HEADER TRANSFERASE/STRUCTURAL PROTEIN/DNA 26-SEP-19 6UGM
TITLE STRUCTURAL BASIS OF COMPASS ECM RECOGNITION OF AN UNMODIFIED
TITLE 2 NUCLEOSOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A;
COMPND 11 CHAIN: C, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H2B;
COMPND 15 CHAIN: D;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: HISTONE H2B 1.1;
COMPND 19 CHAIN: H;
COMPND 20 SYNONYM: H2B1.1;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: DNA (146-MER);
COMPND 24 CHAIN: I;
COMPND 25 ENGINEERED: YES;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: DNA (146-MER);
COMPND 28 CHAIN: J;
COMPND 29 ENGINEERED: YES;
COMPND 30 MOL_ID: 8;
COMPND 31 MOLECULE: SWD3;
COMPND 32 CHAIN: K;
COMPND 33 ENGINEERED: YES;
COMPND 34 MOL_ID: 9;
COMPND 35 MOLECULE: HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-4 SPECIFIC;
COMPND 36 CHAIN: M;
COMPND 37 SYNONYM: COMPASS COMPONENT SET1,SET DOMAIN-CONTAINING PROTEIN 1;
COMPND 38 EC: 2.1.1.43;
COMPND 39 ENGINEERED: YES;
COMPND 40 MOL_ID: 10;
COMPND 41 MOLECULE: SWD1;
COMPND 42 CHAIN: N;
COMPND 43 ENGINEERED: YES;
COMPND 44 MOL_ID: 11;
COMPND 45 MOLECULE: H3 N-TERMINUS;
COMPND 46 CHAIN: R;
COMPND 47 ENGINEERED: YES;
COMPND 48 MOL_ID: 12;
COMPND 49 MOLECULE: SPP1;
COMPND 50 CHAIN: X;
COMPND 51 ENGINEERED: YES;
COMPND 52 MOL_ID: 13;
COMPND 53 MOLECULE: BRE2;
COMPND 54 CHAIN: L;
COMPND 55 ENGINEERED: YES;
COMPND 56 MOL_ID: 14;
COMPND 57 MOLECULE: SDC1;
COMPND 58 CHAIN: O, P;
COMPND 59 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: HIST1H3G, H3L;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 10 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 11 ORGANISM_TAXID: 8355;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 16 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 17 ORGANISM_TAXID: 8355;
SOURCE 18 GENE: HIST1H2AJ, LOC494591, XELAEV_18003602MG;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 21 MOL_ID: 4;
SOURCE 22 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 23 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 24 ORGANISM_TAXID: 8355;
SOURCE 25 GENE: XELAEV_18032686MG;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 MOL_ID: 5;
SOURCE 29 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 30 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 31 ORGANISM_TAXID: 8355;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 34 MOL_ID: 6;
SOURCE 35 SYNTHETIC: YES;
SOURCE 36 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 37 ORGANISM_TAXID: 32630;
SOURCE 38 MOL_ID: 7;
SOURCE 39 SYNTHETIC: YES;
SOURCE 40 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 41 ORGANISM_TAXID: 32630;
SOURCE 42 MOL_ID: 8;
SOURCE 43 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 44 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 45 ORGANISM_COMMON: YEAST;
SOURCE 46 ORGANISM_TAXID: 284590;
SOURCE 47 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 48 WM37;
SOURCE 49 GENE: KLLA0_E24487G;
SOURCE 50 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 51 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 52 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 53 MOL_ID: 9;
SOURCE 54 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 55 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 56 ORGANISM_COMMON: YEAST;
SOURCE 57 ORGANISM_TAXID: 284590;
SOURCE 58 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 59 WM37;
SOURCE 60 GENE: SET1, KLLA0F24134G;
SOURCE 61 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 62 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 63 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 64 MOL_ID: 10;
SOURCE 65 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 66 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 67 ORGANISM_COMMON: YEAST;
SOURCE 68 ORGANISM_TAXID: 284590;
SOURCE 69 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 70 WM37;
SOURCE 71 GENE: KLLA0_A08800G;
SOURCE 72 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 73 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 74 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 75 MOL_ID: 11;
SOURCE 76 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 77 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 78 ORGANISM_TAXID: 8355;
SOURCE 79 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 80 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 81 MOL_ID: 12;
SOURCE 82 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 83 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 84 ORGANISM_COMMON: YEAST;
SOURCE 85 ORGANISM_TAXID: 284590;
SOURCE 86 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 87 WM37;
SOURCE 88 GENE: KLLA0_D07260G;
SOURCE 89 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 90 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 91 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 92 MOL_ID: 13;
SOURCE 93 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 94 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 95 ORGANISM_COMMON: YEAST;
SOURCE 96 ORGANISM_TAXID: 284590;
SOURCE 97 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 98 WM37;
SOURCE 99 GENE: KLLA0_C10945G;
SOURCE 100 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 101 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 102 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 103 MOL_ID: 14;
SOURCE 104 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS (STRAIN ATCC 8585 / CBS
SOURCE 105 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37);
SOURCE 106 ORGANISM_COMMON: YEAST;
SOURCE 107 ORGANISM_TAXID: 284590;
SOURCE 108 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 109 WM37;
SOURCE 110 GENE: KLLA0_E03521G;
SOURCE 111 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 112 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 113 EXPRESSION_SYSTEM_TAXID: 7111
KEYWDS COMPLEX, METHYLTRANSFERASE, EPIGENETICS, CHROMATIN, NUCLEOSOME,
KEYWDS 2 TRANSFERASE-STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR P.L.HSU,H.SHI,N.ZHENG
REVDAT 4 20-MAR-24 6UGM 1 REMARK
REVDAT 3 18-DEC-19 6UGM 1 JRNL
REVDAT 2 27-NOV-19 6UGM 1 JRNL
REVDAT 1 20-NOV-19 6UGM 0
JRNL AUTH P.L.HSU,H.SHI,C.LEONEN,J.KANG,C.CHATTERJEE,N.ZHENG
JRNL TITL STRUCTURAL BASIS OF H2B UBIQUITINATION-DEPENDENT H3K4
JRNL TITL 2 METHYLATION BY COMPASS.
JRNL REF MOL.CELL V. 76 712 2019
JRNL REFN ISSN 1097-2765
JRNL PMID 31733991
JRNL DOI 10.1016/J.MOLCEL.2019.10.013
REMARK 2
REMARK 2 RESOLUTION. 3.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.700
REMARK 3 NUMBER OF PARTICLES : 100905
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6UGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1000243234.
