HEADER STRUCTURAL PROTEIN/TRANSCRIPTION/DNA 22-MAY-13 4KUD
TITLE CRYSTAL STRUCTURE OF N-TERMINAL ACETYLATED SIR3 BAH DOMAIN D205N
TITLE 2 MUTANT IN COMPLEX WITH YEAST NUCLEOSOME CORE PARTICLE
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 MUTATION: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: HISTONE H2A.2;
COMPND 12 CHAIN: C, G;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: HISTONE H2B.1;
COMPND 16 CHAIN: D, H;
COMPND 17 SYNONYM: SUPPRESSOR OF TY PROTEIN 12;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: NUCLOESOME DNA;
COMPND 21 CHAIN: I, J;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: REGULATORY PROTEIN SIR3;
COMPND 25 CHAIN: K, L;
COMPND 26 FRAGMENT: BAH DOMAIN, UNP RESIDUES 2-219;
COMPND 27 SYNONYM: SILENT INFORMATION REGULATOR 3;
COMPND 28 ENGINEERED: YES;
COMPND 29 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: HHT1, YBR010W, YBR0201, HHT2, SIN2, YNL031C, N2749;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: YEAST;
SOURCE 14 ORGANISM_TAXID: 559292;
SOURCE 15 STRAIN: ATCC 204508 / S288C;
SOURCE 16 GENE: HHF1, YBR009C, YBR0122, HHF2, YNL030W, N2752;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: YEAST;
SOURCE 24 ORGANISM_TAXID: 559292;
SOURCE 25 STRAIN: ATCC 204508 / S288C;
SOURCE 26 GENE: HTA2, H2A2, YBL003C, YBL0103;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 29 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 30 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: YEAST;
SOURCE 34 ORGANISM_TAXID: 559292;
SOURCE 35 STRAIN: ATCC 204508 / S288C;
SOURCE 36 GENE: HTB1, H2B1, SPT12, YDR224C, YD9934.09C;
SOURCE 37 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 38 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 39 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 40 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 41 MOL_ID: 5;
SOURCE 42 SYNTHETIC: YES;
SOURCE 43 MOL_ID: 6;
SOURCE 44 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 45 ORGANISM_COMMON: YEAST;
SOURCE 46 ORGANISM_TAXID: 559292;
SOURCE 47 STRAIN: ATCC 204508 / S288C;
SOURCE 48 GENE: SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10;
SOURCE 49 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 50 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 51 EXPRESSION_SYSTEM_CELL: SF21;
SOURCE 52 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROTEPROTEIN-DNA COMPLEX, NUCLEOSOME, BAH DOMAIN, SILENCING, NUCLEUS,
KEYWDS 2 STRUCTURAL PROTEIN-TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.YANG,Q.FANG,M.WANG,R.REN,H.WANG,M.HE,Y.SUN,N.YANG,R.M.XU
REVDAT 2 04-SEP-13 4KUD 1 JRNL
REVDAT 1 07-AUG-13 4KUD 0
JRNL AUTH D.YANG,Q.FANG,M.WANG,R.REN,H.WANG,M.HE,Y.SUN,N.YANG,R.M.XU
JRNL TITL N ALPHA-ACETYLATED SIR3 STABILIZES THE CONFORMATION OF A
JRNL TITL 2 NUCLEOSOME-BINDING LOOP IN THE BAH DOMAIN
JRNL REF NAT.STRUCT.MOL.BIOL. 2013
JRNL REFN ESSN 1545-9985
JRNL PMID 23934152
JRNL DOI 10.1038/NSMB.2637
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 53825
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2757
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 45.3900 - 8.6746 0.98 2527 141 0.1574 0.1649
REMARK 3 2 8.6746 - 6.8931 0.99 2568 136 0.1560 0.2043
REMARK 3 3 6.8931 - 6.0240 1.00 2548 133 0.2167 0.2456
REMARK 3 4 6.0240 - 5.4742 1.00 2604 133 0.2103 0.2612
REMARK 3 5 5.4742 - 5.0824 1.00 2565 135 0.1849 0.2409
REMARK 3 6 5.0824 - 4.7831 1.00 2576 128 0.1730 0.2104
REMARK 3 7 4.7831 - 4.5438 1.00 2517 142 0.1662 0.2000
REMARK 3 8 4.5438 - 4.3462 1.00 2581 120 0.1756 0.1945
REMARK 3 9 4.3462 - 4.1790 1.00 2573 126 0.1807 0.2465
REMARK 3 10 4.1790 - 4.0349 1.00 2578 135 0.2011 0.2520
REMARK 3 11 4.0349 - 3.9088 1.00 2540 134 0.2024 0.2695
REMARK 3 12 3.9088 - 3.7971 1.00 2599 130 0.2127 0.2413
REMARK 3 13 3.7971 - 3.6972 1.00 2531 158 0.2160 0.2749
REMARK 3 14 3.6972 - 3.6070 0.99 2493 144 0.2162 0.2570
REMARK 3 15 3.6070 - 3.5250 0.99 2571 141 0.2383 0.2761
REMARK 3 16 3.5250 - 3.4501 0.99 2568 135 0.2494 0.3072
REMARK 3 17 3.4501 - 3.3811 0.99 2515 154 0.2653 0.2957
REMARK 3 18 3.3811 - 3.3173 0.99 2558 153 0.2698 0.3370
