185 LYS ASP PRO GLN TRP LEU ILE MET LEU GLY ILE CYS THR
SEQRES 11 E 185 HIS LEU GLY CYS VAL PRO ILE GLY GLU ALA GLY ASP PHE
SEQRES 12 E 185 GLY GLY TRP PHE CYS PRO CYS HIS GLY SER HIS TYR ASP
SEQRES 13 E 185 ILE SER GLY ARG ILE ARG LYS GLY PRO ALA PRO LEU ASN
SEQRES 14 E 185 LEU GLU ILE PRO ALA TYR GLU PHE ASP GLY ASP LYS VAL
SEQRES 15 E 185 ILE VAL GLY
SEQRES 1 F 147 MET GLY MET LEU GLU LEU VAL GLY GLU TYR TRP GLU GLN
SEQRES 2 F 147 LEU LYS ILE THR VAL VAL PRO VAL VAL ALA ALA ALA GLU
SEQRES 3 F 147 ASP ASP ASP ASN GLU GLN HIS GLU GLU LYS ALA ALA GLU
SEQRES 4 F 147 GLY GLU GLU LYS GLU GLU GLU ASN GLY ASP GLU ASP GLU
SEQRES 5 F 147 ASP GLU ASP GLU ASP GLU ASP ASP ASP ASP ASP ASP ASP
SEQRES 6 F 147 GLU ASP GLU GLU GLU GLU GLU GLU VAL THR ASP GLN LEU
SEQRES 7 F 147 GLU ASP LEU ARG GLU HIS PHE LYS ASN THR GLU GLU GLY
SEQRES 8 F 147 LYS ALA LEU VAL HIS HIS TYR GLU GLU CYS ALA GLU ARG
SEQRES 9 F 147 VAL LYS ILE GLN GLN GLN GLN PRO GLY TYR ALA ASP LEU
SEQRES 10 F 147 GLU HIS LYS GLU ASP CYS VAL GLU GLU PHE PHE HIS LEU
SEQRES 11 F 147 GLN HIS TYR LEU ASP THR ALA THR ALA PRO ARG LEU PHE
SEQRES 12 F 147 ASP LYS LEU LYS
SEQRES 1 G 127 MET PRO GLN SER PHE THR SER ILE ALA ARG ILE GLY ASP
SEQRES 2 G 127 TYR ILE LEU LYS SER PRO VAL LEU SER LYS LEU CYS VAL
SEQRES 3 G 127 PRO VAL ALA ASN GLN PHE ILE ASN LEU ALA GLY TYR LYS
SEQRES 4 G 127 LYS LEU GLY LEU LYS PHE ASP ASP LEU ILE ALA GLU GLU
SEQRES 5 G 127 ASN PRO ILE MET GLN THR ALA LEU ARG ARG LEU PRO GLU
SEQRES 6 G 127 ASP GLU SER TYR ALA ARG ALA TYR ARG ILE ILE ARG ALA
SEQRES 7 G 127 HIS GLN THR GLU LEU THR HIS HIS LEU LEU PRO ARG ASN
SEQRES 8 G 127 GLU TRP ILE LYS ALA GLN GLU ASP VAL PRO TYR LEU LEU
SEQRES 9 G 127 PRO TYR ILE LEU GLU ALA GLU ALA ALA ALA LYS GLU LYS
SEQRES 10 G 127 ASP GLU LEU ASP ASN ILE GLU VAL SER LYS
SEQRES 1 H 93 GLY PRO PRO SER GLY LYS THR TYR MET GLY TRP TRP GLY
SEQRES 2 H 93 HIS MET GLY GLY PRO LYS GLN LYS GLY ILE THR SER TYR
SEQRES 3 H 93 ALA VAL SER PRO TYR ALA GLN LYS PRO LEU GLN GLY ILE
SEQRES 4 H 93 PHE HIS ASN ALA VAL PHE ASN SER PHE ARG ARG PHE LYS
SEQRES 5 H 93 SER GLN PHE LEU TYR VAL LEU ILE PRO ALA GLY ILE TYR
SEQRES 6 H 93 TRP TYR TRP TRP LYS ASN GLY ASN GLU TYR ASN GLU PHE
SEQRES 7 H 93 LEU TYR SER LYS ALA GLY ARG GLU GLU LEU GLU ARG VAL
SEQRES 8 H 93 ASN VAL
SEQRES 1 I 66 MET SER PHE SER SER LEU TYR LYS THR PHE PHE LYS ARG
SEQRES 2 I 66 ASN ALA VAL PHE VAL GLY THR ILE PHE ALA GLY ALA PHE
SEQRES 3 I 66 VAL PHE GLN THR VAL PHE ASP THR ALA ILE THR SER TRP
SEQRES 4 I 66 TYR GLU ASN HIS ASN LYS GLY LYS LEU TRP LYS ASP VAL
SEQRES 5 I 66 LYS ALA ARG ILE ALA ALA GLY ASP GLY ASP ASP ASP ASP
SEQRES 6 I 66 GLU
SEQRES 1 J 77 MET ALA TYR THR SER HIS LEU SER SER LYS THR GLY LEU
SEQRES 2 J 77 HIS PHE GLY ARG LEU SER LEU ARG SER LEU THR ALA TYR
SEQRES 3 J 77 ALA PRO ASN LEU MET LEU TRP GLY GLY ALA SER MET LEU
SEQRES 4 J 77 GLY LEU PHE VAL PHE THR GLU GLY TRP PRO LYS PHE GLN
SEQRES 5 J 77 ASP THR LEU TYR LYS LYS ILE PRO LEU LEU GLY PRO THR
SEQRES 6 J 77 LEU GLU ASP HIS THR PRO PRO GLU ASP LYS PRO ASN
SEQRES 1 L 431 ALA GLU VAL THR GLN LEU SER ASN GLY ILE VAL VAL ALA
SEQRES 2 L 431 THR GLU HIS ASN PRO SER ALA HIS THR ALA SER VAL GLY
SEQRES 3 L 431 VAL VAL PHE GLY SER GLY ALA ALA ASN GLU ASN PRO TYR
SEQRES 4 L 431 ASN ASN GLY VAL SER ASN LEU TRP LYS ASN ILE PHE LEU
SEQRES 5 L 431 SER LYS GLU ASN SER ALA VAL ALA ALA LYS GLU GLY LEU
SEQRES 6 L 431 ALA LEU SER SER ASN ILE SER ARG ASP PHE GLN SER TYR
SEQRES 7 L 431 ILE VAL SER SER LEU PRO GLY SER THR ASP LYS SER LEU
SEQRES 8 L 431 ASP PHE LEU ASN GLN SER PHE ILE GLN GLN LYS ALA ASN
SEQRES 9 L 431 LEU LEU SER SER SER ASN PHE GLU ALA THR LYS LYS SER
SEQRES 10 L 431 VAL LEU LYS GLN VAL GLN ASP PHE GLU GLU ASN ASP HIS
SEQRES 11 L 431 PRO ASN ARG VAL LEU GLU HIS LEU HIS SER THR ALA PHE
SEQRES 12 L 431 GLN ASN THR PRO LEU SER LEU PRO THR ARG GLY THR LEU
SEQRES 13 L 431 GLU SER LEU GLU ASN LEU VAL VAL ALA ASP LEU GLU SER
SEQRES 14 L 431 PHE ALA ASN ASN HIS PHE LEU ASN SER ASN ALA VAL VAL
SEQRES 15 L 431 VAL GLY THR GLY ASN ILE LYS HIS GLU ASP LEU VAL ASN
SEQRES 16 L 431 SER ILE GLU SER LYS ASN LEU SER LEU GLN THR GLY THR
SEQRES 17 L 431 LYS PRO VAL LEU LYS LYS LYS ALA ALA PHE LEU GLY SER
SEQRES 18 L 431 GLU VAL ARG LEU ARG ASP ASP THR LEU PRO LYS ALA TRP
SEQRES 19 L 431 ILE SER LEU ALA VAL GLU GLY GLU PRO VAL ASN SER PRO
SEQRES 20 L 431 ASN TYR PHE VAL ALA LYS LEU ALA ALA GLN ILE PHE GLY
SEQRES 21 L 431 SER TYR ASN ALA PHE GLU PRO ALA SER ARG LEU GLN GLY
SEQRES 22 L 431 ILE LYS LEU LEU ASP ASN ILE GLN GLU TYR GLN LEU CYS
SEQRES 23 L 431 ASP ASN PHE ASN HIS PHE SER LEU SER TYR LYS ASP SER
SEQRES 24 L 431 GLY LEU TRP GLY PHE SER THR ALA THR ARG ASN VAL THR
SEQRES 25 L 431 MET ILE ASP ASP LEU ILE HIS PHE THR LEU LYS GLN TRP
SEQRES 26 L 431 ASN ARG LEU THR ILE SER VAL THR ASP THR GLU VAL GLU
SEQRES 27 L 431 ARG ALA LYS SER LEU LEU LYS LEU GLN LEU GLY GLN LEU
SEQRES 28 L 431 TYR GLU SER GLY ASN PRO VAL ASN ASP ALA ASN LEU LEU
SEQRES 29 L 431 GLY ALA GLU VAL LEU ILE LYS GLY SER LYS LEU SER LEU
SEQRES 30 L 431 GLY GLU ALA PHE LYS LYS ILE ASP ALA ILE THR VAL LYS
SEQRES 31 L 431 ASP VAL LYS ALA TRP ALA GLY LYS ARG LEU TRP ASP GLN
SEQRES 32 L 431 ASP ILE ALA ILE ALA GLY THR GLY GLN ILE GLU GLY LEU
SEQRES 33 L 431 LEU ASP TYR MET ARG ILE ARG SER ASP MET SER MET MET
SEQRES 34 L 431 ARG TRP
SEQRES 1 M 352 LEU THR VAL SER ALA ARG ASP ALA PRO THR LYS ILE SER
SEQRES 2 M 352 THR LEU ALA VAL LYS VAL HIS GLY GLY SER ARG TYR ALA
SEQRES 3 M 352 THR LYS ASP GLY VAL ALA HIS LEU LEU ASN ARG PHE ASN
SEQRES 4 M 352 PHE GLN ASN THR ASN THR ARG SER ALA LEU LYS LEU VAL
SEQRES 5 M 352 ARG GLU SER GLU LEU LEU GLY GLY THR PHE LYS SER THR
SEQRES 6 M 352 LEU ASP ARG GLU TYR ILE THR LEU LYS ALA THR PHE LEU
SEQRES 7 M 352 LYS ASP ASP LEU PRO TYR TYR VAL ASN ALA LEU ALA ASP
SEQRES 8 M 352 VAL LEU TYR LYS THR ALA PHE LYS PRO HIS GLU LEU THR
SEQRES 9 M 352 GLU SER VAL LEU PRO ALA ALA ARG TYR ASP TYR ALA VAL
SEQRES 10 M 352 ALA GLU GLN CYS PRO VAL LYS SER ALA GLU ASP GLN LEU
SEQRES 11 M 352 TYR ALA ILE THR PHE ARG LYS GLY LEU GLY ASN PRO LEU
SEQRES 12 M 352 LEU TYR ASP GLY VAL GLU ARG VAL SER LEU GLN ASP ILE
SEQRES 13 M 352 LYS ASP PHE ALA ASP LYS VAL TYR THR LYS GLU ASN LEU
SEQRES 14 M 352 GLU VAL SER GLY GLU ASN VAL VAL GLU ALA ASP LEU LYS
SEQRES 15 M 352 ARG PHE VAL ASP GLU SER LEU LEU SER THR LEU PRO ALA
SEQRES 16 M 352 GLY LYS SER LEU VAL SER LYS SER GLU PRO LYS PHE PHE
SEQRES 17 M 352 LEU GLY GLU GLU ASN ARG VAL ARG PHE ILE GLY ASP SER
SEQRES 18 M 352 VAL ALA ALA ILE GLY ILE PRO VAL ASN LYS ALA SER LEU
SEQRES 19 M 352 ALA GLN TYR GLU VAL LEU ALA ASN TYR LEU THR SER ALA
SEQRES 20 M 352 LEU SER GLU LEU SER GLY LEU ILE SER SER ALA LYS LEU
SEQRES 21 M 352 ASP LYS PHE THR ASP GLY GLY LEU PHE THR LEU PHE VAL
SEQRES 22 M 352 ARG ASP GLN ASP SER ALA VAL VAL SER SER ASN ILE LYS
SEQRES 23 M 352 LYS ILE VAL ALA ASP LEU LYS LYS GLY LYS ASP LEU SER
SEQRES 24 M 352 PRO ALA ILE ASN TYR THR LYS LEU LYS ASN ALA VAL GLN
SEQRES 25 M 352 ASN GLU SER VAL SER SER PRO ILE GLU LEU ASN PHE ASP
SEQRES 26 M 352 ALA VAL LYS ASP PHE LYS LEU GLY LYS PHE ASN TYR VAL
SEQRES 27 M 352 ALA VAL GLY ASP VAL SER ASN LEU PRO TYR LEU ASP GLU
SEQRES 28 M 352 LEU
SEQRES 1 N 385 MET ALA PHE ARG LYS SER ASN VAL TYR LEU SER LEU VAL
SEQRES 2 N 385 ASN SER TYR ILE ILE ASP SER PRO GLN PRO SER SER ILE
SEQRES 3 N 385 ASN TYR TRP TRP ASN MET GLY SER LEU LEU GLY LEU CYS
SEQRES 4 N 385 LEU VAL ILE GLN ILE VAL THR GLY ILE PHE MET ALA MET
SEQRES 5 N 385 HIS TYR SER SER ASN ILE GLU LEU ALA PHE SER SER VAL
SEQRES 6 N 385 GLU HIS ILE MET ARG ASP VAL HIS ASN GLY TYR ILE LEU
SEQRES 7 N 385 ARG TYR LEU HIS ALA ASN GLY ALA SER PHE PHE PHE MET
SEQRES 8 N 385 VAL MET PHE MET HIS MET ALA LYS GLY LEU TYR TYR GLY
SEQRES 9 N 385 SER TYR ARG SER PRO ARG VAL THR LEU TRP ASN VAL GLY
SEQRES 10 N 385 VAL ILE ILE PHE ILE LEU THR ILE ALA THR ALA PHE LEU
SEQRES 11 N 385 GLY TYR CYS CYS VAL TYR GLY GLN MET SER HIS TRP GLY
SEQRES 12 N 385 ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO PHE
SEQRES 13 N 385 VAL GLY ASN ASP ILE VAL SER TRP LEU TRP GLY GLY PHE
SEQRES 14 N 385 SER VAL SER ASN PRO THR ILE GLN ARG PHE PHE ALA LEU
SEQRES 15 N 385 HIS TYR LEU VAL PRO PHE ILE ILE ALA ALA MET VAL ILE
SEQRES 16 N 385 MET HIS LEU MET ALA LEU HIS ILE HIS GLY SER SER ASN
SEQRES 17 N 385 PRO LEU GLY ILE THR GLY ASN LEU ASP ARG ILE PRO MET