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 : YEAST COMPASS ECM BOUND TO AN
REMARK 245 UNMODIFIED NUCLEOSOME;
REMARK 245 NUCLEOSOME; COMPASS ECM
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 7400.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, M, N, R, X, L, O, P
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 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 LYS A 37
REMARK 465 ALA A 135
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 GLY B 102
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 THR D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
REMARK 465 ARG D 27
REMARK 465 LYS D 28
REMARK 465 LYS D 122
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 PRO E 38
REMARK 465 ALA E 135
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 LYS F 16
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 THR H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 ARG H 26
REMARK 465 ARG H 27
REMARK 465 LYS H 28
REMARK 465 LYS H 122
REMARK 465 DC I 1
REMARK 465 MET K 1
REMARK 465 CYS K 2
REMARK 465 ASP K 3
REMARK 465 LEU K 4
REMARK 465 ASP K 5
REMARK 465 SER K 6
REMARK 465 VAL K 7
REMARK 465 SER K 8
REMARK 465 ASP K 9
REMARK 465 LEU K 10
REMARK 465 THR K 11
REMARK 465 LEU K 12
REMARK 465 THR K 13
REMARK 465 LEU K 14
REMARK 465 ARG K 15
REMARK 465 HIS K 245
REMARK 465 GLN K 246
REMARK 465 GLU K 247
REMARK 465 THR K 248
REMARK 465 LYS K 249
REMARK 465 ALA K 250
REMARK 465 HIS K 327
REMARK 465 TYR M 774
REMARK 465 LEU M 775
REMARK 465 LEU M 776
REMARK 465 HIS M 777
REMARK 465 HIS M 778
REMARK 465 ARG M 779
REMARK 465 ARG M 780
REMARK 465 LEU M 781
REMARK 465 ALA M 782
REMARK 465 GLN M 783
REMARK 465 PRO M 784
REMARK 465 LEU M 785
REMARK 465 ASN M 786
REMARK 465 THR M 787
REMARK 465 VAL M 788
REMARK 465 HIS M 789
REMARK 465 ASN M 790
REMARK 465 HIS M 791
REMARK 465 GLN M 792
REMARK 465 GLU M 793
REMARK 465 GLN M 794
REMARK 465 ASN M 795
REMARK 465 PHE M 796
REMARK 465 MET M 797
REMARK 465 ALA M 798
REMARK 465 LEU M 799
REMARK 465 ASN M 800
REMARK 465 GLY M 801
REMARK 465 THR M 802
REMARK 465 GLU M 803
REMARK 465 SER M 804
REMARK 465 THR M 805
REMARK 465 ASN M 806
REMARK 465 GLN M 807
REMARK 465 GLU M 808
REMARK 465 ALA M 809
REMARK 465 ASP M 810
REMARK 465 LEU M 811
REMARK 465 GLU M 812
REMARK 465 GLN M 813
REMARK 465 ASP M 814
REMARK 465 ASN M 815
REMARK 465 HIS M 816
REMARK 465 ASN M 817
REMARK 465 ALA M 818
REMARK 465 SER M 819
REMARK 465 SER M 820
REMARK 465 ARG M 821
REMARK 465 LEU M 822
REMARK 465 ASN M 823
REMARK 465 ARG M 824
REMARK 465 VAL M 825
REMARK 465 PHE M 826
REMARK 465 GLN M 827
REMARK 465 ARG M 828
REMARK 465 ARG M 829
REMARK 465 PHE M 830
REMARK 465 GLN M 831
REMARK 465 GLN M 832
REMARK 465 ASP M 833
REMARK 465 ILE M 834
REMARK 465 GLU M 835
REMARK 465 ALA M 836
REMARK 465 GLN M 837
REMARK 465 ARG M 838
REMARK 465 ALA M 839
REMARK 465 ALA M 840
REMARK 465 ILE M 841
REMARK 465 GLY M 842
REMARK 465 PHE M 843
REMARK 465 GLU M 844
REMARK 465 SER M 845
REMARK 465 ASP M 846
REMARK 465 LEU M 847
REMARK 465 LEU M 848
REMARK 465 SER M 849
REMARK 465 LEU M 850
REMARK 465 GLU M 977
REMARK 465 ARG M 978
REMARK 465 GLU M 979
REMARK 465 THR M 980
REMARK 465 ASP M 981
REMARK 465 GLU M 982
REMARK 465 GLY M 983
REMARK 465 GLU M 984
REMARK 465 ARG M 985
REMARK 465 LEU M 986
REMARK 465 MET N 1
REMARK 465 GLU N 199
REMARK 465 SER N 200
REMARK 465 GLY N 201
REMARK 465 PHE N 202
REMARK 465 ASP N 249
REMARK 465 ASN N 250
REMARK 465 GLU N 251
REMARK 465 SER N 252
REMARK 465 GLU N 253
REMARK 465 GLY N 254
REMARK 465 GLY N 255
REMARK 465 SER N 256
REMARK 465 SER N 257
REMARK 465 MET N 382
REMARK 465 ASP N 383
REMARK 465 ASP N 384
REMARK 465 ASP N 385
REMARK 465 ASN N 386
REMARK 465 ASN N 387
REMARK 465 LEU N 388
REMARK 465 GLN N 389
REMARK 465 ALA N 390
REMARK 465 MET N 391
REMARK 465 THR N 392
REMARK 465 GLU N 393
REMARK 465 ALA N 394
REMARK 465 HIS N 436
REMARK 465 GLN N 437
REMARK 465 GLU N 438
REMARK 465 GLN N 439
REMARK 465 MET X 1
REMARK 465 SER X 2
REMARK 465 LEU X 3
REMARK 465 PRO X 4
REMARK 465 SER X 5
REMARK 465 TRP X 6
REMARK 465 CYS X 7
REMARK 465 PRO X 8
REMARK 465 ARG X 9
REMARK 465 TYR X 10
REMARK 465 ASP X 11
REMARK 465 SER X 12
REMARK 465 ARG X 13
REMARK 465 LYS X 14
REMARK 465 HIS X 15
REMARK 465 ASP X 16
REMARK 465 PRO X 17
REMARK 465 LYS X 18
REMARK 465 THR X 19
REMARK 465 GLY X 20
REMARK 465 GLU X 21
REMARK 465 GLU X 22
REMARK 465 VAL X 23
REMARK 465 TYR X 24
REMARK 465 CYS X 25
REMARK 465 ILE X 26
REMARK 465 CYS X 27
REMARK 465 LYS X 28
REMARK 465 LYS X 29
REMARK 465 PRO X 30
REMARK 465 ASP X 31
REMARK 465 THR X 32
REMARK 465 GLY X 33
REMARK 465 GLU X 34
REMARK 465 LEU X 35
REMARK 465 MET X 36
REMARK 465 VAL X 37
REMARK 465 GLY X 38
REMARK 465 CYS X 39
REMARK 465 ASP X 40
REMARK 465 GLY X 41
REMARK 465 CYS X 42
REMARK 465 ASP X 43
REMARK 465 ASP X 44
REMARK 465 TRP X 45
REMARK 465 PHE X 46
REMARK 465 HIS X 47
REMARK 465 PHE X 48
REMARK 465 SER X 49
REMARK 465 CYS X 50
REMARK 465 LEU X 51
REMARK 465 LYS X 52
REMARK 465 ILE X 53
REMARK 465 PRO X 54
REMARK 465 GLU X 55
REMARK 465 LYS X 56
REMARK 465 TYR X 57
REMARK 465 ARG X 58
REMARK 465 ASP X 59
REMARK 465 LEU X 60
REMARK 465 VAL X 61
REMARK 465 PHE X 62
REMARK 465 SER X 63
REMARK 465 PHE X 64
REMARK 465 TYR X 65
REMARK 465 CYS X 66
REMARK 465 SER X 67
REMARK 465 TYR X 68
REMARK 465 CYS X 69
REMARK 465 SER X 70
REMARK 465 ALA X 71
REMARK 465 GLY X 72
REMARK 465 ILE X 73
REMARK 465 THR X 74
REMARK 465 GLY X 75
REMARK 465 PRO X 76
REMARK 465 ALA X 77
REMARK 465 LEU X 78
REMARK 465 ILE X 79
REMARK 465 ASN X 80
REMARK 465 GLY X 81
REMARK 465 GLY X 82
REMARK 465 LYS X 83
REMARK 465 LEU X 84
REMARK 465 PRO X 85
REMARK 465 LYS X 86
REMARK 465 THR X 87
REMARK 465 LEU X 88
REMARK 465 TRP X 89
REMARK 465 LYS X 90
REMARK 465 ARG X 91
REMARK 465 LYS X 92
REMARK 465 CYS X 93