REMARK 3 19 3.3173 - 3.2581 0.99 2518 134 0.2932 0.2993
REMARK 3 20 3.2581 - 3.2028 0.99 2538 145 0.3060 0.3238
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.28
REMARK 3 B_SOL : 38.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 81.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 94.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.15500
REMARK 3 B22 (A**2) : 7.15500
REMARK 3 B33 (A**2) : -14.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 16557
REMARK 3 ANGLE : 0.980 23610
REMARK 3 CHIRALITY : 0.055 2653
REMARK 3 PLANARITY : 0.003 1988
REMARK 3 DIHEDRAL : 24.572 6704
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUN-13.
REMARK 100 THE RCSB ID CODE IS RCSB079805.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54233
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.67700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1ID3, 2FVU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 400, 0.1M KCL, 0.01M CACL2,
REMARK 280 0.05M SODIUM CITRATE(PH4.8), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 166.30667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 332.61333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 249.46000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 415.76667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 83.15333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 SER 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 SER 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 ARG A 134
REMARK 465 SER A 135
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 GLY C 2
REMARK 465 GLY C 3
REMARK 465 LYS C 4
REMARK 465 GLY C 5
REMARK 465 GLY C 6
REMARK 465 LYS C 7
REMARK 465 ALA C 8
REMARK 465 GLY C 9
REMARK 465 SER C 10
REMARK 465 ALA C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 ALA C 14
REMARK 465 SER C 15
REMARK 465 LYS C 119
REMARK 465 LYS C 120
REMARK 465 SER C 121
REMARK 465 ALA C 122
REMARK 465 LYS C 123
REMARK 465 THR C 124
REMARK 465 ALA C 125
REMARK 465 LYS C 126
REMARK 465 ALA C 127
REMARK 465 SER C 128
REMARK 465 GLN C 129
REMARK 465 GLU C 130
REMARK 465 LEU C 131
REMARK 465 MET D 0
REMARK 465 SER D 1
REMARK 465 ALA D 2
REMARK 465 LYS D 3
REMARK 465 ALA D 4
REMARK 465 GLU D 5
REMARK 465 LYS D 6
REMARK 465 LYS D 7
REMARK 465 PRO D 8
REMARK 465 ALA D 9
REMARK 465 SER D 10
REMARK 465 LYS D 11
REMARK 465 ALA D 12
REMARK 465 PRO D 13
REMARK 465 ALA D 14
REMARK 465 GLU D 15
REMARK 465 LYS D 16
REMARK 465 LYS D 17
REMARK 465 PRO D 18
REMARK 465 ALA D 19
REMARK 465 ALA D 20
REMARK 465 LYS D 21
REMARK 465 LYS D 22
REMARK 465 THR D 23
REMARK 465 SER D 24
REMARK 465 THR D 25
REMARK 465 SER D 26
REMARK 465 THR D 27
REMARK 465 ASP D 28
REMARK 465 GLY D 29
REMARK 465 LYS D 30
REMARK 465 LYS D 31
REMARK 465 ARG D 32
REMARK 465 SER D 33
REMARK 465 LYS D 34
REMARK 465 ALA D 35
REMARK 465 ARG D 36
REMARK 465 ALA D 130
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 SER 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 SER E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 ARG E 134
REMARK 465 SER E 135
REMARK 465 MET F 0
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 MET G 0
REMARK 465 ALA G 1
REMARK 465 GLY G 2
REMARK 465 GLY G 3
REMARK 465 LYS G 4
REMARK 465 GLY G 5
REMARK 465 GLY G 6
REMARK 465 LYS G 7
REMARK 465 ALA G 8
REMARK 465 GLY G 9
REMARK 465 SER G 10
REMARK 465 ALA G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 ALA G 14
REMARK 465 LYS G 120
REMARK 465 SER G 121
REMARK 465 ALA G 122
REMARK 465 LYS G 123
REMARK 465 THR G 124
REMARK 465 ALA G 125
REMARK 465 LYS G 126
REMARK 465 ALA G 127
REMARK 465 SER G 128
REMARK 465 GLN G 129
REMARK 465 GLU G 130
REMARK 465 LEU G 131
REMARK 465 MET H 0
REMARK 465 SER H 1
REMARK 465 ALA H 2
REMARK 465 LYS H 3
REMARK 465 ALA H 4
REMARK 465 GLU H 5
REMARK 465 LYS H 6
REMARK 465 LYS H 7
REMARK 465 PRO H 8
REMARK 465 ALA H 9
REMARK 465 SER H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 PRO H 13
REMARK 465 ALA H 14
REMARK 465 GLU H 15
REMARK 465 LYS H 16
REMARK 465 LYS H 17
REMARK 465 PRO H 18