SEQRES 18 N 385 HIS SER TYR PHE ILE PHE LYS ASP LEU VAL THR VAL PHE
SEQRES 19 N 385 LEU PHE MET LEU ILE LEU ALA LEU PHE VAL PHE TYR SER
SEQRES 20 N 385 PRO ASN THR LEU GLY HIS PRO ASP ASN TYR ILE PRO GLY
SEQRES 21 N 385 ASN PRO LEU VAL THR PRO ALA SER ILE VAL PRO GLU TRP
SEQRES 22 N 385 TYR LEU LEU PRO PHE TYR ALA ILE LEU ARG SER ILE PRO
SEQRES 23 N 385 ASP LYS LEU LEU GLY VAL ILE THR MET PHE ALA ALA ILE
SEQRES 24 N 385 LEU VAL LEU LEU VAL LEU PRO PHE THR ASP ARG SER VAL
SEQRES 25 N 385 VAL ARG GLY ASN THR PHE LYS VAL LEU SER LYS PHE PHE
SEQRES 26 N 385 PHE PHE ILE PHE VAL PHE ASN PHE VAL LEU LEU GLY GLN
SEQRES 27 N 385 ILE GLY ALA CYS HIS VAL GLU VAL PRO TYR VAL LEU MET
SEQRES 28 N 385 GLY GLN ILE ALA THR PHE ILE TYR PHE ALA TYR PHE LEU
SEQRES 29 N 385 ILE ILE VAL PRO VAL ILE SER THR ILE GLU ASN VAL LEU
SEQRES 30 N 385 PHE TYR ILE GLY ARG VAL ASN LYS
SEQRES 1 O 248 MET THR ALA ALA GLU HIS GLY LEU HIS ALA PRO ALA TYR
SEQRES 2 O 248 ALA TRP SER HIS ASN GLY PRO PHE GLU THR PHE ASP HIS
SEQRES 3 O 248 ALA SER ILE ARG ARG GLY TYR GLN VAL TYR ARG GLU VAL
SEQRES 4 O 248 CYS ALA ALA CYS HIS SER LEU ASP ARG VAL ALA TRP ARG
SEQRES 5 O 248 THR LEU VAL GLY VAL SER HIS THR ASN GLU GLU VAL ARG
SEQRES 6 O 248 ASN MET ALA GLU GLU PHE GLU TYR ASP ASP GLU PRO ASP
SEQRES 7 O 248 GLU GLN GLY ASN PRO LYS LYS ARG PRO GLY LYS LEU SER
SEQRES 8 O 248 ASP TYR ILE PRO GLY PRO TYR PRO ASN GLU GLN ALA ALA
SEQRES 9 O 248 ARG ALA ALA ASN GLN GLY ALA LEU PRO PRO ASP LEU SER
SEQRES 10 O 248 LEU ILE VAL LYS ALA ARG HIS GLY GLY CYS ASP TYR ILE
SEQRES 11 O 248 PHE SER LEU LEU THR GLY TYR PRO ASP GLU PRO PRO ALA
SEQRES 12 O 248 GLY VAL ALA LEU PRO PRO GLY SER ASN TYR ASN PRO TYR
SEQRES 13 O 248 PHE PRO GLY GLY SER ILE ALA MET ALA ARG VAL LEU PHE
SEQRES 14 O 248 ASP ASP MET VAL GLU TYR GLU ASP GLY THR PRO ALA THR
SEQRES 15 O 248 THR SER GLN MET ALA LYS ASP VAL THR THR PHE LEU ASN
SEQRES 16 O 248 TRP CYS ALA GLU PRO GLU HIS ASP GLU ARG LYS ARG LEU
SEQRES 17 O 248 GLY LEU LYS THR VAL ILE ILE LEU SER SER LEU TYR LEU
SEQRES 18 O 248 LEU SER ILE TRP VAL LYS LYS PHE LYS TRP ALA GLY ILE
SEQRES 19 O 248 LYS THR ARG LYS PHE VAL PHE ASN PRO PRO LYS PRO ARG
SEQRES 20 O 248 LYS
SEQRES 1 P 185 LYS SER THR TYR ARG THR PRO ASN PHE ASP ASP VAL LEU
SEQRES 2 P 185 LYS GLU ASN ASN ASP ALA ASP LYS GLY ARG SER TYR ALA
SEQRES 3 P 185 TYR PHE MET VAL GLY ALA MET GLY LEU LEU SER SER ALA
SEQRES 4 P 185 GLY ALA LYS SER THR VAL GLU THR PHE ILE SER SER MET
SEQRES 5 P 185 THR ALA THR ALA ASP VAL LEU ALA MET ALA LYS VAL GLU
SEQRES 6 P 185 VAL ASN LEU ALA ALA ILE PRO LEU GLY LYS ASN VAL VAL
SEQRES 7 P 185 VAL LYS TRP GLN GLY LYS PRO VAL PHE ILE ARG HIS ARG
SEQRES 8 P 185 THR PRO HIS GLU ILE GLN GLU ALA ASN SER VAL ASP MET
SEQRES 9 P 185 SER ALA LEU LYS ASP PRO GLN THR ASP ALA ASP ARG VAL
SEQRES 10 P 185 LYS ASP PRO GLN TRP LEU ILE MET LEU GLY ILE CYS THR
SEQRES 11 P 185 HIS LEU GLY CYS VAL PRO ILE GLY GLU ALA GLY ASP PHE
SEQRES 12 P 185 GLY GLY TRP PHE CYS PRO CYS HIS GLY SER HIS TYR ASP
SEQRES 13 P 185 ILE SER GLY ARG ILE ARG LYS GLY PRO ALA PRO LEU ASN
SEQRES 14 P 185 LEU GLU ILE PRO ALA TYR GLU PHE ASP GLY ASP LYS VAL
SEQRES 15 P 185 ILE VAL GLY
SEQRES 1 Q 147 MET GLY MET LEU GLU LEU VAL GLY GLU TYR TRP GLU GLN
SEQRES 2 Q 147 LEU LYS ILE THR VAL VAL PRO VAL VAL ALA ALA ALA GLU
SEQRES 3 Q 147 ASP ASP ASP ASN GLU GLN HIS GLU GLU LYS ALA ALA GLU
SEQRES 4 Q 147 GLY GLU GLU LYS GLU GLU GLU ASN GLY ASP GLU ASP GLU
SEQRES 5 Q 147 ASP GLU ASP GLU ASP GLU ASP ASP ASP ASP ASP ASP ASP
SEQRES 6 Q 147 GLU ASP GLU GLU GLU GLU GLU GLU VAL THR ASP GLN LEU
SEQRES 7 Q 147 GLU ASP LEU ARG GLU HIS PHE LYS ASN THR GLU GLU GLY
SEQRES 8 Q 147 LYS ALA LEU VAL HIS HIS TYR GLU GLU CYS ALA GLU ARG
SEQRES 9 Q 147 VAL LYS ILE GLN GLN GLN GLN PRO GLY TYR ALA ASP LEU
SEQRES 10 Q 147 GLU HIS LYS GLU ASP CYS VAL GLU GLU PHE PHE HIS LEU
SEQRES 11 Q 147 GLN HIS TYR LEU ASP THR ALA THR ALA PRO ARG LEU PHE
SEQRES 12 Q 147 ASP LYS LEU LYS
SEQRES 1 R 127 MET PRO GLN SER PHE THR SER ILE ALA ARG ILE GLY ASP
SEQRES 2 R 127 TYR ILE LEU LYS SER PRO VAL LEU SER LYS LEU CYS VAL
SEQRES 3 R 127 PRO VAL ALA ASN GLN PHE ILE ASN LEU ALA GLY TYR LYS
SEQRES 4 R 127 LYS LEU GLY LEU LYS PHE ASP ASP LEU ILE ALA GLU GLU
SEQRES 5 R 127 ASN PRO ILE MET GLN THR ALA LEU ARG ARG LEU PRO GLU
SEQRES 6 R 127 ASP GLU SER TYR ALA ARG ALA TYR ARG ILE ILE ARG ALA
SEQRES 7 R 127 HIS GLN THR GLU LEU THR HIS HIS LEU LEU PRO ARG ASN
SEQRES 8 R 127 GLU TRP ILE LYS ALA GLN GLU ASP VAL PRO TYR LEU LEU
SEQRES 9 R 127 PRO TYR ILE LEU GLU ALA GLU ALA ALA ALA LYS GLU LYS
SEQRES 10 R 127 ASP GLU LEU ASP ASN ILE GLU VAL SER LYS
SEQRES 1 S 93 GLY PRO PRO SER GLY LYS THR TYR MET GLY TRP TRP GLY
SEQRES 2 S 93 HIS MET GLY GLY PRO LYS GLN LYS GLY ILE THR SER TYR
SEQRES 3 S 93 ALA VAL SER PRO TYR ALA GLN LYS PRO LEU GLN GLY ILE
SEQRES 4 S 93 PHE HIS ASN ALA VAL PHE ASN SER PHE ARG ARG PHE LYS
SEQRES 5 S 93 SER GLN PHE LEU TYR VAL LEU ILE PRO ALA GLY ILE TYR
SEQRES 6 S 93 TRP TYR TRP TRP LYS ASN GLY ASN GLU TYR ASN GLU PHE
SEQRES 7 S 93 LEU TYR SER LYS ALA GLY ARG GLU GLU LEU GLU ARG VAL
SEQRES 8 S 93 ASN VAL
SEQRES 1 T 66 MET SER PHE SER SER LEU TYR LYS THR PHE PHE LYS ARG
SEQRES 2 T 66 ASN ALA VAL PHE VAL GLY THR ILE PHE ALA GLY ALA PHE
SEQRES 3 T 66 VAL PHE GLN THR VAL PHE ASP THR ALA ILE THR SER TRP
SEQRES 4 T 66 TYR GLU ASN HIS ASN LYS GLY LYS LEU TRP LYS ASP VAL
SEQRES 5 T 66 LYS ALA ARG ILE ALA ALA GLY ASP GLY ASP ASP ASP ASP
SEQRES 6 T 66 GLU
SEQRES 1 U 77 MET ALA TYR THR SER HIS LEU SER SER LYS THR GLY LEU
SEQRES 2 U 77 HIS PHE GLY ARG LEU SER LEU ARG SER LEU THR ALA TYR
SEQRES 3 U 77 ALA PRO ASN LEU MET LEU TRP GLY GLY ALA SER MET LEU
SEQRES 4 U 77 GLY LEU PHE VAL PHE THR GLU GLY TRP PRO LYS PHE GLN
SEQRES 5 U 77 ASP THR LEU TYR LYS LYS ILE PRO LEU LEU GLY PRO THR
SEQRES 6 U 77 LEU GLU ASP HIS THR PRO PRO GLU ASP LYS PRO ASN
SEQRES 1 a 534 MET VAL GLN ARG TRP LEU TYR SER THR ASN ALA LYS ASP
SEQRES 2 a 534 ILE ALA VAL LEU TYR PHE MET LEU ALA ILE PHE SER GLY
SEQRES 3 a 534 MET ALA GLY THR ALA MET SER LEU ILE ILE ARG LEU GLU
SEQRES 4 a 534 LEU ALA ALA PRO GLY SER GLN TYR LEU HIS GLY ASN SER
SEQRES 5 a 534 GLN LEU PHE ASN VAL LEU VAL VAL GLY HIS ALA VAL LEU
SEQRES 6 a 534 MET ILE PHE PHE LEU VAL MET PRO ALA LEU ILE GLY GLY
SEQRES 7 a 534 PHE GLY ASN TYR LEU LEU PRO LEU MET ILE GLY ALA THR
SEQRES 8 a 534 ASP THR ALA PHE PRO ARG ILE ASN ASN ILE ALA PHE TRP
SEQRES 9 a 534 VAL LEU PRO MET GLY LEU VAL CYS LEU VAL THR SER THR
SEQRES 10 a 534 LEU VAL GLU SER GLY ALA GLY THR GLY TRP THR VAL TYR
SEQRES 11 a 534 PRO PRO LEU SER SER ILE GLN ALA HIS SER GLY PRO SER
SEQRES 12 a 534 VAL ASP LEU ALA ILE PHE ALA LEU HIS LEU THR SER ILE
SEQRES 13 a 534 SER SER LEU LEU GLY ALA ILE ASN PHE ILE VAL THR THR
SEQRES 14 a 534 LEU ASN MET ARG THR ASN GLY MET THR MET HIS LYS LEU
SEQRES 15 a 534 PRO LEU PHE VAL TRP SER ILE PHE ILE THR ALA PHE LEU
SEQRES 16 a 534 LEU LEU LEU SER LEU PRO VAL LEU SER ALA GLY ILE THR
SEQRES 17 a 534 MET LEU LEU LEU ASP ARG ASN PHE ASN THR SER PHE PHE
SEQRES 18 a 534 GLU VAL SER GLY GLY GLY ASP PRO ILE LEU TYR GLU HIS
SEQRES 19 a 534 LEU PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU
SEQRES 20 a 534 ILE ILE PRO GLY PHE GLY ILE ILE SER HIS VAL VAL SER
SEQRES 21 a 534 THR TYR SER LYS LYS PRO VAL PHE GLY GLU ILE SER MET
SEQRES 22 a 534 VAL TYR ALA MET ALA SER ILE GLY LEU LEU GLY PHE LEU
SEQRES 23 a 534 VAL TRP SER HIS HIS MET TYR ILE VAL GLY LEU ASP ALA
SEQRES 24 a 534 ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES 25 a 534 ALA ILE PRO THR GLY ILE LYS ILE PHE SER TRP LEU ALA
SEQRES 26 a 534 THR ILE HIS GLY GLY SER ILE ARG LEU ALA THR PRO MET
SEQRES 27 a 534 LEU TYR ALA ILE ALA PHE LEU PHE LEU PHE THR MET GLY
SEQRES 28 a 534 GLY LEU THR GLY VAL ALA LEU ALA ASN ALA SER LEU ASP
SEQRES 29 a 534 VAL ALA PHE HIS ASP THR TYR TYR VAL VAL GLY HIS PHE
SEQRES 30 a 534 HIS TYR VAL LEU SER MET GLY ALA ILE PHE SER LEU PHE
SEQRES 31 a 534 ALA GLY TYR TYR TYR TRP SER PRO GLN ILE LEU GLY LEU
SEQRES 32 a 534 ASN TYR ASN GLU LYS LEU ALA GLN ILE GLN PHE TRP LEU
SEQRES 33 a 534 ILE PHE ILE GLY ALA ASN VAL ILE PHE PHE PRO MET HIS
SEQRES 34 a 534 PHE LEU GLY ILE ASN GLY MET PRO ARG ARG ILE PRO ASP
SEQRES 35 a 534 TYR PRO ASP ALA PHE ALA GLY TRP ASN TYR VAL ALA SER
SEQRES 36 a 534 ILE GLY SER PHE ILE ALA THR LEU SER LEU PHE LEU PHE