REMARK 465 ARG X 94
REMARK 465 LEU X 95
REMARK 465 PRO X 96
REMARK 465 GLU X 97
REMARK 465 CYS X 98
REMARK 465 TYR X 99
REMARK 465 THR X 100
REMARK 465 GLU X 101
REMARK 465 CYS X 102
REMARK 465 ASP X 103
REMARK 465 ALA X 104
REMARK 465 ASN X 105
REMARK 465 SER X 106
REMARK 465 ARG X 107
REMARK 465 SER X 108
REMARK 465 LYS X 109
REMARK 465 TYR X 110
REMARK 465 CYS X 111
REMARK 465 SER X 112
REMARK 465 LYS X 113
REMARK 465 LYS X 114
REMARK 465 HIS X 115
REMARK 465 ALA X 116
REMARK 465 VAL X 117
REMARK 465 GLN X 118
REMARK 465 TYR X 119
REMARK 465 VAL X 120
REMARK 465 GLN X 121
REMARK 465 SER X 122
REMARK 465 ILE X 123
REMARK 465 VAL X 124
REMARK 465 ASP X 125
REMARK 465 LYS X 126
REMARK 465 LEU X 127
REMARK 465 ASN X 128
REMARK 465 LEU X 129
REMARK 465 PRO X 130
REMARK 465 GLY X 131
REMARK 465 VAL X 132
REMARK 465 ASP X 133
REMARK 465 LYS X 134
REMARK 465 ILE X 135
REMARK 465 ALA X 136
REMARK 465 LEU X 137
REMARK 465 LEU X 138
REMARK 465 ARG X 139
REMARK 465 GLN X 140
REMARK 465 LEU X 141
REMARK 465 LEU X 142
REMARK 465 ASN X 143
REMARK 465 GLU X 144
REMARK 465 THR X 145
REMARK 465 THR X 146
REMARK 465 SER X 147
REMARK 465 LEU X 148
REMARK 465 GLU X 149
REMARK 465 GLU X 150
REMARK 465 PHE X 151
REMARK 465 LYS X 152
REMARK 465 THR X 153
REMARK 465 LEU X 154
REMARK 465 GLY X 155
REMARK 465 ARG X 156
REMARK 465 ASP X 157
REMARK 465 LYS X 158
REMARK 465 LEU X 159
REMARK 465 PRO X 160
REMARK 465 GLU X 161
REMARK 465 VAL X 162
REMARK 465 THR X 163
REMARK 465 SER X 164
REMARK 465 PRO X 165
REMARK 465 LEU X 166
REMARK 465 SER X 167
REMARK 465 LYS X 168
REMARK 465 ASP X 169
REMARK 465 GLN X 170
REMARK 465 TYR X 171
REMARK 465 SER X 172
REMARK 465 LYS X 173
REMARK 465 LEU X 174
REMARK 465 LEU X 175
REMARK 465 GLU X 176
REMARK 465 ASN X 177
REMARK 465 ASP X 178
REMARK 465 GLN X 179
REMARK 465 HIS X 180
REMARK 465 LEU X 181
REMARK 465 ASN X 182
REMARK 465 LYS X 183
REMARK 465 LEU X 184
REMARK 465 ILE X 185
REMARK 465 ASN X 186
REMARK 465 GLU X 187
REMARK 465 HIS X 188
REMARK 465 ASP X 189
REMARK 465 GLU X 190
REMARK 465 LEU X 191
REMARK 465 VAL X 192
REMARK 465 SER X 193
REMARK 465 VAL X 194
REMARK 465 ARG X 230
REMARK 465 LYS X 231
REMARK 465 LYS X 232
REMARK 465 SER X 233
REMARK 465 LYS X 234
REMARK 465 SER X 235
REMARK 465 ALA X 236
REMARK 465 SER X 237
REMARK 465 LYS X 238
REMARK 465 VAL X 239
REMARK 465 THR X 240
REMARK 465 ILE X 241
REMARK 465 CYS X 242
REMARK 465 GLY X 243
REMARK 465 TYR X 244
REMARK 465 HIS X 245
REMARK 465 ASN X 246
REMARK 465 GLU X 247
REMARK 465 PHE X 248
REMARK 465 THR X 249
REMARK 465 ILE X 250
REMARK 465 PRO X 251
REMARK 465 ARG X 252
REMARK 465 SER X 253
REMARK 465 VAL X 254
REMARK 465 GLU X 255
REMARK 465 GLU X 256
REMARK 465 PHE X 257
REMARK 465 LEU X 258
REMARK 465 ASP X 259
REMARK 465 LYS X 260
REMARK 465 LEU X 261
REMARK 465 LEU X 262
REMARK 465 GLN X 263
REMARK 465 LEU X 264
REMARK 465 LYS X 265
REMARK 465 GLU X 266
REMARK 465 ASP X 267
REMARK 465 GLU X 268
REMARK 465 ASN X 269
REMARK 465 SER X 270
REMARK 465 ASN X 271
REMARK 465 ILE X 272
REMARK 465 THR X 273
REMARK 465 SER X 274
REMARK 465 VAL X 275
REMARK 465 ASP X 276
REMARK 465 GLY X 277
REMARK 465 VAL X 278
REMARK 465 CYS X 279
REMARK 465 VAL X 280
REMARK 465 LYS X 281
REMARK 465 THR X 282
REMARK 465 LYS X 283
REMARK 465 CYS X 284
REMARK 465 ALA X 285
REMARK 465 LYS X 286
REMARK 465 HIS X 287
REMARK 465 GLN X 288
REMARK 465 ASP X 289
REMARK 465 PHE X 328
REMARK 465 GLU X 329
REMARK 465 GLN X 330
REMARK 465 GLU X 331
REMARK 465 MET X 332
REMARK 465 SER X 333
REMARK 465 ASN X 334
REMARK 465 ARG X 335
REMARK 465 VAL X 336
REMARK 465 LEU X 337
REMARK 465 PRO X 338
REMARK 465 GLY X 339
REMARK 465 VAL X 340
REMARK 465 LYS X 341
REMARK 465 THR X 342
REMARK 465 MET L 1
REMARK 465 ASP L 216
REMARK 465 ASP L 217
REMARK 465 SER L 218
REMARK 465 ARG L 219
REMARK 465 THR L 220
REMARK 465 ASN L 221
REMARK 465 LYS L 222
REMARK 465 ARG L 223
REMARK 465 ASN L 224
REMARK 465 LYS L 225
REMARK 465 TRP L 327
REMARK 465 ASN L 328
REMARK 465 LYS L 329
REMARK 465 ARG L 330
REMARK 465 ASN L 331
REMARK 465 VAL L 332
REMARK 465 THR L 333
REMARK 465 LYS L 334
REMARK 465 GLY L 335
REMARK 465 ILE L 336
REMARK 465 ASP L 404
REMARK 465 THR L 405
REMARK 465 MET O 1
REMARK 465 SER O 2
REMARK 465 GLU O 3
REMARK 465 PRO O 4
REMARK 465 VAL O 5
REMARK 465 MET O 6
REMARK 465 GLU O 7
REMARK 465 ASN O 8
REMARK 465 MET O 9
REMARK 465 ALA O 10
REMARK 465 PRO O 11
REMARK 465 GLU O 12
REMARK 465 ASP O 13
REMARK 465 VAL O 14
REMARK 465 VAL O 15
REMARK 465 LYS O 16
REMARK 465 LEU O 17
REMARK 465 GLU O 18
REMARK 465 LYS O 19
REMARK 465 GLU O 20
REMARK 465 GLU O 21
REMARK 465 HIS O 22
REMARK 465 ILE O 23
REMARK 465 VAL O 24
REMARK 465 PRO O 25
REMARK 465 ASP O 26
REMARK 465 ILE O 27
REMARK 465 GLY O 28
REMARK 465 VAL O 29
REMARK 465 SER O 30
REMARK 465 SER O 31
REMARK 465 ILE O 32
REMARK 465 SER O 33
REMARK 465 THR O 34
REMARK 465 THR O 35
REMARK 465 GLU O 36
REMARK 465 PRO O 37
REMARK 465 LEU O 38
REMARK 465 SER O 39
REMARK 465 PRO O 40
REMARK 465 SER O 41
REMARK 465 GLY O 42
REMARK 465 ILE O 43
REMARK 465 PRO O 44
REMARK 465 ARG O 45
REMARK 465 GLU O 46
REMARK 465 SER O 47
REMARK 465 SER O 48
REMARK 465 GLY O 49
REMARK 465 THR O 50
REMARK 465 VAL O 51
REMARK 465 THR O 52
REMARK 465 SER O 53
REMARK 465 ALA O 54
REMARK 465 THR O 55
REMARK 465 ALA O 56
REMARK 465 ALA O 57
REMARK 465 THR O 58
REMARK 465 THR O 59
REMARK 465 GLU O 60
REMARK 465 ARG O 61
REMARK 465 GLU O 62
REMARK 465 VAL O 63
REMARK 465 SER O 64
REMARK 465 PRO O 65
REMARK 465 LYS O 66
REMARK 465 LYS O 67
REMARK 465 GLU O 68
REMARK 465 LEU O 69
REMARK 465 GLN O 70
REMARK 465 ILE O 71
REMARK 465 ASP O 72
REMARK 465 HIS O 73
REMARK 465 ASP O 74
REMARK 465 ARG O 75
REMARK 465 VAL O 76
REMARK 465 ASP O 77
REMARK 465 PRO O 78
REMARK 465 VAL O 79
REMARK 465 ALA O 80
REMARK 465 MET O 81