REMARK 465 ALA H 19
REMARK 465 ALA H 20
REMARK 465 LYS H 21
REMARK 465 LYS H 22
REMARK 465 THR H 23
REMARK 465 SER H 24
REMARK 465 THR H 25
REMARK 465 SER H 26
REMARK 465 THR H 27
REMARK 465 ASP H 28
REMARK 465 GLY H 29
REMARK 465 LYS H 30
REMARK 465 LYS H 31
REMARK 465 ARG H 32
REMARK 465 SER H 33
REMARK 465 LYS H 34
REMARK 465 ALA H 35
REMARK 465 ALA H 130
REMARK 465 VAL K 215
REMARK 465 SER K 216
REMARK 465 GLY K 217
REMARK 465 GLN K 218
REMARK 465 LYS K 219
REMARK 465 HIS K 220
REMARK 465 HIS K 221
REMARK 465 HIS K 222
REMARK 465 HIS K 223
REMARK 465 HIS K 224
REMARK 465 HIS K 225
REMARK 465 VAL L 215
REMARK 465 SER L 216
REMARK 465 GLY L 217
REMARK 465 GLN L 218
REMARK 465 LYS L 219
REMARK 465 HIS L 220
REMARK 465 HIS L 221
REMARK 465 HIS L 222
REMARK 465 HIS L 223
REMARK 465 HIS L 224
REMARK 465 HIS L 225
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 OG SER C 46 OP2 DA J 257 2.04
REMARK 500 NH1 ARG G 33 OP1 DA J 176 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC I 3 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC I 10 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT I 21 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT I 23 O4' - C4' - C3' ANGL. DEV. = -3.1 DEGREES
REMARK 500 DT I 23 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 DC I 25 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC I 26 O4' - C1' - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DA I 27 C3' - C2' - C1' ANGL. DEV. = -6.2 DEGREES
REMARK 500 DA I 27 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA I 28 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA I 29 C3' - C2' - C1' ANGL. DEV. = -7.7 DEGREES
REMARK 500 DA I 29 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DG I 33 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT I 48 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC I 53 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA I 55 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DG I 59 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DG I 59 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT I 64 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG I 68 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG I 68 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DT I 75 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC I 76 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I 77 C3' - C2' - C1' ANGL. DEV. = -6.0 DEGREES
REMARK 500 DC I 79 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC I 89 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG I 94 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA I 95 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DT I 96 C3' - C2' - C1' ANGL. DEV. = -6.1 DEGREES
REMARK 500 DT I 96 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG I 100 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DG I 100 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA I 102 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA I 110 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DA I 115 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DA I 115 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC I 116 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 DT I 123 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG I 125 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA I 127 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DT I 128 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT I 130 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG I 135 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG I 137 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT J 154 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC J 158 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC J 162 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DC J 162 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DA J 163 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J 164 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 102 ANGLE DEVIATIONS.