SEQRES 37 a 534 ILE TYR ILE LEU TYR ASP GLN LEU VAL ASN GLY LEU ASN
SEQRES 38 a 534 ASN LYS VAL ASN ASN LYS SER VAL ILE TYR ASN LYS ALA
SEQRES 39 a 534 PRO ASP PHE VAL GLU SER ASN THR ILE PHE ASN LEU ASN
SEQRES 40 a 534 THR VAL LYS SER SER SER ILE GLU PHE LEU LEU THR SER
SEQRES 41 a 534 PRO PRO ALA VAL HIS SER PHE ASN THR PRO ALA VAL GLN
SEQRES 42 a 534 SER
SEQRES 1 b 236 ASP VAL PRO THR PRO TYR ALA CYS TYR PHE GLN ASP SER
SEQRES 2 b 236 ALA THR PRO ASN GLN GLU GLY ILE LEU GLU LEU HIS ASP
SEQRES 3 b 236 ASN ILE MET PHE TYR LEU LEU VAL ILE LEU GLY LEU VAL
SEQRES 4 b 236 SER TRP MET LEU TYR THR ILE VAL MET THR TYR SER LYS
SEQRES 5 b 236 ASN PRO ILE ALA TYR LYS TYR ILE LYS HIS GLY GLN THR
SEQRES 6 b 236 ILE GLU VAL ILE TRP THR ILE PHE PRO ALA VAL ILE LEU
SEQRES 7 b 236 LEU ILE ILE ALA PHE PRO SER PHE ILE LEU LEU TYR LEU
SEQRES 8 b 236 CYS ASP GLU VAL ILE SER PRO ALA MET THR ILE LYS ALA
SEQRES 9 b 236 ILE GLY TYR GLN TRP TYR TRP LYS TYR GLU TYR SER ASP
SEQRES 10 b 236 PHE ILE ASN ASP SER GLY GLU THR VAL GLU PHE GLU SER
SEQRES 11 b 236 TYR VAL ILE PRO ASP GLU LEU LEU GLU GLU GLY GLN LEU
SEQRES 12 b 236 ARG LEU LEU ASP THR ASP THR SER MET VAL VAL PRO VAL
SEQRES 13 b 236 ASP THR HIS ILE ARG PHE VAL VAL THR ALA ALA ASP VAL
SEQRES 14 b 236 ILE HIS ASP PHE ALA ILE PRO SER LEU GLY ILE LYS VAL
SEQRES 15 b 236 ASP ALA THR PRO GLY ARG LEU ASN GLN VAL SER ALA LEU
SEQRES 16 b 236 ILE GLN ARG GLU GLY VAL PHE TYR GLY ALA CYS SER GLU
SEQRES 17 b 236 LEU CYS GLY THR GLY HIS ALA ASN MET PRO ILE LYS ILE
SEQRES 18 b 236 GLU ALA VAL SER LEU PRO LYS PHE LEU GLU TRP LEU ASN
SEQRES 19 b 236 GLU GLN
SEQRES 1 c 269 MET THR HIS LEU GLU ARG SER ARG HIS GLN GLN HIS PRO
SEQRES 2 c 269 PHE HIS MET VAL MET PRO SER PRO TRP PRO ILE VAL VAL
SEQRES 3 c 269 SER PHE ALA LEU LEU SER LEU ALA LEU SER THR ALA LEU
SEQRES 4 c 269 THR MET HIS GLY TYR ILE GLY ASN MET ASN MET VAL TYR
SEQRES 5 c 269 LEU ALA LEU PHE VAL LEU LEU THR SER SER ILE LEU TRP
SEQRES 6 c 269 PHE ARG ASP ILE VAL ALA GLU ALA THR TYR LEU GLY ASP
SEQRES 7 c 269 HIS THR MET ALA VAL ARG LYS GLY ILE ASN LEU GLY PHE
SEQRES 8 c 269 LEU MET PHE VAL LEU SER GLU VAL LEU ILE PHE ALA GLY
SEQRES 9 c 269 LEU PHE TRP ALA TYR PHE HIS SER ALA MET SER PRO ASP
SEQRES 10 c 269 VAL THR LEU GLY ALA CYS TRP PRO PRO VAL GLY ILE GLU
SEQRES 11 c 269 ALA VAL GLN PRO THR GLU LEU PRO LEU LEU ASN THR ILE
SEQRES 12 c 269 ILE LEU LEU SER SER GLY ALA THR VAL THR TYR SER HIS
SEQRES 13 c 269 HIS ALA LEU ILE ALA GLY ASN ARG ASN LYS ALA LEU SER
SEQRES 14 c 269 GLY LEU LEU ILE THR PHE TRP LEU ILE VAL ILE PHE VAL
SEQRES 15 c 269 THR CYS GLN TYR ILE GLU TYR THR ASN ALA ALA PHE THR
SEQRES 16 c 269 ILE SER ASP GLY VAL TYR GLY SER VAL PHE TYR ALA GLY
SEQRES 17 c 269 THR GLY LEU HIS PHE LEU HIS MET VAL MET LEU ALA ALA
SEQRES 18 c 269 MET LEU GLY VAL ASN TYR TRP ARG MET ARG ASN TYR HIS
SEQRES 19 c 269 LEU THR ALA GLY HIS HIS VAL GLY TYR GLU THR THR ILE
SEQRES 20 c 269 ILE TYR THR HIS VAL LEU ASP VAL ILE TRP LEU PHE LEU
SEQRES 21 c 269 TYR VAL VAL PHE TYR TRP TRP GLY VAL
SEQRES 1 d 130 GLN GLN LYS PRO VAL VAL LYS THR ALA GLN ASN LEU ALA
SEQRES 2 d 130 GLU VAL ASN GLY PRO GLU THR LEU ILE GLY PRO GLY ALA
SEQRES 3 d 130 LYS GLU GLY THR VAL PRO THR ASP LEU ASP GLN GLU THR
SEQRES 4 d 130 GLY LEU ALA ARG LEU GLU LEU LEU GLY LYS LEU GLU GLY
SEQRES 5 d 130 ILE ASP VAL PHE ASP THR LYS PRO LEU ASP SER SER ARG
SEQRES 6 d 130 LYS GLY THR MET LYS ASP PRO ILE ILE ILE GLU SER TYR
SEQRES 7 d 130 ASP ASP TYR ARG TYR VAL GLY CYS THR GLY SER PRO ALA
SEQRES 8 d 130 GLY SER HIS THR ILE MET TRP LEU LYS PRO THR VAL ASN
SEQRES 9 d 130 GLU VAL ALA ARG CYS TRP GLU CYS GLY SER VAL TYR LYS
SEQRES 10 d 130 LEU ASN PRO VAL GLY VAL PRO ASN ASP ASP HIS HIS HIS
SEQRES 1 e 133 ALA GLN THR HIS ALA LEU SER ASN ALA ALA VAL MET ASP
SEQRES 2 e 133 LEU GLN SER ARG TRP GLU ASN MET PRO SER THR GLU GLN
SEQRES 3 e 133 GLN ASP ILE VAL SER LYS LEU SER GLU ARG GLN LYS LEU
SEQRES 4 e 133 PRO TRP ALA GLN LEU THR GLU PRO GLU LYS GLN ALA VAL
SEQRES 5 e 133 TRP TYR ILE SER TYR GLY GLU TRP GLY PRO ARG ARG PRO
SEQRES 6 e 133 VAL LEU ASN LYS GLY ASP SER SER PHE ILE ALA LYS GLY
SEQRES 7 e 133 VAL ALA ALA GLY LEU LEU PHE SER VAL GLY LEU PHE ALA
SEQRES 8 e 133 VAL VAL ARG MET ALA GLY GLY GLN ASP ALA LYS THR MET
SEQRES 9 e 133 ASN LYS GLU TRP GLN LEU LYS SER ASP GLU TYR LEU LYS
SEQRES 10 e 133 SER LYS ASN ALA ASN PRO TRP GLY GLY TYR SER GLN VAL
SEQRES 11 e 133 GLN SER LYS
SEQRES 1 f 108 SER ASP ALA HIS ASP GLU GLU THR PHE GLU GLU PHE THR
SEQRES 2 f 108 ALA ARG TYR GLU LYS GLU PHE ASP GLU ALA TYR ASP LEU
SEQRES 3 f 108 PHE GLU VAL GLN ARG VAL LEU ASN ASN CYS PHE SER TYR
SEQRES 4 f 108 ASP LEU VAL PRO ALA PRO ALA VAL ILE GLU LYS ALA LEU
SEQRES 5 f 108 ARG ALA ALA ARG ARG VAL ASN ASP LEU PRO THR ALA ILE
SEQRES 6 f 108 ARG VAL PHE GLU ALA LEU LYS TYR LYS VAL GLU ASN GLU
SEQRES 7 f 108 ASP GLN TYR LYS ALA TYR LEU ASP GLU LEU LYS ASP VAL
SEQRES 8 f 108 ARG GLN GLU LEU GLY VAL PRO LEU LYS GLU GLU LEU PHE
SEQRES 9 f 108 PRO SER SER SER
SEQRES 1 g 59 ALA ASN LYS VAL ILE GLN LEU GLN LYS ILE PHE GLN SER
SEQRES 2 g 59 SER THR LYS PRO LEU TRP TRP ARG HIS PRO ARG SER ALA
SEQRES 3 g 59 LEU TYR LEU TYR PRO PHE TYR ALA ILE PHE ALA VAL ALA
SEQRES 4 g 59 VAL VAL THR PRO LEU LEU TYR ILE PRO ASN ALA ILE ARG
SEQRES 5 g 59 GLY ILE LYS ALA LYS LYS ALA
SEQRES 1 h 47 VAL HIS PHE LYS ASP GLY VAL TYR GLU ASN ILE PRO PHE
SEQRES 2 h 47 LYS VAL LYS GLY ARG LYS THR PRO TYR ALA LEU SER HIS
SEQRES 3 h 47 PHE GLY PHE PHE ALA ILE GLY PHE ALA VAL PRO PHE VAL
SEQRES 4 h 47 ALA CYS TYR VAL GLN LEU LYS LYS
SEQRES 1 i 55 THR ILE ALA PRO ILE THR GLY THR ILE LYS ARG ARG VAL
SEQRES 2 i 55 ILE MET ASP ILE VAL LEU GLY PHE SER LEU GLY GLY VAL
SEQRES 3 i 55 MET ALA SER TYR TRP TRP TRP GLY PHE HIS MET ASP LYS
SEQRES 4 i 55 ILE ASN LYS ARG GLU LYS PHE TYR ALA GLU LEU ALA GLU
SEQRES 5 i 55 ARG LYS LYS
SEQRES 1 j 82 ALA ASP GLN GLU ASN SER PRO LEU HIS THR VAL GLY PHE
SEQRES 2 j 82 ASP ALA ARG PHE PRO GLN GLN ASN GLN THR LYS HIS CYS
SEQRES 3 j 82 TRP GLN SER TYR VAL ASP TYR HIS LYS CYS VAL ASN MET
SEQRES 4 j 82 LYS GLY GLU ASP PHE ALA PRO CYS LYS VAL PHE TRP LYS
SEQRES 5 j 82 THR TYR ASN ALA LEU CYS PRO LEU ASP TRP ILE GLU LYS
SEQRES 6 j 82 TRP ASP ASP GLN ARG GLU LYS GLY ILE PHE ALA GLY ASP
SEQRES 7 j 82 ILE ASN SER ASP
SEQRES 1 k 131 ALA SER SER LEU PRO PRO ASN ALA LEU LYS PRO ALA PHE
SEQRES 2 k 131 GLY PRO PRO ASP LYS VAL ALA ALA GLN LYS PHE LYS GLU
SEQRES 3 k 131 SER LEU MET ALA THR GLU LYS HIS ALA LYS ASP THR SER
SEQRES 4 k 131 ASN MET TRP VAL LYS ILE SER VAL TRP VAL ALA LEU PRO
SEQRES 5 k 131 ALA ILE ALA LEU THR ALA VAL ASN THR TYR PHE VAL GLU
SEQRES 6 k 131 LYS GLU HIS ALA GLU HIS ARG GLU HIS LEU LYS HIS VAL
SEQRES 7 k 131 PRO ASP SER GLU TRP PRO ARG ASP TYR GLU PHE MET ASN
SEQRES 8 k 131 ILE ARG SER LYS PRO PHE PHE TRP GLY ASP GLY ASP LYS
SEQRES 9 k 131 THR LEU PHE TRP ASN PRO VAL VAL ASN ARG HIS ILE GLU
SEQRES 10 k 131 HIS ASP ASP GLY ALA ARG GLY SER HIS HIS HIS HIS HIS
SEQRES 11 k 131 HIS
SEQRES 1 l 66 MET PHE PHE SER GLN VAL LEU ARG SER SER ALA ARG ALA
SEQRES 2 l 66 ALA PRO ILE LYS ARG TYR THR GLY GLY ARG ILE GLY GLU
SEQRES 3 l 66 SER TRP VAL ILE THR GLU GLY ARG ARG LEU ILE PRO GLU
SEQRES 4 l 66 ILE PHE GLN TRP SER ALA VAL LEU SER VAL CYS LEU GLY
SEQRES 5 l 66 TRP PRO GLY ALA VAL TYR PHE PHE SER LYS ALA ARG LYS
SEQRES 6 l 66 ALA
SEQRES 1 m 534 MET VAL GLN ARG TRP LEU TYR SER THR ASN ALA LYS ASP
SEQRES 2 m 534 ILE ALA VAL LEU TYR PHE MET LEU ALA ILE PHE SER GLY
SEQRES 3 m 534 MET ALA GLY THR ALA MET SER LEU ILE ILE ARG LEU GLU
SEQRES 4 m 534 LEU ALA ALA PRO GLY SER GLN TYR LEU HIS GLY ASN SER
SEQRES 5 m 534 GLN LEU PHE ASN VAL LEU VAL VAL GLY HIS ALA VAL LEU
SEQRES 6 m 534 MET ILE PHE PHE LEU VAL MET PRO ALA LEU ILE GLY GLY
SEQRES 7 m 534 PHE GLY ASN TYR LEU LEU PRO LEU MET ILE GLY ALA THR
SEQRES 8 m 534 ASP THR ALA PHE PRO ARG ILE ASN ASN ILE ALA PHE TRP
SEQRES 9 m 534 VAL LEU PRO MET GLY LEU VAL CYS LEU VAL THR SER THR
SEQRES 10 m 534 LEU VAL GLU SER GLY ALA GLY THR GLY TRP THR VAL TYR
SEQRES 11 m 534 PRO PRO LEU SER SER ILE GLN ALA HIS SER GLY PRO SER
SEQRES 12 m 534 VAL ASP LEU ALA ILE PHE ALA LEU HIS LEU THR SER ILE
SEQRES 13 m 534 SER SER LEU LEU GLY ALA ILE ASN PHE ILE VAL THR THR
SEQRES 14 m 534 LEU ASN MET ARG THR ASN GLY MET THR MET HIS LYS LEU