REMARK 465 ILE O 82
REMARK 465 GLY O 83
REMARK 465 GLY O 84
REMARK 465 GLU O 127
REMARK 465 MET O 128
REMARK 465 ASN O 129
REMARK 465 GLN O 130
REMARK 465 LYS O 131
REMARK 465 PRO O 132
REMARK 465 SER O 133
REMARK 465 SER O 134
REMARK 465 MET P 1
REMARK 465 SER P 2
REMARK 465 GLU P 3
REMARK 465 PRO P 4
REMARK 465 VAL P 5
REMARK 465 MET P 6
REMARK 465 GLU P 7
REMARK 465 ASN P 8
REMARK 465 MET P 9
REMARK 465 ALA P 10
REMARK 465 PRO P 11
REMARK 465 GLU P 12
REMARK 465 ASP P 13
REMARK 465 VAL P 14
REMARK 465 VAL P 15
REMARK 465 LYS P 16
REMARK 465 LEU P 17
REMARK 465 GLU P 18
REMARK 465 LYS P 19
REMARK 465 GLU P 20
REMARK 465 GLU P 21
REMARK 465 HIS P 22
REMARK 465 ILE P 23
REMARK 465 VAL P 24
REMARK 465 PRO P 25
REMARK 465 ASP P 26
REMARK 465 ILE P 27
REMARK 465 GLY P 28
REMARK 465 VAL P 29
REMARK 465 SER P 30
REMARK 465 SER P 31
REMARK 465 ILE P 32
REMARK 465 SER P 33
REMARK 465 THR P 34
REMARK 465 THR P 35
REMARK 465 GLU P 36
REMARK 465 PRO P 37
REMARK 465 LEU P 38
REMARK 465 SER P 39
REMARK 465 PRO P 40
REMARK 465 SER P 41
REMARK 465 GLY P 42
REMARK 465 ILE P 43
REMARK 465 PRO P 44
REMARK 465 ARG P 45
REMARK 465 GLU P 46
REMARK 465 SER P 47
REMARK 465 SER P 48
REMARK 465 GLY P 49
REMARK 465 THR P 50
REMARK 465 VAL P 51
REMARK 465 THR P 52
REMARK 465 SER P 53
REMARK 465 ALA P 54
REMARK 465 THR P 55
REMARK 465 ALA P 56
REMARK 465 ALA P 57
REMARK 465 THR P 58
REMARK 465 THR P 59
REMARK 465 GLU P 60
REMARK 465 ARG P 61
REMARK 465 GLU P 62
REMARK 465 VAL P 63
REMARK 465 SER P 64
REMARK 465 PRO P 65
REMARK 465 LYS P 66
REMARK 465 LYS P 67
REMARK 465 GLU P 68
REMARK 465 LEU P 69
REMARK 465 GLN P 70
REMARK 465 ILE P 71
REMARK 465 ASP P 72
REMARK 465 HIS P 73
REMARK 465 ASP P 74
REMARK 465 ARG P 75
REMARK 465 VAL P 76
REMARK 465 ASP P 77
REMARK 465 ALA P 107
REMARK 465 ARG P 108
REMARK 465 GLU P 109
REMARK 465 LYS P 110
REMARK 465 PRO P 111
REMARK 465 GLU P 112
REMARK 465 GLU P 127
REMARK 465 MET P 128
REMARK 465 ASN P 129
REMARK 465 GLN P 130
REMARK 465 LYS P 131
REMARK 465 PRO P 132
REMARK 465 SER P 133
REMARK 465 SER P 134
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 CYS A 110 SG
REMARK 470 MET K 16 CG SD CE
REMARK 470 GLU K 200 CG CD OE1 OE2
REMARK 470 ASP N 197 CG OD1 OD2
REMARK 470 LYS L 226 CG CD CE NZ
REMARK 470 ARG P 116 CG CD NE CZ NH1 NH2
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 SG CYS K 256 O LEU K 302 2.09
REMARK 500 OE2 GLU M 940 O SER M 994 2.15
REMARK 500 NH2 ARG E 42 OP2 DC I 144 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DC I 111 O3' DC I 111 C3' -0.042
REMARK 500 DG J 82 O3' DG J 82 C3' -0.038
REMARK 500 DG J 101 O3' DG J 101 C3' -0.040
REMARK 500 PRO O 114 CD PRO O 114 N 0.086
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 TYR E 41 CB - CA - C ANGL. DEV. = -27.1 DEGREES
REMARK 500 DT I 2 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG I 33 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT I 46 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA I 97 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT I 112 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT I 127 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA I 135 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC J 20 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC J 34 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J 86 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT J 107 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT J 109 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 LEU K 302 CB - CA - C ANGL. DEV. = -16.9 DEGREES
REMARK 500 LEU K 302 N - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 LEU N 20 CB - CA - C ANGL. DEV. = -20.7 DEGREES
REMARK 500 LEU N 20 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 THR N 21 CB - CA - C ANGL. DEV. = -20.6 DEGREES
REMARK 500 THR N 21 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 LEU N 88 CB - CA - C ANGL. DEV. = 16.0 DEGREES
REMARK 500 GLU N 212 CB - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 LYS N 213 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP N 413 N - CA - C ANGL. DEV. = -19.6 DEGREES
REMARK 500 ILE N 414 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 ASP L 83 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 PHE L 309 N - CA - CB ANGL. DEV. = -15.8 DEGREES
REMARK 500 PHE L 309 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 LEU L 310 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 PHE L 322 CB - CA - C ANGL. DEV. = 13.5 DEGREES
REMARK 500 LYS L 376 CB - CA - C ANGL. DEV. = 21.4 DEGREES
REMARK 500 LYS L 376 N - CA - C ANGL. DEV. = -30.9 DEGREES
REMARK 500 PRO O 114 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR C 16 77.47 58.54
REMARK 500 LYS C 36 33.32 -92.28
REMARK 500 LEU C 97 57.45 -94.89
REMARK 500 HIS D 46 74.07 -155.06
REMARK 500 THR G 16 77.57 54.71
REMARK 500 LYS G 36 33.33 -92.25
REMARK 500 LYS G 74 7.82 88.77
REMARK 500 LEU G 97 57.40 -105.14
REMARK 500 HIS H 79 -31.38 -130.37
REMARK 500 ASP K 20 -61.12 -103.70
REMARK 500 ASP K 90 32.70 -95.47
REMARK 500 ILE K 103 -63.24 -100.53
REMARK 500 ASP K 131 37.41 -97.85
REMARK 500 SER K 165 34.54 -97.06
REMARK 500 TRP K 197 -9.86 82.25
REMARK 500 ALA K 199 18.12 54.12
REMARK 500 ASP K 201 26.54 82.57
REMARK 500 PRO M 767 22.89 -79.91
REMARK 500 ILE M 917 -67.64 -95.44
REMARK 500 ALA M 925 27.86 -143.66
REMARK 500 ASN M 967 18.69 59.05
REMARK 500 LYS M 975 62.42 60.34
REMARK 500 MET N 56 57.33 -94.08
REMARK 500 GLN N 77 -61.02 -93.80
REMARK 500 VAL N 124 -62.68 -103.68
REMARK 500 GLU N 212 -173.32 -177.77
REMARK 500 SER N 298 -1.47 71.03
REMARK 500 LEU N 324 -63.28 -93.32
REMARK 500 SER N 415 21.39 80.85
REMARK 500 SER X 197 0.11 -66.69
REMARK 500 LEU X 293 70.46 59.14
REMARK 500 SER X 294 30.32 -92.76
REMARK 500 LEU L 9 -169.66 -117.84