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 ARG B 95 77.70 -117.96
REMARK 500 ASP C 73 -9.41 -55.31
REMARK 500 LEU C 98 55.99 -110.04
REMARK 500 ASN C 111 99.84 -163.39
REMARK 500 HIS D 52 89.88 -154.68
REMARK 500 PRO E 43 109.85 -51.59
REMARK 500 ARG G 37 78.84 -107.75
REMARK 500 LEU G 98 49.67 -107.00
REMARK 500 HIS H 52 85.21 -152.85
REMARK 500 SER H 127 4.00 -68.82
REMARK 500 GLN K 19 39.08 -150.07
REMARK 500 ASN K 26 83.55 56.08
REMARK 500 ASP K 160 91.48 -62.21
REMARK 500 ARG K 169 -29.92 -141.58
REMARK 500 GLU K 182 -74.35 -110.64
REMARK 500 LYS K 183 78.80 -104.13
REMARK 500 ASP L 17 -165.10 -73.96
REMARK 500 GLN L 19 40.17 -95.83
REMARK 500 THR L 65 -146.51 -131.65
REMARK 500 ARG L 106 62.35 -165.17
REMARK 500 PRO L 115 -165.63 -72.50
REMARK 500 ARG L 169 -36.02 -147.81
REMARK 500 GLU L 182 -82.63 -119.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KUI RELATED DB: PDB
REMARK 900 RELATED ID: 4KUL RELATED DB: PDB
DBREF 4KUD A 0 135 UNP P61830 H3_YEAST 1 136
DBREF 4KUD B 0 102 UNP P02309 H4_YEAST 1 103
DBREF 4KUD C 0 131 UNP P04912 H2A2_YEAST 1 132
DBREF 4KUD D 0 130 UNP P02293 H2B1_YEAST 1 131
DBREF 4KUD E 0 135 UNP P61830 H3_YEAST 1 136
DBREF 4KUD F 0 102 UNP P02309 H4_YEAST 1 103
DBREF 4KUD G 0 131 UNP P04912 H2A2_YEAST 1 132
DBREF 4KUD H 0 130 UNP P02293 H2B1_YEAST 1 131
DBREF 4KUD I 1 146 PDB 4KUD 4KUD 1 146
DBREF 4KUD J 147 292 PDB 4KUD 4KUD 147 292
DBREF 4KUD K 2 219 UNP P06701 SIR3_YEAST 2 219
DBREF 4KUD L 2 219 UNP P06701 SIR3_YEAST 2 219
SEQADV 4KUD ALA C 1 UNP P04912 SER 2 ENGINEERED MUTATION
SEQADV 4KUD ALA G 1 UNP P04912 SER 2 ENGINEERED MUTATION
SEQADV 4KUD ASN K 205 UNP P06701 ASP 205 ENGINEERED MUTATION
SEQADV 4KUD HIS K 220 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS K 221 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS K 222 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS K 223 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS K 224 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS K 225 UNP P06701 EXPRESSION TAG
SEQADV 4KUD ASN L 205 UNP P06701 ASP 205 ENGINEERED MUTATION
SEQADV 4KUD HIS L 220 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS L 221 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS L 222 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS L 223 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS L 224 UNP P06701 EXPRESSION TAG
SEQADV 4KUD HIS L 225 UNP P06701 EXPRESSION TAG
SEQRES 1 A 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 A 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA SER LYS ALA ALA
SEQRES 3 A 136 ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO
SEQRES 4 A 136 HIS ARG TYR LYS PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 A 136 ARG ARG PHE GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 A 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 A 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA ILE GLY