SEQRES 15 m 534 PRO LEU PHE VAL TRP SER ILE PHE ILE THR ALA PHE LEU
SEQRES 16 m 534 LEU LEU LEU SER LEU PRO VAL LEU SER ALA GLY ILE THR
SEQRES 17 m 534 MET LEU LEU LEU ASP ARG ASN PHE ASN THR SER PHE PHE
SEQRES 18 m 534 GLU VAL SER GLY GLY GLY ASP PRO ILE LEU TYR GLU HIS
SEQRES 19 m 534 LEU PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU
SEQRES 20 m 534 ILE ILE PRO GLY PHE GLY ILE ILE SER HIS VAL VAL SER
SEQRES 21 m 534 THR TYR SER LYS LYS PRO VAL PHE GLY GLU ILE SER MET
SEQRES 22 m 534 VAL TYR ALA MET ALA SER ILE GLY LEU LEU GLY PHE LEU
SEQRES 23 m 534 VAL TRP SER HIS HIS MET TYR ILE VAL GLY LEU ASP ALA
SEQRES 24 m 534 ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES 25 m 534 ALA ILE PRO THR GLY ILE LYS ILE PHE SER TRP LEU ALA
SEQRES 26 m 534 THR ILE HIS GLY GLY SER ILE ARG LEU ALA THR PRO MET
SEQRES 27 m 534 LEU TYR ALA ILE ALA PHE LEU PHE LEU PHE THR MET GLY
SEQRES 28 m 534 GLY LEU THR GLY VAL ALA LEU ALA ASN ALA SER LEU ASP
SEQRES 29 m 534 VAL ALA PHE HIS ASP THR TYR TYR VAL VAL GLY HIS PHE
SEQRES 30 m 534 HIS TYR VAL LEU SER MET GLY ALA ILE PHE SER LEU PHE
SEQRES 31 m 534 ALA GLY TYR TYR TYR TRP SER PRO GLN ILE LEU GLY LEU
SEQRES 32 m 534 ASN TYR ASN GLU LYS LEU ALA GLN ILE GLN PHE TRP LEU
SEQRES 33 m 534 ILE PHE ILE GLY ALA ASN VAL ILE PHE PHE PRO MET HIS
SEQRES 34 m 534 PHE LEU GLY ILE ASN GLY MET PRO ARG ARG ILE PRO ASP
SEQRES 35 m 534 TYR PRO ASP ALA PHE ALA GLY TRP ASN TYR VAL ALA SER
SEQRES 36 m 534 ILE GLY SER PHE ILE ALA THR LEU SER LEU PHE LEU PHE
SEQRES 37 m 534 ILE TYR ILE LEU TYR ASP GLN LEU VAL ASN GLY LEU ASN
SEQRES 38 m 534 ASN LYS VAL ASN ASN LYS SER VAL ILE TYR ASN LYS ALA
SEQRES 39 m 534 PRO ASP PHE VAL GLU SER ASN THR ILE PHE ASN LEU ASN
SEQRES 40 m 534 THR VAL LYS SER SER SER ILE GLU PHE LEU LEU THR SER
SEQRES 41 m 534 PRO PRO ALA VAL HIS SER PHE ASN THR PRO ALA VAL GLN
SEQRES 42 m 534 SER
SEQRES 1 n 236 ASP VAL PRO THR PRO TYR ALA CYS TYR PHE GLN ASP SER
SEQRES 2 n 236 ALA THR PRO ASN GLN GLU GLY ILE LEU GLU LEU HIS ASP
SEQRES 3 n 236 ASN ILE MET PHE TYR LEU LEU VAL ILE LEU GLY LEU VAL
SEQRES 4 n 236 SER TRP MET LEU TYR THR ILE VAL MET THR TYR SER LYS
SEQRES 5 n 236 ASN PRO ILE ALA TYR LYS TYR ILE LYS HIS GLY GLN THR
SEQRES 6 n 236 ILE GLU VAL ILE TRP THR ILE PHE PRO ALA VAL ILE LEU
SEQRES 7 n 236 LEU ILE ILE ALA PHE PRO SER PHE ILE LEU LEU TYR LEU
SEQRES 8 n 236 CYS ASP GLU VAL ILE SER PRO ALA MET THR ILE LYS ALA
SEQRES 9 n 236 ILE GLY TYR GLN TRP TYR TRP LYS TYR GLU TYR SER ASP
SEQRES 10 n 236 PHE ILE ASN ASP SER GLY GLU THR VAL GLU PHE GLU SER
SEQRES 11 n 236 TYR VAL ILE PRO ASP GLU LEU LEU GLU GLU GLY GLN LEU
SEQRES 12 n 236 ARG LEU LEU ASP THR ASP THR SER MET VAL VAL PRO VAL
SEQRES 13 n 236 ASP THR HIS ILE ARG PHE VAL VAL THR ALA ALA ASP VAL
SEQRES 14 n 236 ILE HIS ASP PHE ALA ILE PRO SER LEU GLY ILE LYS VAL
SEQRES 15 n 236 ASP ALA THR PRO GLY ARG LEU ASN GLN VAL SER ALA LEU
SEQRES 16 n 236 ILE GLN ARG GLU GLY VAL PHE TYR GLY ALA CYS SER GLU
SEQRES 17 n 236 LEU CYS GLY THR GLY HIS ALA ASN MET PRO ILE LYS ILE
SEQRES 18 n 236 GLU ALA VAL SER LEU PRO LYS PHE LEU GLU TRP LEU ASN
SEQRES 19 n 236 GLU GLN
SEQRES 1 o 269 MET THR HIS LEU GLU ARG SER ARG HIS GLN GLN HIS PRO
SEQRES 2 o 269 PHE HIS MET VAL MET PRO SER PRO TRP PRO ILE VAL VAL
SEQRES 3 o 269 SER PHE ALA LEU LEU SER LEU ALA LEU SER THR ALA LEU
SEQRES 4 o 269 THR MET HIS GLY TYR ILE GLY ASN MET ASN MET VAL TYR
SEQRES 5 o 269 LEU ALA LEU PHE VAL LEU LEU THR SER SER ILE LEU TRP
SEQRES 6 o 269 PHE ARG ASP ILE VAL ALA GLU ALA THR TYR LEU GLY ASP
SEQRES 7 o 269 HIS THR MET ALA VAL ARG LYS GLY ILE ASN LEU GLY PHE
SEQRES 8 o 269 LEU MET PHE VAL LEU SER GLU VAL LEU ILE PHE ALA GLY
SEQRES 9 o 269 LEU PHE TRP ALA TYR PHE HIS SER ALA MET SER PRO ASP
SEQRES 10 o 269 VAL THR LEU GLY ALA CYS TRP PRO PRO VAL GLY ILE GLU
SEQRES 11 o 269 ALA VAL GLN PRO THR GLU LEU PRO LEU LEU ASN THR ILE
SEQRES 12 o 269 ILE LEU LEU SER SER GLY ALA THR VAL THR TYR SER HIS
SEQRES 13 o 269 HIS ALA LEU ILE ALA GLY ASN ARG ASN LYS ALA LEU SER
SEQRES 14 o 269 GLY LEU LEU ILE THR PHE TRP LEU ILE VAL ILE PHE VAL
SEQRES 15 o 269 THR CYS GLN TYR ILE GLU TYR THR ASN ALA ALA PHE THR
SEQRES 16 o 269 ILE SER ASP GLY VAL TYR GLY SER VAL PHE TYR ALA GLY
SEQRES 17 o 269 THR GLY LEU HIS PHE LEU HIS MET VAL MET LEU ALA ALA
SEQRES 18 o 269 MET LEU GLY VAL ASN TYR TRP ARG MET ARG ASN TYR HIS
SEQRES 19 o 269 LEU THR ALA GLY HIS HIS VAL GLY TYR GLU THR THR ILE
SEQRES 20 o 269 ILE TYR THR HIS VAL LEU ASP VAL ILE TRP LEU PHE LEU
SEQRES 21 o 269 TYR VAL VAL PHE TYR TRP TRP GLY VAL
SEQRES 1 p 130 GLN GLN LYS PRO VAL VAL LYS THR ALA GLN ASN LEU ALA
SEQRES 2 p 130 GLU VAL ASN GLY PRO GLU THR LEU ILE GLY PRO GLY ALA
SEQRES 3 p 130 LYS GLU GLY THR VAL PRO THR ASP LEU ASP GLN GLU THR
SEQRES 4 p 130 GLY LEU ALA ARG LEU GLU LEU LEU GLY LYS LEU GLU GLY
SEQRES 5 p 130 ILE ASP VAL PHE ASP THR LYS PRO LEU ASP SER SER ARG
SEQRES 6 p 130 LYS GLY THR MET LYS ASP PRO ILE ILE ILE GLU SER TYR
SEQRES 7 p 130 ASP ASP TYR ARG TYR VAL GLY CYS THR GLY SER PRO ALA
SEQRES 8 p 130 GLY SER HIS THR ILE MET TRP LEU LYS PRO THR VAL ASN
SEQRES 9 p 130 GLU VAL ALA ARG CYS TRP GLU CYS GLY SER VAL TYR LYS
SEQRES 10 p 130 LEU ASN PRO VAL GLY VAL PRO ASN ASP ASP HIS HIS HIS
SEQRES 1 q 133 ALA GLN THR HIS ALA LEU SER ASN ALA ALA VAL MET ASP
SEQRES 2 q 133 LEU GLN SER ARG TRP GLU ASN MET PRO SER THR GLU GLN
SEQRES 3 q 133 GLN ASP ILE VAL SER LYS LEU SER GLU ARG GLN LYS LEU
SEQRES 4 q 133 PRO TRP ALA GLN LEU THR GLU PRO GLU LYS GLN ALA VAL
SEQRES 5 q 133 TRP TYR ILE SER TYR GLY GLU TRP GLY PRO ARG ARG PRO
SEQRES 6 q 133 VAL LEU ASN LYS GLY ASP SER SER PHE ILE ALA LYS GLY
SEQRES 7 q 133 VAL ALA ALA GLY LEU LEU PHE SER VAL GLY LEU PHE ALA
SEQRES 8 q 133 VAL VAL ARG MET ALA GLY GLY GLN ASP ALA LYS THR MET
SEQRES 9 q 133 ASN LYS GLU TRP GLN LEU LYS SER ASP GLU TYR LEU LYS
SEQRES 10 q 133 SER LYS ASN ALA ASN PRO TRP GLY GLY TYR SER GLN VAL
SEQRES 11 q 133 GLN SER LYS
SEQRES 1 r 108 SER ASP ALA HIS ASP GLU GLU THR PHE GLU GLU PHE THR
SEQRES 2 r 108 ALA ARG TYR GLU LYS GLU PHE ASP GLU ALA TYR ASP LEU
SEQRES 3 r 108 PHE GLU VAL GLN ARG VAL LEU ASN ASN CYS PHE SER TYR
SEQRES 4 r 108 ASP LEU VAL PRO ALA PRO ALA VAL ILE GLU LYS ALA LEU
SEQRES 5 r 108 ARG ALA ALA ARG ARG VAL ASN ASP LEU PRO THR ALA ILE
SEQRES 6 r 108 ARG VAL PHE GLU ALA LEU LYS TYR LYS VAL GLU ASN GLU
SEQRES 7 r 108 ASP GLN TYR LYS ALA TYR LEU ASP GLU LEU LYS ASP VAL
SEQRES 8 r 108 ARG GLN GLU LEU GLY VAL PRO LEU LYS GLU GLU LEU PHE
SEQRES 9 r 108 PRO SER SER SER
SEQRES 1 s 59 ALA ASN LYS VAL ILE GLN LEU GLN LYS ILE PHE GLN SER
SEQRES 2 s 59 SER THR LYS PRO LEU TRP TRP ARG HIS PRO ARG SER ALA
SEQRES 3 s 59 LEU TYR LEU TYR PRO PHE TYR ALA ILE PHE ALA VAL ALA
SEQRES 4 s 59 VAL VAL THR PRO LEU LEU TYR ILE PRO ASN ALA ILE ARG
SEQRES 5 s 59 GLY ILE LYS ALA LYS LYS ALA
SEQRES 1 t 47 VAL HIS PHE LYS ASP GLY VAL TYR GLU ASN ILE PRO PHE
SEQRES 2 t 47 LYS VAL LYS GLY ARG LYS THR PRO TYR ALA LEU SER HIS
SEQRES 3 t 47 PHE GLY PHE PHE ALA ILE GLY PHE ALA VAL PRO PHE VAL
SEQRES 4 t 47 ALA CYS TYR VAL GLN LEU LYS LYS
SEQRES 1 u 55 THR ILE ALA PRO ILE THR GLY THR ILE LYS ARG ARG VAL
SEQRES 2 u 55 ILE MET ASP ILE VAL LEU GLY PHE SER LEU GLY GLY VAL
SEQRES 3 u 55 MET ALA SER TYR TRP TRP TRP GLY PHE HIS MET ASP LYS
SEQRES 4 u 55 ILE ASN LYS ARG GLU LYS PHE TYR ALA GLU LEU ALA GLU
SEQRES 5 u 55 ARG LYS LYS
SEQRES 1 v 82 ALA ASP GLN GLU ASN SER PRO LEU HIS THR VAL GLY PHE
SEQRES 2 v 82 ASP ALA ARG PHE PRO GLN GLN ASN GLN THR LYS HIS CYS
SEQRES 3 v 82 TRP GLN SER TYR VAL ASP TYR HIS LYS CYS VAL ASN MET
SEQRES 4 v 82 LYS GLY GLU ASP PHE ALA PRO CYS LYS VAL PHE TRP LYS
SEQRES 5 v 82 THR TYR ASN ALA LEU CYS PRO LEU ASP TRP ILE GLU LYS
SEQRES 6 v 82 TRP ASP ASP GLN ARG GLU LYS GLY ILE PHE ALA GLY ASP
SEQRES 7 v 82 ILE ASN SER ASP
SEQRES 1 w 131 ALA SER SER LEU PRO PRO ASN ALA LEU LYS PRO ALA PHE
SEQRES 2 w 131 GLY PRO PRO ASP LYS VAL ALA ALA GLN LYS PHE LYS GLU
SEQRES 3 w 131 SER LEU MET ALA THR GLU LYS HIS ALA LYS ASP THR SER
SEQRES 4 w 131 ASN MET TRP VAL LYS ILE SER VAL TRP VAL ALA LEU PRO
SEQRES 5 w 131 ALA ILE ALA LEU THR ALA VAL ASN THR TYR PHE VAL GLU
SEQRES 6 w 131 LYS GLU HIS ALA GLU HIS ARG GLU HIS LEU LYS HIS VAL
SEQRES 7 w 131 PRO ASP SER GLU TRP PRO ARG ASP TYR GLU PHE MET ASN
SEQRES 8 w 131 ILE ARG SER LYS PRO PHE PHE TRP GLY ASP GLY ASP LYS