REMARK 500 SER L 31 -61.61 -101.59
REMARK 500 THR L 366 -61.09 -96.07
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 THR A 45 VAL A 46 146.70
REMARK 500 PHE L 309 LEU L 310 -147.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL K 113 11.01
REMARK 500 PRO L 308 10.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAM M 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN M 1102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-20765 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-20767 RELATED DB: EMDB
DBREF 6UGM A 1 135 UNP Q92133 Q92133_XENLA 2 136
DBREF 6UGM B 1 102 UNP P62799 H4_XENLA 2 103
DBREF 6UGM C 12 118 UNP Q6AZJ8 Q6AZJ8_XENLA 13 119
DBREF1 6UGM D -2 122 UNP A0A1L8FQ56_XENLA
DBREF2 6UGM D A0A1L8FQ56 2 126
DBREF 6UGM E 1 135 UNP Q92133 Q92133_XENLA 2 136
DBREF 6UGM F 1 102 UNP P62799 H4_XENLA 2 103
DBREF 6UGM G 12 118 UNP Q6AZJ8 Q6AZJ8_XENLA 13 119
DBREF 6UGM H -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 6UGM I 1 147 PDB 6UGM 6UGM 1 147
DBREF 6UGM J 1 146 PDB 6UGM 6UGM 1 146
DBREF 6UGM K 1 327 UNP Q6CLY5 Q6CLY5_KLULA 1 327
DBREF 6UGM M 726 1000 UNP Q6CIT4 SET1_KLULA 726 1000
DBREF 6UGM N 1 439 UNP Q6CXF3 Q6CXF3_KLULA 1 439
DBREF 6UGM R 3 5 PDB 6UGM 6UGM 3 5
DBREF 6UGM X 1 342 UNP Q6CRQ4 Q6CRQ4_KLULA 1 342
DBREF 6UGM L 1 405 UNP Q6CTQ1 Q6CTQ1_KLULA 1 405
DBREF 6UGM O 1 134 UNP Q6CPN6 Q6CPN6_KLULA 1 134
DBREF 6UGM P 1 134 UNP Q6CPN6 Q6CPN6_KLULA 1 134
SEQADV 6UGM PRO D 7 UNP A0A1L8FQ5 ALA 11 CONFLICT
SEQADV 6UGM GLU M 761 UNP Q6CIT4 ASP 761 CONFLICT
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS GLY ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 107 ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN
SEQRES 2 C 107 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY
SEQRES 3 C 107 ASN TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR
SEQRES 4 C 107 LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU
SEQRES 5 C 107 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 6 C 107 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN
SEQRES 7 C 107 ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE
SEQRES 8 C 107 ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU
SEQRES 9 C 107 LEU PRO LYS
SEQRES 1 D 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 D 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 D 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 D 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 D 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 D 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 D 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 D 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 D 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 D 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS GLY ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 107 ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN
SEQRES 2 G 107 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY
SEQRES 3 G 107 ASN TYR ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR
SEQRES 4 G 107 LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU
SEQRES 5 G 107 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 6 G 107 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN
SEQRES 7 G 107 ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE
SEQRES 8 G 107 ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU
SEQRES 9 G 107 LEU PRO LYS
SEQRES 1 H 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 H 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 H 125 LYS LYS ARG ARG LYS SER ARG LYS GLU SER TYR ALA ILE
SEQRES 4 H 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 H 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 H 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 H 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 H 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 H 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 H 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 147 DC DT DC DG DA DG DA DA DT DC DC DC DG
SEQRES 2 I 147 DG DT DG DC DC DG DA DG DG DC DC DG DC
SEQRES 3 I 147 DT DC DA DA DT DT DG DG DT DC DG DT DA
SEQRES 4 I 147 DG DA DC DA DG DC DT DC DT DA DG DC DA
SEQRES 5 I 147 DC DC DG DC DT DT DA DA DA DC DG DC DA
SEQRES 6 I 147 DC DG DT DA DC DG DC DG DC DT DG DT DC
SEQRES 7 I 147 DC DC DC DC DG DC DG DT DT DT DT DA DA
SEQRES 8 I 147 DC DC DG DC DC DA DA DG DG DG DG DA DT
SEQRES 9 I 147 DT DA DC DT DC DC DC DT DA DG DT DC DT
SEQRES 10 I 147 DC DC DA DG DG DC DA DC DG DT DG DT DC
SEQRES 11 I 147 DA DG DA DT DA DT DA DT DA DC DA DT DC
SEQRES 12 I 147 DC DG DA DT
SEQRES 1 J 146 DA DT DC DG DG DA DT DG DT DA DT DA DT
SEQRES 2 J 146 DA DT DC DT DG DA DC DA DC DG DT DG DC
SEQRES 3 J 146 DC DT DG DG DA DG DA DC DT DA DG DG DG
SEQRES 4 J 146 DA DG DT DA DA DT DC DC DC DC DT DT DG
SEQRES 5 J 146 DG DC DG DG DT DT DA DA DA DA DC DG DC
SEQRES 6 J 146 DG DG DG DG DG DA DC DA DG DC DG DC DG
SEQRES 7 J 146 DT DA DC DG DT DG DC DG DT DT DT DA DA
SEQRES 8 J 146 DG DC DG DG DT DG DC DT DA DG DA DG DC
SEQRES 9 J 146 DT DG DT DC DT DA DC DG DA DC DC DA DA
SEQRES 10 J 146 DT DT DG DA DG DC DG DG DC DC DT DC DG
SEQRES 11 J 146 DG DC DA DC DC DG DG DG DA DT DT DC DT
SEQRES 12 J 146 DC DG DA
SEQRES 1 K 327 MET CYS ASP LEU ASP SER VAL SER ASP LEU THR LEU THR
SEQRES 2 K 327 LEU ARG MET LEU GLN PHE ASP LYS GLN VAL LEU PRO ALA
SEQRES 3 K 327 SER GLY LYS ILE SER THR SER CYS GLN ILE SER PRO ASP
SEQRES 4 K 327 GLY GLU LEU ILE ALA ILE CYS GLN ASN THR ASP MET LEU
SEQRES 5 K 327 VAL TYR GLU ILE SER SER SER LYS MET MET LYS LEU THR
SEQRES 6 K 327 THR THR HIS LYS GLU CYS ILE ASN CYS LEU CYS TRP SER
SEQRES 7 K 327 PRO ASP SER LYS CYS ILE ALA SER GLY SER GLU ASP PHE
SEQRES 8 K 327 THR VAL GLU ILE THR HIS ILE ILE TYR GLY ARG ILE ARG