SEQRES 8 A 136 ALA LEU GLN GLU SER VAL GLU ALA TYR LEU VAL SER LEU
SEQRES 9 A 136 PHE GLU ASP THR ASN LEU ALA ALA ILE HIS ALA LYS ARG
SEQRES 10 A 136 VAL THR ILE GLN LYS LYS ASP ILE LYS LEU ALA ARG ARG
SEQRES 11 A 136 LEU ARG GLY GLU ARG SER
SEQRES 1 B 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 B 103 GLY GLY ALA LYS ARG HIS ARG LYS ILE LEU ARG ASP ASN
SEQRES 3 B 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 B 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 B 103 GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU GLU SER
SEQRES 6 B 103 VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 B 103 ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR ALA LEU
SEQRES 8 B 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 132 MET ALA GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 C 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 C 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 C 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 C 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 C 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 C 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 C 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 C 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 C 132 LEU PRO LYS LYS SER ALA LYS THR ALA LYS ALA SER GLN
SEQRES 11 C 132 GLU LEU
SEQRES 1 D 131 MET SER ALA LYS ALA GLU LYS LYS PRO ALA SER LYS ALA
SEQRES 2 D 131 PRO ALA GLU LYS LYS PRO ALA ALA LYS LYS THR SER THR
SEQRES 3 D 131 SER THR ASP GLY LYS LYS ARG SER LYS ALA ARG LYS GLU
SEQRES 4 D 131 THR TYR SER SER TYR ILE TYR LYS VAL LEU LYS GLN THR
SEQRES 5 D 131 HIS PRO ASP THR GLY ILE SER GLN LYS SER MET SER ILE
SEQRES 6 D 131 LEU ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 D 131 THR GLU ALA SER LYS LEU ALA ALA TYR ASN LYS LYS SER
SEQRES 8 D 131 THR ILE SER ALA ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 D 131 ILE LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 D 131 GLY THR ARG ALA VAL THR LYS TYR SER SER SER THR GLN
SEQRES 11 D 131 ALA
SEQRES 1 E 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 E 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA SER LYS ALA ALA
SEQRES 3 E 136 ARG LYS SER ALA PRO SER THR GLY GLY VAL LYS LYS PRO
SEQRES 4 E 136 HIS ARG TYR LYS PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 E 136 ARG ARG PHE GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 E 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 E 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA ILE GLY
SEQRES 8 E 136 ALA LEU GLN GLU SER VAL GLU ALA TYR LEU VAL SER LEU
SEQRES 9 E 136 PHE GLU ASP THR ASN LEU ALA ALA ILE HIS ALA LYS ARG
SEQRES 10 E 136 VAL THR ILE GLN LYS LYS ASP ILE LYS LEU ALA ARG ARG
SEQRES 11 E 136 LEU ARG GLY GLU ARG SER
SEQRES 1 F 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 F 103 GLY GLY ALA LYS ARG HIS ARG LYS ILE LEU ARG ASP ASN