SEQRES 9 w 131 THR LEU PHE TRP ASN PRO VAL VAL ASN ARG HIS ILE GLU
SEQRES 10 w 131 HIS ASP ASP GLY ALA ARG GLY SER HIS HIS HIS HIS HIS
SEQRES 11 w 131 HIS
SEQRES 1 x 66 MET PHE PHE SER GLN VAL LEU ARG SER SER ALA ARG ALA
SEQRES 2 x 66 ALA PRO ILE LYS ARG TYR THR GLY GLY ARG ILE GLY GLU
SEQRES 3 x 66 SER TRP VAL ILE THR GLU GLY ARG ARG LEU ILE PRO GLU
SEQRES 4 x 66 ILE PHE GLN TRP SER ALA VAL LEU SER VAL CYS LEU GLY
SEQRES 5 x 66 TRP PRO GLY ALA VAL TYR PHE PHE SER LYS ALA ARG LYS
SEQRES 6 x 66 ALA
HET PEF A 501 44
HET HEM C 601 43
HET HEM C 602 43
HET UQ6 C 603 86
HET CDL C 604 58
HET PEF C 605 39
HET PEF C 606 36
HET PCF C 607 39
HET HEC D 401 43
HET PEF D 402 42
HET FES E 301 4
HET CDL E 302 53
HET PEF E 303 29
HET CDL H 601 66
HET CDL H 602 71
HET PEF H 603 32
HET PCF H 604 32
HET PCF I 101 30
HET CDL L 501 55
HET HEM N 601 43
HET HEM N 602 43
HET PEF N 603 40
HET PEF N 604 43
HET PEF N 605 31
HET PCF N 606 50
HET HEC O 401 43
HET CDL O 402 67
HET PEF O 403 43
HET FES P 301 4
HET CDL P 302 48
HET PEF P 303 29
HET CDL S 601 53
HET PEF S 602 36
HET PCF S 603 32
HET PCF T 101 39
HET CU a 601 1
HET HEA a 602 60
HET HEA a 603 60
HET CA a 604 1
HET MG a 605 1
HET PEF a 606 47
HET PEF a 607 33
HET PEF a 608 33
HET CUA b 301 1
HET CUA b 302 1
HET PEF b 303 40
HET PEF c 301 36
HET PEF c 302 41
HET ZN d 201 1
HET PEF e 201 47
HET PCF e 202 36
HET PEF h 101 47
HET CU m 601 1
HET HEA m 602 60
HET HEA m 603 60
HET CA m 604 1
HET MG m 605 1
HET PEF m 606 47
HET PEF m 607 33
HET CUA n 301 1
HET CUA n 302 1
HET PEF n 303 40
HET PEF n 304 33
HET PEF o 301 36
HET PEF o 302 41
HET ZN p 201 1
HET PEF q 201 47
HET PCF q 202 36
HET PEF t 101 47
HETNAM PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,
HETNAM 2 UQ6 22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL
HETNAM CDL CARDIOLIPIN
HETNAM PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE
HETNAM HEC HEME C
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM CU COPPER (II) ION
HETNAM HEA HEME-A
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM CUA DINUCLEAR COPPER ION
HETNAM ZN ZINC ION
HETSYN PEF 3-[AMINOETHYLPHOSPHORYL]-[1,2-DI-PALMITOYL]-SN-GLYCEROL
HETSYN HEM HEME
HETSYN CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-
HETSYN 2 CDL PHOSPHO)-1',3'-SN-GLYCEROL
FORMUL 45 PEF 28(C37 H74 N O8 P)
FORMUL 46 HEM 4(C34 H32 FE N4 O4)
FORMUL 48 UQ6 C39 H60 O4
FORMUL 49 CDL 8(C81 H156 O17 P2 2-)
FORMUL 52 PCF 8(C40 H80 N O8 P)
FORMUL 53 HEC 2(C34 H34 FE N4 O4)
FORMUL 55 FES 2(FE2 S2)
FORMUL 80 CU 2(CU 2+)
FORMUL 81 HEA 4(C49 H56 FE N4 O6)
FORMUL 83 CA 2(CA 2+)
FORMUL 84 MG 2(MG 2+)
FORMUL 88 CUA 4(CU2)
FORMUL 93 ZN 2(ZN 2+)
HELIX 1 AA1 GLY A 58 GLU A 62 5 5
HELIX 2 AA2 GLY A 68 LEU A 78 1 11
HELIX 3 AA3 SER A 79 GLU A 89 1 11
HELIX 4 AA4 SER A 112 SER A 123 1 12
HELIX 5 AA5 ASN A 136 ASP A 155 1 20
HELIX 6 AA6 ASP A 155 PHE A 169 1 15
HELIX 7 AA7 THR A 172 LEU A 176 5 5
HELIX 8 AA8 VAL A 189 PHE A 201 1 13
HELIX 9 AA9 LYS A 215 LYS A 226 1 12
HELIX 10 AB1 ASN A 274 GLY A 286 1 13
HELIX 11 AB2 LEU A 302 GLN A 307 1 6
HELIX 12 AB3 MET A 339 SER A 357 1 19
HELIX 13 AB4 THR A 359 GLU A 379 1 21
HELIX 14 AB5 ASN A 382 LYS A 397 1 16
HELIX 15 AB6 SER A 402 ALA A 412 1 11
HELIX 16 AB7 THR A 414 LEU A 426 1 13
HELIX 17 AB8 ASP A 444 SER A 450 1 7
HELIX 18 AB9 GLY B 38 ALA B 42 5 5
HELIX 19 AC1 GLY B 46 PHE B 54 1 9
HELIX 20 AC2 SER B 63 GLY B 75 1 13
HELIX 21 AC3 ASP B 97 LYS B 111 1 15
HELIX 22 AC4 LYS B 115 SER B 122 1 8
HELIX 23 AC5 SER B 122 GLN B 136 1 15
HELIX 24 AC6 CYS B 137 PHE B 151 1 15
HELIX 25 AC7 SER B 168 TYR B 180 1 13
HELIX 26 AC8 VAL B 193 ASP B 202 1 10
HELIX 27 AC9 SER B 249 SER B 262 1 14
HELIX 28 AD1 ASP B 293 LYS B 310 1 18
HELIX 29 AD2 ALA B 317 VAL B 332 1 16
HELIX 30 AD3 ALA C 2 ASN C 7 1 6
HELIX 31 AD4 VAL C 8 ILE C 17 1 10
HELIX 32 AD5 ASN C 27 TRP C 30 5 4
HELIX 33 AD6 ASN C 31 MET C 52 1 22
HELIX 34 AD7 LEU C 60 ASP C 71 1 12
HELIX 35 AD8 ASN C 74 TYR C 103 1 30
HELIX 36 AD9 ARG C 110 VAL C 135 1 26
HELIX 37 AE1 GLY C 137 LEU C 150 1 14
HELIX 38 AE2 PHE C 151 ILE C 154 5 4
HELIX 39 AE3 VAL C 157 GLY C 167 1 11
HELIX 40 AE4 SER C 172 ILE C 203 1 32
HELIX 41 AE5 TYR C 224 TYR C 246 1 23
HELIX 42 AE6 HIS C 253 ILE C 258 5 6
HELIX 43 AE7 GLU C 272 TYR C 274 5 3
HELIX 44 AE8 LEU C 275 ILE C 285 1 11
HELIX 45 AE9 ASP C 287 VAL C 301 1 15
HELIX 46 AF1 VAL C 304 ASP C 309 1 6
HELIX 47 AF2 GLY C 315 PHE C 318 5 4
HELIX 48 AF3 LYS C 319 ALA C 341 1 23
HELIX 49 AF4 GLU C 345 ILE C 365 1 21
HELIX 50 AF5 ILE C 365 GLY C 381 1 17
HELIX 51 AF6 THR D 63 GLY D 68 1 6
HELIX 52 AF7 ASP D 86 VAL D 100 1 15
HELIX 53 AF8 CYS D 101 CYS D 104 5 4
HELIX 54 AF9 TRP D 112 VAL D 116 5 5
HELIX 55 AG1 THR D 121 PHE D 132 1 12
HELIX 56 AG2 ASN D 161 ASN D 169 1 9
HELIX 57 AG3 LEU D 179 ARG D 184 1 6
HELIX 58 AG4 GLY D 187 GLY D 197 1 11
HELIX 59 AG5 THR D 243 GLU D 260 1 18
HELIX 60 AG6 GLU D 262 THR D 297 1 36
HELIX 61 AG7 ASP E 48 ALA E 84 1 37
HELIX 62 AG8 THR E 85 ALA E 90 1 6
HELIX 63 AG9 THR E 122 ASN E 130 1 9
HELIX 64 AH1 ASP E 133 LEU E 137 5 5
HELIX 65 AH2 THR E 142 VAL E 147 1 6
HELIX 66 AH3 ASP F 76 ASN F 87 1 12
HELIX 67 AH4 THR F 88 GLN F 111 1 24
HELIX 68 AH5 GLY F 113 LEU F 117 5 5
HELIX 69 AH6 CYS F 123 LEU F 146 1 24
HELIX 70 AH7 SER G 4 SER G 18 1 15
HELIX 71 AH8 SER G 18 GLY G 37 1 20
HELIX 72 AH9 TYR G 38 GLY G 42 5 5
HELIX 73 AI1 LYS G 44 ILE G 49 1 6
HELIX 74 AI2 ASN G 53 LEU G 63 1 11
HELIX 75 AI3 PRO G 64 THR G 84 1 21
HELIX 76 AI4 LEU G 103 ASN G 122 1 20
HELIX 77 AI5 PRO H 31 GLN H 34 5 4
HELIX 78 AI6 GLY H 39 PHE H 46 1 8
HELIX 79 AI7 PHE H 46 GLN H 55 1 10
HELIX 80 AI8 PHE H 56 TYR H 81 1 26
HELIX 81 AI9 GLY H 85 VAL H 94 1 10
HELIX 82 AJ1 PHE I 3 PHE I 11 1 9
HELIX 83 AJ2 ARG I 13 ASN I 44 1 32
HELIX 84 AJ3 LEU I 48 ALA I 58 1 11
HELIX 85 AJ4 LEU J 20 THR J 45 1 26
HELIX 86 AJ5 TRP J 48 LEU J 55 1 8
HELIX 87 AJ6 TYR J 56 ILE J 59 5 4
HELIX 88 AJ7 LEU J 62 GLU J 67 1 6
HELIX 89 AJ8 GLY L 58 GLU L 62 5 5
HELIX 90 AJ9 GLY L 68 LEU L 78 1 11
HELIX 91 AK1 SER L 79 GLY L 90 1 12
HELIX 92 AK2 SER L 112 ILE L 125 1 14
HELIX 93 AK3 ASN L 136 ASP L 155 1 20
HELIX 94 AK4 ASP L 155 PHE L 169 1 15
HELIX 95 AK5 THR L 172 LEU L 176 5 5
HELIX 96 AK6 VAL L 189 PHE L 201 1 13
HELIX 97 AK7 LYS L 215 LYS L 226 1 12
HELIX 98 AK8 ASN L 274 GLY L 286 1 13
HELIX 99 AK9 LEU L 302 GLN L 307 1 6
HELIX 100 AL1 MET L 339 SER L 357 1 19
HELIX 101 AL2 THR L 359 GLU L 379 1 21
HELIX 102 AL3 ASN L 382 LYS L 397 1 16
HELIX 103 AL4 SER L 402 ALA L 412 1 11
HELIX 104 AL5 THR L 414 LEU L 426 1 13
HELIX 105 AL6 ASP L 444 SER L 450 1 7
HELIX 106 AL7 GLY M 38 ALA M 42 5 5
HELIX 107 AL8 GLY M 46 PHE M 54 1 9
HELIX 108 AL9 SER M 63 GLY M 75 1 13
HELIX 109 AM1 ASP M 97 LYS M 111 1 15
HELIX 110 AM2 LYS M 115 SER M 122 1 8
HELIX 111 AM3 SER M 122 CYS M 137 1 16
HELIX 112 AM4 CYS M 137 PHE M 151 1 15
HELIX 113 AM5 SER M 168 TYR M 180 1 13
HELIX 114 AM6 VAL M 193 ASP M 202 1 10
HELIX 115 AM7 SER M 249 SER M 262 1 14
HELIX 116 AM8 ASP M 293 LYS M 310 1 18
HELIX 117 AM9 ALA M 317 GLU M 330 1 14
HELIX 118 AN1 ALA N 2 ASN N 7 1 6
HELIX 119 AN2 TYR N 9 ILE N 17 1 9
HELIX 120 AN3 ASN N 27 TRP N 30 5 4
HELIX 121 AN4 ASN N 31 MET N 52 1 22
HELIX 122 AN5 LEU N 60 ASP N 71 1 12
HELIX 123 AN6 ASN N 74 GLY N 104 1 31
HELIX 124 AN7 ARG N 107 PRO N 109 5 3
HELIX 125 AN8 ARG N 110 TYR N 136 1 27
HELIX 126 AN9 GLY N 137 LEU N 150 1 14
HELIX 127 AO1 PHE N 151 ALA N 153 5 3
HELIX 128 AO2 VAL N 157 TRP N 166 1 10
HELIX 129 AO3 SER N 172 ILE N 203 1 32
HELIX 130 AO4 TYR N 224 TYR N 246 1 23
HELIX 131 AO5 HIS N 253 ILE N 258 5 6
HELIX 132 AO6 GLU N 272 TYR N 274 5 3
HELIX 133 AO7 LEU N 275 ILE N 285 1 11
HELIX 134 AO8 ASP N 287 VAL N 301 1 15
HELIX 135 AO9 VAL N 304 ASP N 309 1 6
HELIX 136 AP1 GLY N 315 PHE N 318 5 4
HELIX 137 AP2 LYS N 319 CYS N 342 1 24
HELIX 138 AP3 GLU N 345 ILE N 365 1 21
HELIX 139 AP4 ILE N 365 GLY N 381 1 17
HELIX 140 AP5 THR O 63 GLY O 68 1 6
HELIX 141 AP6 ASP O 86 VAL O 100 1 15
HELIX 142 AP7 CYS O 101 CYS O 104 5 4
HELIX 143 AP8 ALA O 111 LEU O 115 5 5
HELIX 144 AP9 THR O 121 PHE O 132 1 12
HELIX 145 AQ1 ASN O 161 ASN O 169 1 9
HELIX 146 AQ2 GLY O 187 GLY O 197 1 11
HELIX 147 AQ3 THR O 243 GLU O 260 1 18
HELIX 148 AQ4 GLU O 262 TRP O 292 1 31
HELIX 149 AQ5 TRP O 292 THR O 297 1 6
HELIX 150 AQ6 ASP P 48 ALA P 84 1 37
HELIX 151 AQ7 THR P 85 ALA P 90 1 6