SEQRES 9 K 327 ARG LEU MET GLY HIS THR ALA PRO VAL ILE SER ILE CYS
SEQRES 10 K 327 TYR ASN ASN LYS GLY ASN ILE LEU CYS SER SER SER MET
SEQRES 11 K 327 ASP GLU SER ILE LYS GLU TRP HIS VAL LEU SER GLY THR
SEQRES 12 K 327 ALA LEU LYS THR MET SER ALA HIS SER ASP ALA VAL VAL
SEQRES 13 K 327 SER ILE ASP ILE PRO LYS PHE ASP SER SER ILE LEU SER
SEQRES 14 K 327 SER GLY SER TYR ASP GLY LEU ILE ARG ILE PHE ASP THR
SEQRES 15 K 327 GLU SER GLY HIS CYS LEU LYS THR LEU THR TYR ASP LYS
SEQRES 16 K 327 ASP TRP ILE ALA GLU ASP GLY VAL VAL PRO ILE SER THR
SEQRES 17 K 327 VAL LYS PHE SER ARG ASN GLY LYS PHE LEU LEU VAL LYS
SEQRES 18 K 327 SER LEU ASP ASN VAL VAL LYS LEU TRP GLU TYR THR ARG
SEQRES 19 K 327 GLY THR VAL VAL ARG THR PHE LEU TRP PRO HIS GLN GLU
SEQRES 20 K 327 THR LYS ALA LYS LEU LYS TYR ASN CYS GLY LEU GLU LEU
SEQRES 21 K 327 ILE TYR PRO GLN GLY LYS ASP PRO LEU VAL ILE SER GLY
SEQRES 22 K 327 ASN ASP SER GLY SER MET CYS VAL TRP ASN VAL TYR SER
SEQRES 23 K 327 LYS ASN LEU VAL GLN LYS ILE ASP GLU LYS HIS ARG ASN
SEQRES 24 K 327 SER PRO LEU ILE SER ILE SER ALA SER TYR ASP LYS VAL
SEQRES 25 K 327 ALA THR LEU SER LEU ASN GLY GLU CYS ASN LEU PHE ARG
SEQRES 26 K 327 VAL HIS
SEQRES 1 M 275 TYR GLN GLN ILE GLU GLN ASN GLY ILE ILE ARG ASP ASN
SEQRES 2 M 275 GLN ILE ALA LEU ASN GLU LYS GLU PHE ASP SER THR LEU
SEQRES 3 M 275 ALA SER THR THR GLY SER PHE ILE ALA GLU GLY PHE LYS
SEQRES 4 M 275 LYS ILE PRO ASP LYS LEU LYS SER SER TYR LEU LEU HIS
SEQRES 5 M 275 HIS ARG ARG LEU ALA GLN PRO LEU ASN THR VAL HIS ASN
SEQRES 6 M 275 HIS GLN GLU GLN ASN PHE MET ALA LEU ASN GLY THR GLU
SEQRES 7 M 275 SER THR ASN GLN GLU ALA ASP LEU GLU GLN ASP ASN HIS
SEQRES 8 M 275 ASN ALA SER SER ARG LEU ASN ARG VAL PHE GLN ARG ARG
SEQRES 9 M 275 PHE GLN GLN ASP ILE GLU ALA GLN ARG ALA ALA ILE GLY
SEQRES 10 M 275 PHE GLU SER ASP LEU LEU SER LEU ASN GLN LEU THR LYS
SEQRES 11 M 275 ARG LYS LYS PRO VAL THR PHE ALA ARG SER ALA ILE HIS
SEQRES 12 M 275 ASN TRP GLY LEU TYR ALA LEU GLU PRO ILE ALA ALA LYS
SEQRES 13 M 275 GLU MET ILE ILE GLU TYR VAL GLY GLU SER ILE ARG GLN
SEQRES 14 M 275 PRO VAL ALA GLU MET ARG GLU LYS ARG TYR ILE LYS SER
SEQRES 15 M 275 GLY ILE GLY SER SER TYR LEU PHE ARG ILE ASP GLU ASN
SEQRES 16 M 275 THR VAL ILE ASP ALA THR LYS ARG GLY GLY ILE ALA ARG
SEQRES 17 M 275 PHE ILE ASN HIS CYS CYS GLU PRO SER CYS THR ALA LYS
SEQRES 18 M 275 ILE ILE LYS VAL ASP GLY ARG LYS ARG ILE VAL ILE TYR
SEQRES 19 M 275 ALA LEU ARG ASP ILE GLY THR ASN GLU GLU LEU THR TYR
SEQRES 20 M 275 ASP TYR LYS PHE GLU ARG GLU THR ASP GLU GLY GLU ARG
SEQRES 21 M 275 LEU PRO CYS LEU CYS GLY ALA PRO SER CYS LYS GLY PHE
SEQRES 22 M 275 LEU ASN
SEQRES 1 N 439 MET ALA ASN LEU LEU LEU GLN ASP PRO PHE GLY VAL LEU
SEQRES 2 N 439 LYS GLU TYR PRO GLU LYS LEU THR HIS THR LEU GLU VAL
SEQRES 3 N 439 PRO VAL ALA ALA VAL CYS VAL LYS PHE SER PRO ARG GLY
SEQRES 4 N 439 ASP TYR LEU ALA VAL GLY CYS SER ASN GLY ALA ILE ILE
SEQRES 5 N 439 ILE TYR ASP MET ASP SER LEU LYS PRO ILE ALA MET LEU
SEQRES 6 N 439 GLY THR HIS SER GLY ALA HIS THR ARG SER VAL GLN SER
SEQRES 7 N 439 VAL CYS TRP SER ASN ASP GLY ARG TYR LEU TRP SER SER
SEQRES 8 N 439 GLY ARG ASP TRP TYR ALA LYS LEU TRP ASP MET THR GLN
SEQRES 9 N 439 PRO THR LYS CYS PHE GLN GLN TYR LYS PHE ASP GLY PRO
SEQRES 10 N 439 LEU TRP SER CYS HIS VAL VAL ARG TRP ASN VAL CYS ILE
SEQRES 11 N 439 VAL THR VAL VAL GLU GLU PRO THR ALA TYR VAL LEU THR
SEQRES 12 N 439 LEU THR ASP ARG GLN ASN ALA PHE HIS CYS PHE PRO LEU
SEQRES 13 N 439 LEU GLU GLN ASP GLN ASP ILE SER GLY HIS GLY TYR THR
SEQRES 14 N 439 LEU VAL ALA CYS PRO HIS PRO THR ILE GLU SER ILE ILE
SEQRES 15 N 439 ILE THR GLY THR SER LYS GLY TRP ILE ASN ALA PHE GLN
SEQRES 16 N 439 LEU ASP LEU GLU SER GLY PHE GLU ASP LYS ILE ARG CYS
SEQRES 17 N 439 CYS TYR GLU GLU LYS ILE ALA ASN ALA ASN ILE LYS GLN
SEQRES 18 N 439 ILE ILE ILE SER PRO SER GLY THR ARG ILE ALA ILE ASN
SEQRES 19 N 439 GLY SER ASP ARG THR ILE ARG GLN TYR GLN LEU ILE VAL
SEQRES 20 N 439 GLU ASP ASN GLU SER GLU GLY GLY SER SER HIS SER VAL
SEQRES 21 N 439 SER ILE GLU LEU GLU HIS LYS TYR GLN ASP ILE ILE ASN
SEQRES 22 N 439 ARG LEU GLN TRP ASN THR ILE PHE PHE SER ASN HIS SER
SEQRES 23 N 439 GLY GLU TYR LEU VAL ALA SER ALA HIS GLY SER SER ALA
SEQRES 24 N 439 HIS ASP LEU TYR LEU TRP GLU THR SER SER GLY SER LEU
SEQRES 25 N 439 VAL ARG VAL LEU GLU GLY ALA ASP GLU GLU LEU LEU ASP
SEQRES 26 N 439 ILE ASP TRP ASN PHE TYR SER MET ARG ILE ALA SER ASN
SEQRES 27 N 439 GLY PHE GLU SER GLY TRP VAL TYR MET TRP SER ILE VAL
SEQRES 28 N 439 ILE PRO PRO LYS TRP SER ALA LEU ALA PRO ASP PHE GLU
SEQRES 29 N 439 GLU VAL GLU GLU ASN ILE ASP TYR GLN GLU LYS GLU ASN
SEQRES 30 N 439 GLU PHE ASP ILE MET ASP ASP ASP ASN ASN LEU GLN ALA
SEQRES 31 N 439 MET THR GLU ALA GLU GLU ILE ALA ILE ASP LEU CYS THR
SEQRES 32 N 439 PRO GLU LYS TYR ASP VAL ARG GLY ASN ASP ILE SER MET
SEQRES 33 N 439 PRO SER PHE VAL ILE PRO ILE ASP TYR GLU GLY VAL ILE
SEQRES 34 N 439 ILE GLN GLN HIS TRP ALA HIS GLN GLU GLN
SEQRES 1 R 3 THR MET GLN
SEQRES 1 X 342 MET SER LEU PRO SER TRP CYS PRO ARG TYR ASP SER ARG
SEQRES 2 X 342 LYS HIS ASP PRO LYS THR GLY GLU GLU VAL TYR CYS ILE
SEQRES 3 X 342 CYS LYS LYS PRO ASP THR GLY GLU LEU MET VAL GLY CYS
SEQRES 4 X 342 ASP GLY CYS ASP ASP TRP PHE HIS PHE SER CYS LEU LYS
SEQRES 5 X 342 ILE PRO GLU LYS TYR ARG ASP LEU VAL PHE SER PHE TYR
SEQRES 6 X 342 CYS SER TYR CYS SER ALA GLY ILE THR GLY PRO ALA LEU
SEQRES 7 X 342 ILE ASN GLY GLY LYS LEU PRO LYS THR LEU TRP LYS ARG
SEQRES 8 X 342 LYS CYS ARG LEU PRO GLU CYS TYR THR GLU CYS ASP ALA
SEQRES 9 X 342 ASN SER ARG SER LYS TYR CYS SER LYS LYS HIS ALA VAL
SEQRES 10 X 342 GLN TYR VAL GLN SER ILE VAL ASP LYS LEU ASN LEU PRO
SEQRES 11 X 342 GLY VAL ASP LYS ILE ALA LEU LEU ARG GLN LEU LEU ASN
SEQRES 12 X 342 GLU THR THR SER LEU GLU GLU PHE LYS THR LEU GLY ARG
SEQRES 13 X 342 ASP LYS LEU PRO GLU VAL THR SER PRO LEU SER LYS ASP