SEQRES 3 F 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 F 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 F 103 GLU GLU VAL ARG ALA VAL LEU LYS SER PHE LEU GLU SER
SEQRES 6 F 103 VAL ILE ARG ASP SER VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 F 103 ARG LYS THR VAL THR SER LEU ASP VAL VAL TYR ALA LEU
SEQRES 8 F 103 LYS ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 132 MET ALA GLY GLY LYS GLY GLY LYS ALA GLY SER ALA ALA
SEQRES 2 G 132 LYS ALA SER GLN SER ARG SER ALA LYS ALA GLY LEU THR
SEQRES 3 G 132 PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG ARG GLY
SEQRES 4 G 132 ASN TYR ALA GLN ARG ILE GLY SER GLY ALA PRO VAL TYR
SEQRES 5 G 132 LEU THR ALA VAL LEU GLU TYR LEU ALA ALA GLU ILE LEU
SEQRES 6 G 132 GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR
SEQRES 7 G 132 ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN
SEQRES 8 G 132 ASP ASP GLU LEU ASN LYS LEU LEU GLY ASN VAL THR ILE
SEQRES 9 G 132 ALA GLN GLY GLY VAL LEU PRO ASN ILE HIS GLN ASN LEU
SEQRES 10 G 132 LEU PRO LYS LYS SER ALA LYS THR ALA LYS ALA SER GLN
SEQRES 11 G 132 GLU LEU
SEQRES 1 H 131 MET SER ALA LYS ALA GLU LYS LYS PRO ALA SER LYS ALA
SEQRES 2 H 131 PRO ALA GLU LYS LYS PRO ALA ALA LYS LYS THR SER THR
SEQRES 3 H 131 SER THR ASP GLY LYS LYS ARG SER LYS ALA ARG LYS GLU
SEQRES 4 H 131 THR TYR SER SER TYR ILE TYR LYS VAL LEU LYS GLN THR
SEQRES 5 H 131 HIS PRO ASP THR GLY ILE SER GLN LYS SER MET SER ILE
SEQRES 6 H 131 LEU ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 H 131 THR GLU ALA SER LYS LEU ALA ALA TYR ASN LYS LYS SER
SEQRES 8 H 131 THR ILE SER ALA ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 H 131 ILE LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 H 131 GLY THR ARG ALA VAL THR LYS TYR SER SER SER THR GLN
SEQRES 11 H 131 ALA
SEQRES 1 I 146 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 I 146 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 I 146 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 I 146 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 I 146 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 I 146 DC DA DG DC DG DG DA DA DT DT DC DC DG
SEQRES 7 I 146 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 I 146 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 I 146 DT DT DC DC DA DA DA DT DA DC DA DC DT
SEQRES 10 I 146 DT DT DT DG DG DT DA DG DA DA DT DC DT
SEQRES 11 I 146 DG DC DA DG DG DT DG DG DA DT DA DT DT
SEQRES 12 I 146 DG DA DT
SEQRES 1 J 146 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 J 146 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 J 146 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 J 146 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 J 146 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 J 146 DC DA DG DC DG DG DA DA DT DT DC DC DG
SEQRES 7 J 146 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 J 146 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 J 146 DT DT DC DC DA DA DA DT DA DC DA DC DT