HELIX 152 AQ8 THR P 122 ASN P 130 1 9
HELIX 153 AQ9 ASP P 133 LEU P 137 5 5
HELIX 154 AR1 THR P 142 VAL P 147 1 6
HELIX 155 AR2 ASP Q 76 ASN Q 87 1 12
HELIX 156 AR3 THR Q 88 GLN Q 111 1 24
HELIX 157 AR4 CYS Q 123 LEU Q 146 1 24
HELIX 158 AR5 SER R 4 SER R 18 1 15
HELIX 159 AR6 SER R 18 GLY R 37 1 20
HELIX 160 AR7 TYR R 38 GLY R 42 5 5
HELIX 161 AR8 LYS R 44 LEU R 48 5 5
HELIX 162 AR9 ASN R 53 ARG R 62 1 10
HELIX 163 AS1 PRO R 64 THR R 84 1 21
HELIX 164 AS2 LEU R 103 ASN R 122 1 20
HELIX 165 AS3 PRO S 31 GLN S 34 5 4
HELIX 166 AS4 GLY S 39 PHE S 46 1 8
HELIX 167 AS5 PHE S 46 GLN S 55 1 10
HELIX 168 AS6 PHE S 56 TYR S 81 1 26
HELIX 169 AS7 GLY S 85 VAL S 94 1 10
HELIX 170 AS8 PHE T 3 PHE T 11 1 9
HELIX 171 AS9 ARG T 13 ASN T 44 1 32
HELIX 172 AT1 LEU T 48 ALA T 58 1 11
HELIX 173 AT2 SER U 19 THR U 45 1 27
HELIX 174 AT3 TRP U 48 LEU U 55 1 8
HELIX 175 AT4 VAL a 2 TYR a 7 1 6
HELIX 176 AT5 ASN a 10 LEU a 40 1 31
HELIX 177 AT6 ASN a 51 PHE a 69 1 19
HELIX 178 AT7 LEU a 70 ILE a 76 1 7
HELIX 179 AT8 ILE a 76 LEU a 84 1 9
HELIX 180 AT9 PHE a 95 VAL a 119 1 25
HELIX 181 AU1 PRO a 142 MET a 172 1 31
HELIX 182 AU2 THR a 178 LEU a 182 5 5
HELIX 183 AU3 PRO a 183 PHE a 216 1 34
HELIX 184 AU4 ASP a 228 LYS a 264 1 37
HELIX 185 AU5 GLY a 269 PHE a 285 1 17
HELIX 186 AU6 VAL a 287 HIS a 291 5 5
HELIX 187 AU7 ASP a 298 ILE a 312 1 15
HELIX 188 AU8 ILE a 312 HIS a 328 1 17
HELIX 189 AU9 ALA a 335 ALA a 359 1 25
HELIX 190 AV1 LEU a 363 HIS a 368 1 6
HELIX 191 AV2 THR a 370 GLY a 402 1 33
HELIX 192 AV3 ASN a 406 PHE a 426 1 21
HELIX 193 AV4 PHE a 426 ASN a 434 1 9
HELIX 194 AV5 PHE a 447 ASN a 478 1 32
HELIX 195 AV6 ASN a 478 ASN a 485 1 8
HELIX 196 AV7 SER a 500 LEU a 506 1 7
HELIX 197 AV8 SER a 513 LEU a 518 5 6
HELIX 198 AV9 THR b 30 SER b 66 1 37
HELIX 199 AW1 GLY b 78 ASP b 108 1 31
HELIX 200 AW2 SER b 240 GLN b 251 1 12
HELIX 201 AW3 THR c 2 SER c 7 1 6
HELIX 202 AW4 PRO c 21 MET c 41 1 21
HELIX 203 AW5 MET c 48 TYR c 75 1 28
HELIX 204 AW6 THR c 80 SER c 115 1 36
HELIX 205 AW7 GLU c 136 GLY c 162 1 27
HELIX 206 AW8 ASN c 163 ASN c 191 1 29
HELIX 207 AW9 ASP c 198 ASN c 232 1 35
HELIX 208 AX1 VAL c 241 TRP c 267 1 27
HELIX 209 AX2 THR d 58 GLU d 63 1 6
HELIX 210 AX3 THR d 64 GLY d 77 1 14
HELIX 211 AX4 SER e 27 MET e 32 1 6
HELIX 212 AX5 ASP e 33 TRP e 38 1 6
HELIX 213 AX6 PRO e 42 LYS e 58 1 17
HELIX 214 AX7 LEU e 59 LEU e 64 5 6
HELIX 215 AX8 THR e 65 GLY e 78 1 14
HELIX 216 AX9 TRP e 80 ARG e 84 5 5
HELIX 217 AY1 GLY e 90 ALA e 116 1 27
HELIX 218 AY2 ASN e 125 LYS e 139 1 15
HELIX 219 AY3 THR f 48 ALA f 63 1 16
HELIX 220 AY4 ASP f 65 SER f 78 1 14
HELIX 221 AY5 ALA f 84 VAL f 98 1 15
HELIX 222 AY6 LEU f 101 VAL f 115 1 15
HELIX 223 AY7 ASN f 117 ASP f 126 1 10
HELIX 224 AY8 LEU f 128 GLY f 136 1 9
HELIX 225 AY9 LEU f 139 PHE f 144 1 6
HELIX 226 AZ1 LYS g 4 SER g 14 1 11
HELIX 227 AZ2 ARG g 25 TYR g 47 1 23
HELIX 228 AZ3 TYR g 47 GLY g 54 1 8
HELIX 229 AZ4 PRO h 48 LYS h 74 1 27
HELIX 230 AZ5 GLY i 8 LYS i 56 1 49
HELIX 231 AZ6 GLN j 23 MET j 40 1 18
HELIX 232 AZ7 ASP j 44 CYS j 59 1 16
HELIX 233 AZ8 PRO j 60 LYS j 73 1 14
HELIX 234 AZ9 LYS k 27 VAL k 58 1 32
HELIX 235 BA1 VAL k 58 HIS k 86 1 29
HELIX 236 BA2 SER l 27 TRP l 53 1 27
HELIX 237 BA3 TRP l 53 PHE l 60 1 8
HELIX 238 BA4 SER l 61 LYS l 65 5 5
HELIX 239 BA5 VAL m 2 TYR m 7 1 6
HELIX 240 BA6 ASN m 10 LEU m 40 1 31
HELIX 241 BA7 ASN m 51 PHE m 69 1 19
HELIX 242 BA8 LEU m 70 ILE m 76 1 7
HELIX 243 BA9 ILE m 76 MET m 87 1 12
HELIX 244 BB1 PHE m 95 VAL m 119 1 25
HELIX 245 BB2 PRO m 142 MET m 172 1 31
HELIX 246 BB3 THR m 178 LEU m 182 5 5
HELIX 247 BB4 PRO m 183 PHE m 216 1 34
HELIX 248 BB5 PRO m 229 SER m 263 1 35
HELIX 249 BB6 GLY m 269 PHE m 285 1 17
HELIX 250 BB7 VAL m 287 HIS m 291 5 5
HELIX 251 BB8 ASP m 298 ILE m 312 1 15
HELIX 252 BB9 ILE m 312 HIS m 328 1 17
HELIX 253 BC1 ALA m 335 ASN m 360 1 26
HELIX 254 BC2 LEU m 363 HIS m 368 1 6
HELIX 255 BC3 THR m 370 GLY m 402 1 33
HELIX 256 BC4 ASN m 406 PHE m 426 1 21
HELIX 257 BC5 PHE m 426 ASN m 434 1 9
HELIX 258 BC6 PHE m 447 ASN m 478 1 32
HELIX 259 BC7 ASN m 478 ASN m 485 1 8
HELIX 260 BC8 SER m 500 LEU m 506 1 7
HELIX 261 BC9 SER m 513 LEU m 517 5 5
HELIX 262 BD1 THR n 30 SER n 66 1 37
HELIX 263 BD2 GLY n 78 ASP n 108 1 31
HELIX 264 BD3 PRO n 149 LEU n 153 5 5
HELIX 265 BD4 GLY n 226 ALA n 230 5 5
HELIX 266 BD5 SER n 240 GLN n 251 1 12
HELIX 267 BD6 GLU o 5 HIS o 9 5 5
HELIX 268 BD7 PRO o 21 MET o 41 1 21
HELIX 269 BD8 MET o 48 TYR o 75 1 28
HELIX 270 BD9 THR o 80 SER o 115 1 36
HELIX 271 BE1 LEU o 137 ALA o 161 1 25
HELIX 272 BE2 ASN o 163 ASN o 191 1 29
HELIX 273 BE3 ASP o 198 ASN o 232 1 35
HELIX 274 BE4 VAL o 241 TYR o 265 1 25
HELIX 275 BE5 ASN p 36 VAL p 40 5 5
HELIX 276 BE6 PRO p 43 ILE p 47 5 5
HELIX 277 BE7 THR p 58 GLU p 63 1 6
HELIX 278 BE8 THR p 64 GLY p 77 1 14
HELIX 279 BE9 SER q 27 MET q 32 1 6
HELIX 280 BF1 ASP q 33 TRP q 38 1 6
HELIX 281 BF2 PRO q 42 GLN q 57 1 16
HELIX 282 BF3 LYS q 58 LEU q 59 5 2
HELIX 283 BF4 PRO q 60 LEU q 64 5 5
HELIX 284 BF5 THR q 65 GLY q 78 1 14
HELIX 285 BF6 TRP q 80 ARG q 84 5 5
HELIX 286 BF7 GLY q 90 ALA q 116 1 27
HELIX 287 BF8 ASN q 125 LYS q 139 1 15
HELIX 288 BF9 THR r 48 ALA r 63 1 16
HELIX 289 BG1 ASP r 65 SER r 78 1 14
HELIX 290 BG2 ALA r 84 VAL r 98 1 15
HELIX 291 BG3 ASP r 100 VAL r 115 1 16
HELIX 292 BG4 GLU r 118 LEU r 128 1 11
HELIX 293 BG5 LEU r 128 GLY r 136 1 9
HELIX 294 BG6 LYS s 4 SER s 14 1 11
HELIX 295 BG7 PRO s 18 ARG s 22 5 5
HELIX 296 BG8 ARG s 25 TYR s 47 1 23
HELIX 297 BG9 TYR s 47 GLY s 54 1 8
HELIX 298 BH1 PRO t 48 LYS t 74 1 27
HELIX 299 BH2 GLY u 8 LYS u 56 1 49
HELIX 300 BH3 GLN v 23 MET v 40 1 18
HELIX 301 BH4 ASP v 44 CYS v 59 1 16
HELIX 302 BH5 PRO v 60 LYS v 73 1 14
HELIX 303 BH6 PRO w 14 LYS w 19 5 6
HELIX 304 BH7 LYS w 27 VAL w 58 1 32
HELIX 305 BH8 VAL w 58 HIS w 86 1 29
HELIX 306 BH9 SER x 27 TRP x 53 1 27
HELIX 307 BI1 TRP x 53 SER x 61 1 9
HELIX 308 BI2 LYS x 62 LYS x 65 5 4
SHEET 1 AA1 6 VAL A 29 LEU A 32 0
SHEET 2 AA1 6 VAL A 37 HIS A 42 -1 O THR A 40 N VAL A 29
SHEET 3 AA1 6 ALA A 206 GLY A 212 1 O VAL A 208 N ALA A 39
SHEET 4 AA1 6 ALA A 49 PHE A 55 -1 N VAL A 54 O VAL A 207
SHEET 5 AA1 6 GLN A 102 SER A 108 -1 O VAL A 106 N VAL A 51
SHEET 6 AA1 6 LEU A 91 ILE A 97 -1 N ALA A 92 O SER A 107
SHEET 1 AA2 8 SER A 287 ASN A 289 0
SHEET 2 AA2 8 ASN A 314 SER A 321 -1 O PHE A 315 N TYR A 288
SHEET 3 AA2 8 GLY A 326 THR A 334 -1 O LEU A 327 N LEU A 320
SHEET 4 AA2 8 ALA A 259 GLY A 267 -1 N VAL A 265 O TRP A 328
SHEET 5 AA2 8 ALA A 432 GLY A 437 -1 O ALA A 432 N ALA A 264
SHEET 6 AA2 8 SER A 247 ARG A 252 1 N LEU A 251 O GLY A 435
SHEET 7 AA2 8 ILE H 24 VAL H 29 -1 O SER H 26 N ARG A 250
SHEET 8 AA2 8 LYS D 299 PHE D 302 -1 N VAL D 301 O THR H 25
SHEET 1 AA3 5 THR B 18 ARG B 22 0
SHEET 2 AA3 5 LEU B 185 GLU B 190 1 O GLY B 189 N SER B 20
SHEET 3 AA3 5 ILE B 28 VAL B 35 -1 N LYS B 34 O GLU B 186
SHEET 4 AA3 5 ILE B 87 LEU B 94 -1 O ILE B 87 N VAL B 35
SHEET 5 AA3 5 THR B 77 LEU B 82 -1 N LYS B 79 O LYS B 90
SHEET 1 AA4 5 GLU B 228 ARG B 232 0
SHEET 2 AA4 5 ASN B 352 GLY B 357 1 O ALA B 355 N VAL B 231
SHEET 3 AA4 5 SER B 237 VAL B 245 -1 N ALA B 240 O VAL B 354
SHEET 4 AA4 5 GLY B 283 ASP B 291 -1 O LEU B 287 N ILE B 241
SHEET 5 AA4 5 SER B 273 LYS B 278 -1 N LYS B 275 O THR B 286
SHEET 1 AA5 2 LYS B 312 ASP B 313 0
SHEET 2 AA5 2 ASP B 345 PHE B 346 -1 O PHE B 346 N LYS B 312
SHEET 1 AA6 2 PRO C 21 PRO C 23 0
SHEET 2 AA6 2 ARG C 218 PRO C 220 -1 O ILE C 219 N GLN C 22
SHEET 1 AA7 2 GLU D 133 ASP D 135 0
SHEET 2 AA7 2 LYS D 146 PRO D 148 -1 O ARG D 147 N TYR D 134
SHEET 1 AA8 2 ASN D 213 TYR D 214 0
SHEET 2 AA8 2 SER D 222 ILE D 223 -1 O ILE D 223 N ASN D 213
SHEET 1 AA9 3 VAL E 94 ASN E 97 0
SHEET 2 AA9 3 LYS E 211 VAL E 214 -1 O VAL E 212 N VAL E 96
SHEET 3 AA9 3 TYR E 205 ASP E 208 -1 N ASP E 208 O LYS E 211
SHEET 1 AB1 3 ASN E 106 TRP E 111 0
SHEET 2 AB1 3 LYS E 114 HIS E 120 -1 O VAL E 116 N VAL E 109
SHEET 3 AB1 3 TRP E 152 LEU E 156 -1 O MET E 155 N PHE E 117
SHEET 1 AB2 2 TRP E 176 CYS E 178 0
SHEET 2 AB2 2 SER E 183 TYR E 185 -1 O SER E 183 N CYS E 178
SHEET 1 AB3 2 GLU G 124 VAL G 125 0
SHEET 2 AB3 2 SER U 9 LYS U 10 -1 O LYS U 10 N GLU G 124
SHEET 1 AB4 2 SER J 9 LYS J 10 0
SHEET 2 AB4 2 GLU R 124 VAL R 125 -1 O GLU R 124 N LYS J 10
SHEET 1 AB5 2 HIS J 14 PHE J 15 0
SHEET 2 AB5 2 LEU J 18 SER J 19 -1 O LEU J 18 N PHE J 15