SEQRES 14 X 342 GLN TYR SER LYS LEU LEU GLU ASN ASP GLN HIS LEU ASN
SEQRES 15 X 342 LYS LEU ILE ASN GLU HIS ASP GLU LEU VAL SER VAL LYS
SEQRES 16 X 342 LEU SER LYS LEU ASN GLU GLU ASP ALA VAL ILE GLU LYS
SEQRES 17 X 342 TYR VAL ASN TRP ILE GLY GLU VAL ASN GLU ARG LEU SER
SEQRES 18 X 342 PRO HIS PHE ASN GLN PRO THR GLY ARG LYS LYS SER LYS
SEQRES 19 X 342 SER ALA SER LYS VAL THR ILE CYS GLY TYR HIS ASN GLU
SEQRES 20 X 342 PHE THR ILE PRO ARG SER VAL GLU GLU PHE LEU ASP LYS
SEQRES 21 X 342 LEU LEU GLN LEU LYS GLU ASP GLU ASN SER ASN ILE THR
SEQRES 22 X 342 SER VAL ASP GLY VAL CYS VAL LYS THR LYS CYS ALA LYS
SEQRES 23 X 342 HIS GLN ASP TRP ILE THR LEU SER GLN ASN ASP LEU SER
SEQRES 24 X 342 GLU GLN LYS ASP SER LEU GLU ASN VAL LYS ARG ARG LEU
SEQRES 25 X 342 ASP LEU LEU ILE SER VAL ARG THR ASN GLN LEU ARG ILE
SEQRES 26 X 342 SER PHE PHE GLU GLN GLU MET SER ASN ARG VAL LEU PRO
SEQRES 27 X 342 GLY VAL LYS THR
SEQRES 1 L 405 MET SER VAL PRO VAL ILE PRO TYR LEU ASP TYR ASP ILE
SEQRES 2 L 405 VAL ASP LEU GLY SER ASP ILE LYS LYS PRO ASP PHE PRO
SEQRES 3 L 405 GLN LEU SER GLU SER HIS ARG ILE ASN GLU GLN GLN TYR
SEQRES 4 L 405 TYR ILE THR GLU ASP THR PRO LEU ASN LYS ARG ASN PHE
SEQRES 5 L 405 MET TYR GLN PRO CYS ALA ALA ASN LEU MET LEU ASP LYS
SEQRES 6 L 405 LEU LYS TYR CYS GLY THR ASP TYR PHE ASP LYS SER SER
SEQRES 7 L 405 ILE ASN LEU MET ASP ARG SER ASP LYS LEU ALA PHE SER
SEQRES 8 L 405 LEU ASP ASP HIS SER VAL SER VAL SER GLU ASN CYS GLY
SEQRES 9 L 405 TRP ARG SER VAL ARG SER ASP VAL CYS MET LYS GLU GLY
SEQRES 10 L 405 LYS ILE TYR TRP GLU VAL GLU VAL LYS ASN VAL SER ASP
SEQRES 11 L 405 THR SER HIS ILE ARG CYS GLY ILE SER ARG ARG GLU ALA
SEQRES 12 L 405 SER THR GLU THR PRO VAL GLY CYS ASP PHE TYR GLY TYR
SEQRES 13 L 405 SER ILE ARG ASP LYS GLY LEU GLN VAL ILE HIS GLU GLY
SEQRES 14 L 405 ARG LEU HIS THR VAL LEU LYS PRO HIS GLU MET GLN ALA
SEQRES 15 L 405 GLY ASP ARG ILE GLY PHE LEU LEU THR LEU PRO SER LEU
SEQRES 16 L 405 GLN SER GLN SER GLU GLN ALA MET ASP TYR SER LEU LYS
SEQRES 17 L 405 ARG ILE GLN GLU LEU ASN ASN ASP ASP SER ARG THR ASN
SEQRES 18 L 405 LYS ARG ASN LYS LYS PHE ASN LYS GLU PHE TYR LYS PHE
SEQRES 19 L 405 LEU LEU ARG SER CYS GLU PRO THR ASN VAL VAL ARG ASP
SEQRES 20 L 405 GLN ILE ALA ILE ARG TYR LYS ASN GLN LEU PHE TYR GLU
SEQRES 21 L 405 SER THR ASP TYR VAL LYS THR THR LYS PRO GLU TYR TYR
SEQRES 22 L 405 ASP ASN ARG ASP ASP MET GLN LYS PHE TYR GLU LEU GLU
SEQRES 23 L 405 ASN SER SER PHE GLU VAL PHE VAL ASN GLY VAL SER HIS
SEQRES 24 L 405 GLY ILE ALA PHE GLU GLY LEU THR PRO PHE LEU PRO PRO
SEQRES 25 L 405 PHE SER GLU LEU GLN TYR ASN GLU LYS PHE TYR LEU HIS
SEQRES 26 L 405 HIS TRP ASN LYS ARG ASN VAL THR LYS GLY ILE GLU ILE
SEQRES 27 L 405 ARG ASN LYS TYR VAL ASN ASN ASN ARG LEU GLY TYR TYR
SEQRES 28 L 405 ALA THR LEU SER SER PHE GLN GLY GLY THR ALA SER ILE
SEQRES 29 L 405 ILE THR GLU ALA MET GLU LEU LYS PHE LEU PRO LYS ASP
SEQRES 30 L 405 VAL ASP ILE LYS THR LEU ASN ASP ILE TYR ASN GLU GLN
SEQRES 31 L 405 ILE ALA SER ASP ILE VAL TRP ASP LEU ILE ASP GLU ILE
SEQRES 32 L 405 ASP THR
SEQRES 1 O 134 MET SER GLU PRO VAL MET GLU ASN MET ALA PRO GLU ASP
SEQRES 2 O 134 VAL VAL LYS LEU GLU LYS GLU GLU HIS ILE VAL PRO ASP
SEQRES 3 O 134 ILE GLY VAL SER SER ILE SER THR THR GLU PRO LEU SER
SEQRES 4 O 134 PRO SER GLY ILE PRO ARG GLU SER SER GLY THR VAL THR
SEQRES 5 O 134 SER ALA THR ALA ALA THR THR GLU ARG GLU VAL SER PRO
SEQRES 6 O 134 LYS LYS GLU LEU GLN ILE ASP HIS ASP ARG VAL ASP PRO
SEQRES 7 O 134 VAL ALA MET ILE GLY GLY SER THR THR ARG ARG TYR LEU
SEQRES 8 O 134 ASN GLU HIS VAL THR LYS HIS LEU LEU GLU GLY MET LYS
SEQRES 9 O 134 LEU ILE ALA ARG GLU LYS PRO GLU ASP PRO LEU ARG VAL
SEQRES 10 O 134 LEU GLY GLN PHE LEU ILE ASP ALA SER GLU MET ASN GLN
SEQRES 11 O 134 LYS PRO SER SER
SEQRES 1 P 134 MET SER GLU PRO VAL MET GLU ASN MET ALA PRO GLU ASP
SEQRES 2 P 134 VAL VAL LYS LEU GLU LYS GLU GLU HIS ILE VAL PRO ASP
SEQRES 3 P 134 ILE GLY VAL SER SER ILE SER THR THR GLU PRO LEU SER
SEQRES 4 P 134 PRO SER GLY ILE PRO ARG GLU SER SER GLY THR VAL THR
SEQRES 5 P 134 SER ALA THR ALA ALA THR THR GLU ARG GLU VAL SER PRO
SEQRES 6 P 134 LYS LYS GLU LEU GLN ILE ASP HIS ASP ARG VAL ASP PRO
SEQRES 7 P 134 VAL ALA MET ILE GLY GLY SER THR THR ARG ARG TYR LEU
SEQRES 8 P 134 ASN GLU HIS VAL THR LYS HIS LEU LEU GLU GLY MET LYS
SEQRES 9 P 134 LEU ILE ALA ARG GLU LYS PRO GLU ASP PRO LEU ARG VAL
SEQRES 10 P 134 LEU GLY GLN PHE LEU ILE ASP ALA SER GLU MET ASN GLN
SEQRES 11 P 134 LYS PRO SER SER
HET SAM M1101 27
HET ZN M1102 1
HETNAM SAM S-ADENOSYLMETHIONINE
HETNAM ZN ZINC ION
FORMUL 19 SAM C15 H22 N6 O5 S
FORMUL 20 ZN ZN 2+
HELIX 1 AA1 VAL A 46 GLN A 55 1 10
HELIX 2 AA2 LYS A 64 GLN A 76 1 13
HELIX 3 AA3 SER A 86 HIS A 113 1 28
HELIX 4 AA4 MET A 120 ARG A 131 1 12
HELIX 5 AA5 ASN B 25 ILE B 29 5 5
HELIX 6 AA6 THR B 30 GLY B 42 1 13
HELIX 7 AA7 LEU B 49 THR B 54 1 6
HELIX 8 AA8 THR B 54 HIS B 75 1 22
HELIX 9 AA9 ALA B 83 GLY B 94 1 12
HELIX 10 AB1 THR C 16 GLY C 22 1 7
HELIX 11 AB2 PRO C 26 LEU C 33 1 8
HELIX 12 AB3 GLY C 46 ASP C 72 1 27
HELIX 13 AB4 ILE C 79 ARG C 88 1 10
HELIX 14 AB5 TYR D 34 HIS D 46 1 13
HELIX 15 AB6 SER D 53 ASN D 81 1 29
HELIX 16 AB7 THR D 87 LEU D 99 1 13
HELIX 17 AB8 GLY D 101 SER D 120 1 20
HELIX 18 AB9 VAL E 46 LYS E 56 1 11
HELIX 19 AC1 ARG E 63 ALA E 75 1 13
HELIX 20 AC2 SER E 96 ALA E 114 1 19
HELIX 21 AC3 MET E 120 GLY E 132 1 13
HELIX 22 AC4 ASN F 25 ILE F 29 5 5
HELIX 23 AC5 THR F 30 GLY F 42 1 13
HELIX 24 AC6 GLU F 53 LYS F 77 1 25
HELIX 25 AC7 THR F 82 GLN F 93 1 12
HELIX 26 AC8 THR G 16 GLY G 22 1 7
HELIX 27 AC9 PRO G 26 LEU G 33 1 8
HELIX 28 AD1 GLY G 46 ASP G 72 1 27
HELIX 29 AD2 ILE G 79 ARG G 88 1 10
HELIX 30 AD3 ASP G 90 LEU G 97 1 8
HELIX 31 AD4 TYR H 34 HIS H 46 1 13
HELIX 32 AD5 SER H 53 ALA H 74 1 22
HELIX 33 AD6 ARG H 76 ASN H 81 1 6
HELIX 34 AD7 ARG H 89 LEU H 99 1 11
HELIX 35 AD8 PRO H 100 GLU H 102 5 3
HELIX 36 AD9 LEU H 103 ALA H 121 1 19
HELIX 37 AE1 GLN M 727 ASN M 732 1 6
HELIX 38 AE2 ASN M 738 GLU M 744 1 7
HELIX 39 AE3 GLN M 894 GLY M 908 1 15
HELIX 40 AE4 ILE M 931 ILE M 935 5 5
HELIX 41 AE5 ASN N 3 ASP N 8 1 6
HELIX 42 AE6 LYS N 355 LEU N 359 5 5
HELIX 43 AE7 GLU N 376 ASP N 380 5 5
HELIX 44 AE8 ILE N 429 HIS N 433 5 5
HELIX 45 AE9 LEU X 199 ASN X 211 1 13
HELIX 46 AF1 ILE X 213 GLU X 218 1 6
HELIX 47 AF2 ARG X 219 PHE X 224 5 6
HELIX 48 AF3 ASN X 296 GLU X 300 5 5
HELIX 49 AF4 ASP X 303 SER X 317 1 15
HELIX 50 AF5 VAL X 318 ARG X 324 1 7
HELIX 51 AF6 SER L 194 ARG L 209 1 16
HELIX 52 AF7 LYS L 229 SER L 238 1 10
HELIX 53 AF8 THR L 382 ASP L 398 1 17
HELIX 54 AF9 THR O 86 LEU O 91 1 6
HELIX 55 AG1 ASN O 92 HIS O 94 5 3
HELIX 56 AG2 LYS O 97 LYS O 104 1 8
HELIX 57 AG3 PRO O 114 SER O 126 1 13
HELIX 58 AG4 VAL P 79 GLY P 83 1 5
HELIX 59 AG5 ARG P 89 GLU P 93 5 5
HELIX 60 AG6 VAL P 95 LYS P 104 1 10
HELIX 61 AG7 VAL P 117 LEU P 122 1 6
SHEET 1 AA1 2 ARG A 83 PHE A 84 0
SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 AA2 2 THR C 101 ILE C 102 0
SHEET 2 AA2 2 LEU F 97 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 AA3 2 ARG E 83 PHE E 84 0
SHEET 2 AA3 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA4 2 THR E 118 ILE E 119 0
SHEET 2 AA4 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA5 2 GLN K 18 GLN K 22 0
SHEET 2 AA5 2 ASN K 322 ARG K 325 -1 O ARG K 325 N GLN K 18
SHEET 1 AA6 4 CYS K 34 ILE K 36 0
SHEET 2 AA6 4 LEU K 42 GLN K 47 -1 O ALA K 44 N GLN K 35
SHEET 3 AA6 4 ASP K 50 GLU K 55 -1 O ASP K 50 N GLN K 47
SHEET 4 AA6 4 MET K 62 LEU K 64 -1 O MET K 62 N VAL K 53
SHEET 1 AA7 4 CYS K 74 TRP K 77 0
SHEET 2 AA7 4 CYS K 83 SER K 88 -1 O ALA K 85 N CYS K 76
SHEET 3 AA7 4 THR K 92 HIS K 97 -1 O THR K 96 N ILE K 84
SHEET 4 AA7 4 ARG K 102 ARG K 105 -1 O ILE K 103 N ILE K 95
SHEET 1 AA8 3 ILE K 124 SER K 129 0
SHEET 2 AA8 3 SER K 133 HIS K 138 -1 O SER K 133 N SER K 129
SHEET 3 AA8 3 ALA K 144 MET K 148 -1 O MET K 148 N ILE K 134
SHEET 1 AA9 4 VAL K 155 ASP K 159 0
SHEET 2 AA9 4 ILE K 167 SER K 172 -1 O GLY K 171 N SER K 157
SHEET 3 AA9 4 ARG K 178 ASP K 181 -1 O PHE K 180 N LEU K 168
SHEET 4 AA9 4 CYS K 187 THR K 190 -1 O LYS K 189 N ILE K 179
SHEET 1 AB1 4 ILE K 206 PHE K 211 0
SHEET 2 AB1 4 PHE K 217 SER K 222 -1 O LEU K 219 N LYS K 210
SHEET 3 AB1 4 VAL K 227 GLU K 231 -1 O TRP K 230 N LEU K 218
SHEET 4 AB1 4 VAL K 237 PHE K 241 -1 O PHE K 241 N VAL K 227
SHEET 1 AB2 3 LEU K 258 LEU K 260 0
SHEET 2 AB2 3 VAL K 270 SER K 272 -1 O ILE K 271 N GLU K 259
SHEET 3 AB2 3 VAL K 281 TRP K 282 -1 O TRP K 282 N VAL K 270
SHEET 1 AB3 2 ILE K 305 SER K 306 0
SHEET 2 AB3 2 ALA K 313 THR K 314 -1 O ALA K 313 N SER K 306
SHEET 1 AB4 2 THR M 861 ARG M 864 0
SHEET 2 AB4 2 TRP M 870 TYR M 873 -1 O TYR M 873 N THR M 861
SHEET 1 AB5 3 ILE M 885 TYR M 887 0
SHEET 2 AB5 3 ILE M 956 ILE M 958 -1 O ILE M 956 N TYR M 887
SHEET 3 AB5 3 ALA M 945 ILE M 947 -1 N LYS M 946 O VAL M 957
SHEET 1 AB6 2 ILE M 892 ARG M 893 0
SHEET 2 AB6 2 THR M 921 VAL M 922 -1 O VAL M 922 N ILE M 892
SHEET 1 AB7 4 LYS N 19 LEU N 24 0
SHEET 2 AB7 4 VAL N 345 SER N 349 -1 O VAL N 345 N LEU N 24
SHEET 3 AB7 4 ARG N 334 ASN N 338 -1 N SER N 337 O TYR N 346
SHEET 4 AB7 4 ASP N 327 ASN N 329 -1 N ASP N 327 O ALA N 336
SHEET 1 AB8 3 ALA N 30 PHE N 35 0
SHEET 2 AB8 3 TYR N 41 CYS N 46 -1 O GLY N 45 N VAL N 31
SHEET 3 AB8 3 TYR N 54 ASP N 55 -1 O TYR N 54 N LEU N 42
SHEET 1 AB9 4 VAL N 76 TRP N 81 0
SHEET 2 AB9 4 TYR N 87 GLY N 92 -1 O SER N 91 N SER N 78
SHEET 3 AB9 4 ALA N 97 ASP N 101 -1 O TRP N 100 N LEU N 88
SHEET 4 AB9 4 CYS N 108 GLN N 110 -1 O PHE N 109 N LEU N 99
SHEET 1 AC1 2 LEU N 118 VAL N 123 0
SHEET 2 AC1 2 CYS N 129 VAL N 133 -1 O ILE N 130 N HIS N 122
SHEET 1 AC2 2 TYR N 140 VAL N 141 0
SHEET 2 AC2 2 PHE N 154 PRO N 155 -1 N PHE N 154 O VAL N 141
SHEET 1 AC3 3 THR N 169 PRO N 174 0
SHEET 2 AC3 3 ILE N 181 THR N 186 -1 O ILE N 183 N CYS N 173
SHEET 3 AC3 3 ILE N 191 GLN N 195 -1 O PHE N 194 N ILE N 182
SHEET 1 AC4 4 GLN N 221 ILE N 224 0
SHEET 2 AC4 4 ARG N 230 ASN N 234 -1 O ASN N 234 N GLN N 221
SHEET 3 AC4 4 ILE N 240 VAL N 247 -1 O TYR N 243 N ILE N 231
SHEET 4 AC4 4 VAL N 260 TYR N 268 -1 O GLU N 265 N GLN N 242
SHEET 1 AC5 4 TRP N 277 PHE N 282 0
SHEET 2 AC5 4 TYR N 289 ALA N 294 -1 O SER N 293 N ASN N 278
SHEET 3 AC5 4 LEU N 302 GLU N 306 -1 O TRP N 305 N LEU N 290
SHEET 4 AC5 4 LEU N 312 LEU N 316 -1 O LEU N 316 N LEU N 302
SHEET 1 AC6 3 PHE L 52 GLN L 55 0
SHEET 2 AC6 3 GLN L 256 THR L 262 -1 O TYR L 259 N GLN L 55
SHEET 3 AC6 3 GLN L 248 TYR L 253 -1 N TYR L 253 O GLN L 256
SHEET 1 AC7 2 CYS L 57 ALA L 58 0
SHEET 2 AC7 2 CYS L 69 GLY L 70 -1 O CYS L 69 N ALA L 58
SHEET 1 AC8 6 LEU L 88 ALA L 89 0
SHEET 2 AC8 6 SER L 96 VAL L 99 -1 O SER L 98 N ALA L 89
SHEET 3 AC8 6 ALA L 362 ILE L 365 -1 O ALA L 362 N VAL L 97
SHEET 4 AC8 6 LYS L 118 VAL L 125 -1 N GLU L 124 O SER L 363
SHEET 5 AC8 6 ASP L 184 THR L 191 -1 O ILE L 186 N VAL L 123
SHEET 6 AC8 6 SER L 289 GLU L 291 -1 O GLU L 291 N LEU L 189
SHEET 1 AC9 3 TRP L 105 MET L 114 0
SHEET 2 AC9 3 TYR L 350 PHE L 357 -1 O LEU L 354 N VAL L 108
SHEET 3 AC9 3 HIS L 133 ARG L 140 -1 N SER L 139 O TYR L 351
SHEET 1 AD1 2 VAL L 165 HIS L 167 0
SHEET 2 AD1 2 ARG L 170 HIS L 172 -1 O HIS L 172 N VAL L 165
SHEET 1 AD2 2 GLU L 271 TYR L 272 0
SHEET 2 AD2 2 LYS L 281 PHE L 282 -1 O LYS L 281 N TYR L 272
LINK SG CYS M 988 ZN ZN M1102 1555 1555 2.64
SITE 1 AC1 18 ILE M 867 HIS M 868 TRP M 870 GLY M 910
SITE 2 AC1 18 SER M 911 SER M 912 TYR M 913 ARG M 933
SITE 3 AC1 18 PHE M 934 ASN M 936 HIS M 937 TYR M 974
SITE 4 AC1 18 PRO M 987 CYS M 988 LEU M 989 CYS M 990
SITE 5 AC1 18 LEU M 999 MET R 4
SITE 1 AC2 4 CYS M 988 CYS M 990 ALA M 992 CYS M 995
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END