SHEET 1 AB6 6 VAL L 29 LEU L 32 0
SHEET 2 AB6 6 VAL L 37 HIS L 42 -1 O THR L 40 N VAL L 29
SHEET 3 AB6 6 ALA L 206 GLY L 212 1 O GLY L 210 N ALA L 39
SHEET 4 AB6 6 ALA L 49 PHE L 55 -1 N VAL L 54 O VAL L 207
SHEET 5 AB6 6 GLN L 102 SER L 108 -1 O GLN L 102 N PHE L 55
SHEET 6 AB6 6 ALA L 92 ILE L 97 -1 N ALA L 92 O SER L 107
SHEET 1 AB7 7 ASN L 314 SER L 321 0
SHEET 2 AB7 7 GLY L 326 ALA L 333 -1 O SER L 331 N ASN L 316
SHEET 3 AB7 7 ALA L 259 GLY L 267 -1 N VAL L 265 O TRP L 328
SHEET 4 AB7 7 ILE L 431 GLY L 437 -1 O ALA L 432 N ALA L 264
SHEET 5 AB7 7 SER L 247 ARG L 252 1 N LEU L 251 O GLY L 435
SHEET 6 AB7 7 ILE S 24 VAL S 29 -1 O ALA S 28 N GLU L 248
SHEET 7 AB7 7 LYS O 299 PHE O 302 -1 N VAL O 301 O THR S 25
SHEET 1 AB8 5 THR M 18 ARG M 22 0
SHEET 2 AB8 5 LEU M 185 GLU M 190 1 O GLY M 189 N SER M 20
SHEET 3 AB8 5 ILE M 28 VAL M 35 -1 N LYS M 34 O GLU M 186
SHEET 4 AB8 5 ILE M 87 LEU M 94 -1 O ILE M 87 N VAL M 35
SHEET 5 AB8 5 THR M 77 LEU M 82 -1 N LYS M 79 O LYS M 90
SHEET 1 AB9 5 GLU M 228 ARG M 232 0
SHEET 2 AB9 5 ASN M 352 GLY M 357 1 O ALA M 355 N VAL M 231
SHEET 3 AB9 5 SER M 237 VAL M 245 -1 N ALA M 240 O VAL M 354
SHEET 4 AB9 5 GLY M 283 ASP M 291 -1 O PHE M 285 N ILE M 243
SHEET 5 AB9 5 SER M 273 LYS M 278 -1 N LYS M 275 O THR M 286
SHEET 1 AC1 2 LYS M 312 ASP M 313 0
SHEET 2 AC1 2 ASP M 345 PHE M 346 -1 O PHE M 346 N LYS M 312
SHEET 1 AC2 2 PRO N 21 PRO N 23 0
SHEET 2 AC2 2 ARG N 218 PRO N 220 -1 O ILE N 219 N GLN N 22
SHEET 1 AC3 2 GLU O 133 ASP O 135 0
SHEET 2 AC3 2 LYS O 146 PRO O 148 -1 O ARG O 147 N TYR O 134
SHEET 1 AC4 2 ASN O 213 TYR O 214 0
SHEET 2 AC4 2 SER O 222 ILE O 223 -1 O ILE O 223 N ASN O 213
SHEET 1 AC5 3 VAL P 94 ASN P 97 0
SHEET 2 AC5 3 LYS P 211 VAL P 214 -1 O VAL P 212 N VAL P 96
SHEET 3 AC5 3 TYR P 205 ASP P 208 -1 N ASP P 208 O LYS P 211
SHEET 1 AC6 3 ASN P 106 TRP P 111 0
SHEET 2 AC6 3 LYS P 114 HIS P 120 -1 O VAL P 116 N VAL P 109
SHEET 3 AC6 3 TRP P 152 LEU P 156 -1 O LEU P 153 N ARG P 119
SHEET 1 AC7 2 TRP P 176 CYS P 178 0
SHEET 2 AC7 2 SER P 183 TYR P 185 -1 O TYR P 185 N TRP P 176
SHEET 1 AC8 3 VAL a 532 GLN a 533 0
SHEET 2 AC8 3 VAL d 109 CYS d 111 1 O GLY d 110 N VAL a 532
SHEET 3 AC8 3 MET d 122 LEU d 124 -1 O LEU d 124 N VAL d 109
SHEET 1 AC9 5 VAL b 141 SER b 145 0
SHEET 2 AC9 5 TRP b 126 TYR b 130 -1 N TRP b 126 O SER b 145
SHEET 3 AC9 5 MET b 115 ILE b 120 -1 N LYS b 118 O GLU b 129
SHEET 4 AC9 5 HIS b 174 VAL b 179 1 O ARG b 176 N ILE b 117
SHEET 5 AC9 5 ASN b 205 LEU b 210 -1 O ASN b 205 N VAL b 179
SHEET 1 AD1 3 MET b 167 PRO b 170 0
SHEET 2 AD1 3 PRO b 233 VAL b 239 1 O GLU b 237 N VAL b 169
SHEET 3 AD1 3 GLY b 215 ALA b 220 -1 N PHE b 217 O ILE b 236
SHEET 1 AD2 2 HIS b 186 ILE b 190 0
SHEET 2 AD2 2 ILE b 195 ALA b 199 -1 O ILE b 195 N ILE b 190
SHEET 1 AD3 3 ILE d 98 SER d 102 0
SHEET 2 AD3 3 VAL d 140 PRO d 145 1 O ASN d 144 N ILE d 100
SHEET 3 AD3 3 ALA d 132 ARG d 133 -1 N ALA d 132 O TYR d 141
SHEET 1 AD4 3 VAL m 532 GLN m 533 0
SHEET 2 AD4 3 VAL p 109 CYS p 111 1 O GLY p 110 N VAL m 532
SHEET 3 AD4 3 MET p 122 LEU p 124 -1 O MET p 122 N CYS p 111
SHEET 1 AD5 5 VAL n 141 SER n 145 0
SHEET 2 AD5 5 TYR n 125 TYR n 130 -1 N TYR n 128 O PHE n 143
SHEET 3 AD5 5 MET n 115 TYR n 122 -1 N LYS n 118 O GLU n 129
SHEET 4 AD5 5 HIS n 174 VAL n 179 1 O ARG n 176 N ILE n 117
SHEET 5 AD5 5 ASN n 205 LEU n 210 -1 O ASN n 205 N VAL n 179
SHEET 1 AD6 3 MET n 167 PRO n 170 0
SHEET 2 AD6 3 PRO n 233 VAL n 239 1 O GLU n 237 N VAL n 169
SHEET 3 AD6 3 GLY n 215 ALA n 220 -1 N PHE n 217 O ILE n 236
SHEET 1 AD7 2 HIS n 186 ILE n 190 0
SHEET 2 AD7 2 ILE n 195 ALA n 199 -1 O ILE n 195 N ILE n 190
SHEET 1 AD8 3 ILE p 98 SER p 102 0
SHEET 2 AD8 3 VAL p 140 PRO p 145 1 O VAL p 140 N ILE p 98
SHEET 3 AD8 3 ALA p 132 ARG p 133 -1 N ALA p 132 O TYR p 141
SSBOND 1 CYS E 164 CYS E 180 1555 1555 2.04
SSBOND 2 CYS F 101 CYS F 123 1555 1555 2.04
SSBOND 3 CYS P 164 CYS P 180 1555 1555 2.03
SSBOND 4 CYS Q 101 CYS Q 123 1555 1555 2.03
SSBOND 5 CYS b 221 CYS b 225 1555 1555 2.84
SSBOND 6 CYS j 27 CYS j 59 1555 1555 2.03
SSBOND 7 CYS j 37 CYS j 48 1555 1555 2.02
SSBOND 8 CYS n 221 CYS n 225 1555 1555 2.73
SSBOND 9 CYS v 27 CYS v 59 1555 1555 2.03
SSBOND 10 CYS v 37 CYS v 48 1555 1555 2.03
LINK NE2 HIS C 82 FE HEM C 601 1555 1555 1.99
LINK NE2 HIS C 96 FE HEM C 602 1555 1555 1.99
LINK NE2 HIS C 183 FE HEM C 601 1555 1555 2.00
LINK NE2 HIS C 197 FE HEM C 602 1555 1555 1.99
LINK SG CYS D 101 CAB HEC D 401 1555 1555 1.80
LINK SG CYS D 104 CAC HEC D 401 1555 1555 1.80
LINK NE2 HIS D 105 FE HEC D 401 1555 1555 1.99
LINK SD MET D 225 FE HEC D 401 1555 1555 1.99
LINK SG CYS E 159 FE1 FES E 301 1555 1555 2.19
LINK ND1 HIS E 161 FE2 FES E 301 1555 1555 2.16
LINK SG CYS E 178 FE1 FES E 301 1555 1555 2.17
LINK ND1 HIS E 181 FE2 FES E 301 1555 1555 2.11
LINK NE2 HIS N 82 FE HEM N 601 1555 1555 1.98
LINK NE2 HIS N 96 FE HEM N 602 1555 1555 1.99
LINK NE2 HIS N 183 FE HEM N 601 1555 1555 2.00
LINK NE2 HIS N 197 FE HEM N 602 1555 1555 2.00
LINK SG CYS O 101 CAB HEC O 401 1555 1555 1.80
LINK SG CYS O 104 CAC HEC O 401 1555 1555 1.80
LINK NE2 HIS O 105 FE HEC O 401 1555 1555 1.99
LINK SD MET O 225 FE HEC O 401 1555 1555 1.99
LINK SG CYS P 159 FE1 FES P 301 1555 1555 2.13
LINK ND1 HIS P 161 FE2 FES P 301 1555 1555 2.15
LINK SG CYS P 178 FE1 FES P 301 1555 1555 2.11
LINK ND1 HIS P 181 FE2 FES P 301 1555 1555 2.08
LINK O GLU a 39 CA CA a 604 1555 1555 2.54
LINK OE1 GLU a 39 CA CA a 604 1555 1555 3.07
LINK O ALA a 42 CA CA a 604 1555 1555 2.61
LINK O GLY a 44 CA CA a 604 1555 1555 2.75
LINK NE2 HIS a 62 FE HEA a 602 1555 1555 1.99
LINK ND1 HIS a 241 CU CU a 601 1555 1555 2.10
LINK NE2 HIS a 290 CU CU a 601 1555 1555 2.14
LINK NE2 HIS a 291 CU CU a 601 1555 1555 2.06
LINK OD1 ASP a 369 MG MG a 605 1555 1555 2.13
LINK NE2 HIS a 376 FE HEA a 603 1555 1555 1.99
LINK NE2 HIS a 378 FE HEA a 602 1555 1555 1.99
LINK O PRO a 441 CA CA a 604 1555 1555 3.20
LINK ND1 HIS b 186 CU1 CUA b 301 1555 1555 2.11
LINK SG CYS b 221 CU1 CUA b 301 1555 1555 2.23
LINK SG CYS b 221 CU2 CUA b 302 1555 1555 2.16
LINK O GLU b 223 CU2 CUA b 302 1555 1555 2.54
LINK OE1 GLU b 223 MG MG a 605 1555 1555 2.25
LINK OE2 GLU b 223 MG MG a 605 1555 1555 2.46
LINK SG CYS b 225 CU1 CUA b 301 1555 1555 2.14
LINK SG CYS b 225 CU2 CUA b 302 1555 1555 2.06
LINK ND1 HIS b 229 CU2 CUA b 302 1555 1555 2.04
LINK SD MET b 232 CU1 CUA b 301 1555 1555 2.19
LINK SG CYS d 111 ZN ZN d 201 1555 1555 2.71
LINK SG CYS d 134 ZN ZN d 201 1555 1555 2.49
LINK SG CYS d 137 ZN ZN d 201 1555 1555 2.43
LINK O GLU m 39 CA CA m 604 1555 1555 2.60
LINK O ALA m 42 CA CA m 604 1555 1555 2.56
LINK O GLY m 44 CA CA m 604 1555 1555 3.19
LINK NE2 HIS m 62 FE HEA m 602 1555 1555 1.99
LINK ND1 HIS m 241 CU CU m 601 1555 1555 2.13
LINK NE2 HIS m 290 CU CU m 601 1555 1555 2.17
LINK NE2 HIS m 291 CU CU m 601 1555 1555 2.11
LINK OD1 ASP m 369 MG MG m 605 1555 1555 2.13
LINK NE2 HIS m 376 FE HEA m 603 1555 1555 1.99
LINK NE2 HIS m 378 FE HEA m 602 1555 1555 1.99
LINK ND1 HIS n 186 CU1 CUA n 301 1555 1555 2.09
LINK SG CYS n 221 CU1 CUA n 301 1555 1555 2.31
LINK SG CYS n 221 CU2 CUA n 302 1555 1555 2.26
LINK O GLU n 223 CU2 CUA n 302 1555 1555 2.41
LINK OE1 GLU n 223 MG MG m 605 1555 1555 2.18
LINK OE2 GLU n 223 MG MG m 605 1555 1555 2.61
LINK SG CYS n 225 CU1 CUA n 301 1555 1555 2.00
LINK SG CYS n 225 CU2 CUA n 302 1555 1555 2.22
LINK ND1 HIS n 229 CU2 CUA n 302 1555 1555 2.16
LINK SD MET n 232 CU1 CUA n 301 1555 1555 2.20
LINK SG CYS p 111 ZN ZN p 201 1555 1555 2.97
LINK SG CYS p 134 ZN ZN p 201 1555 1555 2.47
LINK SG CYS p 137 ZN ZN p 201 1555 1555 2.48
LINK CU1 CUA b 301 CU2 CUA b 302 1555 1555 2.60
LINK CU1 CUA n 301 CU2 CUA n 302 1555 1555 2.60
CISPEP 1 PRO a 131 PRO a 132 0 2.25
CISPEP 2 TRP c 124 PRO c 125 0 1.94
CISPEP 3 PRO m 131 PRO m 132 0 -8.28
CISPEP 4 TRP o 124 PRO o 125 0 0.43
SITE 1 AC1 8 SER A 450 SER A 453 SER C 34 HIS C 222
SITE 2 AC1 8 PHE C 227 CDL C 604 LYS D 291 PCF I 101
SITE 1 AC2 15 LEU C 40 GLN C 43 GLY C 47 ILE C 48
SITE 2 AC2 15 MET C 50 ARG C 79 HIS C 82 ALA C 86
SITE 3 AC2 15 GLY C 131 VAL C 135 PHE C 180 HIS C 183
SITE 4 AC2 15 TYR C 184 PRO C 187 TYR C 274
SITE 1 AC3 15 TRP C 30 GLY C 33 LEU C 36 HIS C 96
SITE 2 AC3 15 MET C 97 LYS C 99 SER C 105 GLY C 117
SITE 3 AC3 15 VAL C 118 ILE C 120 VAL C 194 HIS C 197
SITE 4 AC3 15 LEU C 201 SER C 206 SER C 207
SITE 1 AC4 7 LEU C 12 TYR C 16 MET C 199 LEU N 12
SITE 2 AC4 7 TYR N 16 ILE N 17 MET N 199
SITE 1 AC5 10 HIS A 345 MET A 454 MET A 455 TRP A 457
SITE 2 AC5 10 PEF A 501 ARG C 4 ILE C 18 HIS C 222
SITE 3 AC5 10 PEF C 606 TRP J 33
SITE 1 AC6 8 PHE C 3 SER C 6 ASN C 7 VAL C 8
SITE 2 AC6 8 TYR C 9 VAL C 13 THR N 112 ASN N 115
SITE 1 AC7 5 HIS A 345 TRP A 457 ALA C 2 PHE C 3
SITE 2 AC7 5 CDL C 604
SITE 1 AC8 9 TRP C 29 ALA C 98 TYR C 102 TYR C 103
SITE 2 AC8 9 THR C 317 PHE C 326 PHE C 327 GLN H 55
SITE 3 AC8 9 CDL H 601
SITE 1 AC9 12 VAL D 100 CYS D 101 CYS D 104 HIS D 105
SITE 2 AC9 12 ASN D 169 ALA D 172 PRO D 175 ARG D 184
SITE 3 AC9 12 TYR D 190 PHE D 218 ALA D 224 MET D 225
SITE 1 AD1 9 LEU C 81 MET C 237 LEU D 269 LYS D 272
SITE 2 AD1 9 THR D 273 ILE D 276 GLY E 70 SER E 73
SITE 3 AD1 9 THR E 77
SITE 1 AD2 8 CYS E 159 HIS E 161 LEU E 162 GLY E 163
SITE 2 AD2 8 CYS E 164 CYS E 178 HIS E 181 SER E 183
SITE 1 AD3 10 TRP D 286 LYS E 44 LYS E 51 TYR E 55
SITE 2 AD3 10 PHE E 58 MET E 59 PRO H 36 PCF H 604
SITE 3 AD3 10 PHE I 3 LYS e 97
SITE 1 AD4 10 GLU E 76 ILE E 79 SER E 80 THR E 83
SITE 2 AD4 10 PHE J 44 GLY J 47 TRP J 48 PRO J 49
SITE 3 AD4 10 ILE N 161 TRP N 164
SITE 1 AD5 12 ASN C 27 TYR C 28 TRP C 29 PHE C 88
SITE 2 AD5 12 PCF C 607 HIS G 85 ALA H 44 SER H 48
SITE 3 AD5 12 ARG H 51 PHE H 52 GLN H 55 CDL H 602
SITE 1 AD6 13 TYR C 28 TYR D 281 LEU D 282 ILE D 285
SITE 2 AD6 13 LYS D 288 LYS D 289 HIS G 85 ILE H 40
SITE 3 AD6 13 ASN H 43 ALA H 44 ASN H 47 ARG H 51
SITE 4 AD6 13 CDL H 601
SITE 1 AD7 4 LYS H 53 SER H 54 LEU H 57 TYR H 58
SITE 1 AD8 7 CDL E 302 GLY H 39 PHE H 41 HIS H 42
SITE 2 AD8 7 SER e 93 ALA e 96 LYS e 97
SITE 1 AD9 12 ASP A 428 SER A 453 MET A 455 PEF A 501
SITE 2 AD9 12 TYR E 57 VAL E 60 GLY E 64 PHE I 11
SITE 3 AD9 12 LYS I 12 ASN I 14 PHE I 17 VAL I 18
SITE 1 AE1 10 HIS L 345 MET L 454 MET L 455 TRP L 457
SITE 2 AE1 10 ARG N 4 HIS N 222 PEF N 603 PEF N 605
SITE 3 AE1 10 PCF T 101 TRP U 33
SITE 1 AE2 16 GLN N 43 GLY N 47 ILE N 48 MET N 50
SITE 2 AE2 16 ARG N 79 HIS N 82 ALA N 83 ALA N 86
SITE 3 AE2 16 THR N 127 GLY N 131 VAL N 135 PHE N 180
SITE 4 AE2 16 HIS N 183 TYR N 184 PRO N 187 TYR N 274
SITE 1 AE3 17 TRP N 30 GLY N 33 LEU N 36 GLY N 37
SITE 2 AE3 17 HIS N 96 MET N 97 LYS N 99 SER N 105
SITE 3 AE3 17 LEU N 113 TRP N 114 GLY N 117 VAL N 118
SITE 4 AE3 17 ILE N 120 VAL N 194 HIS N 197 SER N 206
SITE 5 AE3 17 SER N 207
SITE 1 AE4 8 SER L 450 CDL L 501 SER N 34 HIS N 222
SITE 2 AE4 8 ILE N 226 PHE N 227 SER P 67 PCF T 101
SITE 1 AE5 4 THR C 112 ASN C 115 PHE N 3 ASN N 7
SITE 1 AE6 5 HIS L 345 TRP L 457 CDL L 501 PHE N 3
SITE 2 AE6 5 ARG U 17
SITE 1 AE7 9 TRP N 29 ALA N 98 TYR N 102 TYR N 103
SITE 2 AE7 9 PHE N 327 VAL N 330 GLU R 82 VAL S 59
SITE 3 AE7 9 CDL S 601
SITE 1 AE8 13 VAL O 100 CYS O 101 CYS O 104 HIS O 105
SITE 2 AE8 13 ASN O 169 ARG O 184 TYR O 190 ILE O 191
SITE 3 AE8 13 LEU O 195 PHE O 218 ILE O 223 MET O 225
SITE 4 AE8 13 VAL O 228
SITE 1 AE9 11 TYR N 28 VAL N 231 TYR O 281 LEU O 282
SITE 2 AE9 11 LYS O 288 LYS O 289 CDL P 302 HIS R 85
SITE 3 AE9 11 ASN S 47 ARG S 51 CDL S 601
SITE 1 AF1 8 ILE N 42 LEU O 269 LYS O 272 THR O 273
SITE 2 AF1 8 GLY P 70 SER P 73 THR P 77 PHE P 78
SITE 1 AF2 8 CYS P 159 HIS P 161 LEU P 162 GLY P 163
SITE 2 AF2 8 CYS P 164 CYS P 178 HIS P 181 SER P 183
SITE 1 AF3 11 TRP O 286 CDL O 402 LYS P 44 LYS P 51
SITE 2 AF3 11 TYR P 55 PHE P 58 MET P 59 PRO S 36
SITE 3 AF3 11 LEU S 37 PHE S 41 PHE T 3
SITE 1 AF4 9 ASP C 160 TRP C 164 GLU P 76 ILE P 79
SITE 2 AF4 9 SER P 80 THR P 83 PHE U 44 TRP U 48
SITE 3 AF4 9 PRO U 49
SITE 1 AF5 9 ASN N 27 TYR N 28 TRP N 29 PCF N 606
SITE 2 AF5 9 CDL O 402 HIS R 85 SER S 48 ARG S 51
SITE 3 AF5 9 GLN S 55
SITE 1 AF6 4 LYS R 40 LYS S 53 LEU S 57 TYR S 58
SITE 1 AF7 8 GLN S 38 GLY S 39 ILE S 40 PHE S 41
SITE 2 AF7 8 HIS S 42 VAL S 45 SER q 93 LYS q 97
SITE 1 AF8 12 ASP L 428 SER L 453 CDL L 501 PEF N 603
SITE 2 AF8 12 TYR P 57 VAL P 60 SER P 68 PHE T 11
SITE 3 AF8 12 LYS T 12 ASN T 14 PHE T 17 VAL T 18
SITE 1 AF9 3 HIS a 241 HIS a 290 HIS a 291
SITE 1 AG1 24 PHE a 19 SER a 33 ARG a 37 VAL a 59
SITE 2 AG1 24 HIS a 62 ALA a 63 MET a 66 ILE a 67
SITE 3 AG1 24 VAL a 71 GLY a 126 TRP a 127 TYR a 371
SITE 4 AG1 24 PHE a 377 HIS a 378 LEU a 381 ILE a 386
SITE 5 AG1 24 LEU a 389 PHE a 390 ILE a 424 PHE a 425
SITE 6 AG1 24 MET a 428 ARG a 438 ARG a 439 LEU a 465
SITE 1 AG2 20 TRP a 127 TRP a 237 VAL a 244 TYR a 245
SITE 2 AG2 20 HIS a 290 THR a 309 GLY a 317 GLY a 352
SITE 3 AG2 20 GLY a 355 LEU a 358 ALA a 359 ASP a 364
SITE 4 AG2 20 HIS a 368 VAL a 373 HIS a 376 PHE a 377
SITE 5 AG2 20 VAL a 380 LEU a 381 ARG a 438 ILE b 50
SITE 1 AG3 4 GLU a 39 ALA a 42 GLY a 44 PRO a 441
SITE 1 AG4 3 HIS a 368 ASP a 369 GLU b 223
SITE 1 AG5 8 PHE a 268 ALA a 325 ILE b 75 ILE b 81
SITE 2 AG5 8 TRP b 85 LYS i 11 VAL i 14 PHE i 22
SITE 1 AG6 9 TYR a 452 VAL a 453 ILE a 456 TYR b 21
SITE 2 AG6 9 PEF e 201 PCF e 202 VAL l 57 PHE l 60
SITE 3 AG6 9 SER l 61
SITE 1 AG7 12 PHE a 95 PRO a 96 ARG a 97 ILE a 98
SITE 2 AG7 12 HIS c 15 SER c 62 TRP c 65 PHE c 66
SITE 3 AG7 12 ILE c 87 GLY c 90 PHE c 91 PHE c 94
SITE 1 AG8 5 HIS b 186 CYS b 221 CYS b 225 MET b 232
SITE 2 AG8 5 CUA b 302
SITE 1 AG9 5 CYS b 221 GLU b 223 CYS b 225 HIS b 229
SITE 2 AG9 5 CUA b 301
SITE 1 AH1 11 HIS a 429 PHE a 430 TRP a 450 PRO b 20
SITE 2 AH1 11 TYR b 21 CYS b 23 SER e 148 PHE i 36
SITE 3 AH1 11 PRO l 54 GLY l 55 TYR l 58
SITE 1 AH2 13 PHE c 66 ILE c 69 VAL c 70 ALA c 73
SITE 2 AH2 13 THR c 74 ILE c 87 ARG c 229 HIS c 234
SITE 3 AH2 13 THR c 236 HIS c 239 HIS c 240 VAL c 241
SITE 4 AH2 13 GLY c 242
SITE 1 AH3 13 THR a 208 PHE a 216 TYR c 189 ALA c 192
SITE 2 AH3 13 PHE c 194 THR c 195 ILE c 196 TYR c 206
SITE 3 AH3 13 GLY c 210 THR k 114 LEU k 115 PHE k 116
SITE 4 AH3 13 ASN k 122
SITE 1 AH4 4 CYS d 111 HIS d 119 CYS d 134 CYS d 137
SITE 1 AH5 5 LEU a 334 TRP a 415 PEF a 607 SER e 92
SITE 2 AH5 5 ILE e 95
SITE 1 AH6 8 TYR a 452 PEF a 607 ALA e 111 ARG e 114
SITE 2 AH6 8 MET e 115 GLY e 117 GLY e 118 ASP e 120
SITE 1 AH7 8 PHE a 19 ILE a 400 PHE h 40 LYS h 41
SITE 2 AH7 8 ARG h 45 TYR h 49 SER h 52 PHE h 56
SITE 1 AH8 3 HIS m 241 HIS m 290 HIS m 291
SITE 1 AH9 24 PHE m 19 SER m 33 ARG m 37 VAL m 59
SITE 2 AH9 24 HIS m 62 ALA m 63 MET m 66 ILE m 67
SITE 3 AH9 24 VAL m 71 GLY m 126 TRP m 127 TYR m 371
SITE 4 AH9 24 PHE m 377 HIS m 378 LEU m 381 ILE m 386
SITE 5 AH9 24 LEU m 389 PHE m 390 ILE m 424 PHE m 425
SITE 6 AH9 24 MET m 428 ARG m 438 ARG m 439 LEU m 465
SITE 1 AI1 24 TRP m 127 THR m 128 TRP m 237 VAL m 244
SITE 2 AI1 24 TYR m 245 HIS m 290 HIS m 291 THR m 309
SITE 3 AI1 24 ALA m 313 THR m 316 GLY m 317 GLY m 352
SITE 4 AI1 24 GLY m 355 VAL m 356 LEU m 358 ALA m 359
SITE 5 AI1 24 ASP m 364 HIS m 368 HIS m 376 PHE m 377
SITE 6 AI1 24 VAL m 380 LEU m 381 ARG m 438 ILE n 50
SITE 1 AI2 4 GLU m 39 ALA m 42 GLY m 44 PRO m 441
SITE 1 AI3 3 HIS m 368 ASP m 369 GLU n 223
SITE 1 AI4 8 PHE m 268 ALA m 325 ILE n 75 ILE n 81
SITE 2 AI4 8 PHE n 88 LYS u 11 VAL u 14 PHE u 22
SITE 1 AI5 12 PHE m 95 ARG m 97 ILE m 98 HIS o 15
SITE 2 AI5 12 SER o 62 TRP o 65 PHE o 66 HIS o 79
SITE 3 AI5 12 GLY o 90 PHE o 91 PHE o 94 PEF o 301
SITE 1 AI6 5 HIS n 186 CYS n 221 CYS n 225 MET n 232
SITE 2 AI6 5 CUA n 302
SITE 1 AI7 5 CYS n 221 GLU n 223 CYS n 225 HIS n 229
SITE 2 AI7 5 CUA n 301
SITE 1 AI8 10 PHE m 430 TRP m 450 PRO n 20 TYR n 21
SITE 2 AI8 10 CYS n 23 SER q 148 PHE u 36 PRO x 54
SITE 3 AI8 10 GLY x 55 TYR x 58
SITE 1 AI9 7 VAL m 453 ILE m 456 TYR n 21 PEF q 201
SITE 2 AI9 7 PCF q 202 VAL x 57 PHE x 60
SITE 1 AJ1 14 PEF m 607 PHE o 66 ILE o 69 VAL o 70
SITE 2 AJ1 14 ALA o 73 THR o 74 ILE o 87 MET o 222
SITE 3 AJ1 14 ARG o 229 HIS o 234 HIS o 239 HIS o 240
SITE 4 AJ1 14 VAL o 241 GLY o 242
SITE 1 AJ2 13 THR m 208 PHE m 216 TYR o 189 ALA o 192
SITE 2 AJ2 13 PHE o 194 THR o 195 ILE o 196 TYR o 206
SITE 3 AJ2 13 GLY o 210 THR w 114 LEU w 115 PHE w 116
SITE 4 AJ2 13 ASN w 122
SITE 1 AJ3 4 CYS p 111 HIS p 119 CYS p 134 CYS p 137
SITE 1 AJ4 5 TRP m 415 PHE m 418 PEF n 304 SER q 92
SITE 2 AJ4 5 ILE q 95
SITE 1 AJ5 7 TYR m 452 ILE m 456 PEF n 304 ARG q 114
SITE 2 AJ5 7 MET q 115 GLY q 118 ASP q 120
SITE 1 AJ6 8 PHE m 19 ILE m 400 PHE t 40 LYS t 41
SITE 2 AJ6 8 ARG t 45 TYR t 49 SER t 52 PHE t 56
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