SEQRES 10 J 146 DT DT DT DG DG DT DA DG DA DA DT DC DT
SEQRES 11 J 146 DG DC DA DG DG DT DG DG DA DT DA DT DT
SEQRES 12 J 146 DG DA DT
SEQRES 1 K 224 AYA LYS THR LEU LYS ASP LEU ASP GLY TRP GLN VAL ILE
SEQRES 2 K 224 ILE THR ASP ASP GLN GLY ARG VAL ILE ASP ASP ASN ASN
SEQRES 3 K 224 ARG ARG ARG SER ARG LYS ARG GLY GLY GLU ASN VAL PHE
SEQRES 4 K 224 LEU LYS ARG ILE SER ASP GLY LEU SER PHE GLY LYS GLY
SEQRES 5 K 224 GLU SER VAL ILE PHE ASN ASP ASN VAL THR GLU THR TYR
SEQRES 6 K 224 SER VAL TYR LEU ILE HIS GLU ILE ARG LEU ASN THR LEU
SEQRES 7 K 224 ASN ASN VAL VAL GLU ILE TRP VAL PHE SER TYR LEU ARG
SEQRES 8 K 224 TRP PHE GLU LEU LYS PRO LYS LEU TYR TYR GLU GLN PHE
SEQRES 9 K 224 ARG PRO ASP LEU ILE LYS GLU ASP HIS PRO LEU GLU PHE
SEQRES 10 K 224 TYR LYS ASP LYS PHE PHE ASN GLU VAL ASN LYS SER GLU
SEQRES 11 K 224 LEU TYR LEU THR ALA GLU LEU SER GLU ILE TRP LEU LYS
SEQRES 12 K 224 ASP PHE ILE ALA VAL GLY GLN ILE LEU PRO GLU SER GLN
SEQRES 13 K 224 TRP ASN ASP SER SER ILE ASP LYS ILE GLU ASP ARG ASP
SEQRES 14 K 224 PHE LEU VAL ARG TYR ALA CYS GLU PRO THR ALA GLU LYS
SEQRES 15 K 224 PHE VAL PRO ILE ASP ILE PHE GLN ILE ILE ARG ARG VAL
SEQRES 16 K 224 LYS GLU MET GLU PRO LYS GLN SER ASN GLU TYR LEU LYS
SEQRES 17 K 224 ARG VAL SER VAL PRO VAL SER GLY GLN LYS HIS HIS HIS
SEQRES 18 K 224 HIS HIS HIS
SEQRES 1 L 224 AYA LYS THR LEU LYS ASP LEU ASP GLY TRP GLN VAL ILE
SEQRES 2 L 224 ILE THR ASP ASP GLN GLY ARG VAL ILE ASP ASP ASN ASN
SEQRES 3 L 224 ARG ARG ARG SER ARG LYS ARG GLY GLY GLU ASN VAL PHE
SEQRES 4 L 224 LEU LYS ARG ILE SER ASP GLY LEU SER PHE GLY LYS GLY
SEQRES 5 L 224 GLU SER VAL ILE PHE ASN ASP ASN VAL THR GLU THR TYR
SEQRES 6 L 224 SER VAL TYR LEU ILE HIS GLU ILE ARG LEU ASN THR LEU
SEQRES 7 L 224 ASN ASN VAL VAL GLU ILE TRP VAL PHE SER TYR LEU ARG
SEQRES 8 L 224 TRP PHE GLU LEU LYS PRO LYS LEU TYR TYR GLU GLN PHE
SEQRES 9 L 224 ARG PRO ASP LEU ILE LYS GLU ASP HIS PRO LEU GLU PHE
SEQRES 10 L 224 TYR LYS ASP LYS PHE PHE ASN GLU VAL ASN LYS SER GLU
SEQRES 11 L 224 LEU TYR LEU THR ALA GLU LEU SER GLU ILE TRP LEU LYS
SEQRES 12 L 224 ASP PHE ILE ALA VAL GLY GLN ILE LEU PRO GLU SER GLN
SEQRES 13 L 224 TRP ASN ASP SER SER ILE ASP LYS ILE GLU ASP ARG ASP
SEQRES 14 L 224 PHE LEU VAL ARG TYR ALA CYS GLU PRO THR ALA GLU LYS
SEQRES 15 L 224 PHE VAL PRO ILE ASP ILE PHE GLN ILE ILE ARG ARG VAL
SEQRES 16 L 224 LYS GLU MET GLU PRO LYS GLN SER ASN GLU TYR LEU LYS
SEQRES 17 L 224 ARG VAL SER VAL PRO VAL SER GLY GLN LYS HIS HIS HIS
SEQRES 18 L 224 HIS HIS HIS
MODRES 4KUD AYA K 2 ALA N-ACETYLALANINE
MODRES 4KUD AYA L 2 ALA N-ACETYLALANINE
HET AYA K 2 8
HET AYA L 2 8
HETNAM AYA N-ACETYLALANINE
FORMUL 11 AYA 2(C5 H9 N O3)
FORMUL 13 HOH *66(H2 O)
HELIX 1 1 GLY A 44 SER A 57 1 14
HELIX 2 2 ARG A 63 GLN A 76 1 14
HELIX 3 3 GLN A 85 ALA A 114 1 30
HELIX 4 4 GLN A 120 ARG A 131 1 12
HELIX 5 5 ASP B 24 ILE B 29 5 6
HELIX 6 6 THR B 30 GLY B 42 1 13
HELIX 7 7 LEU B 49 ALA B 76 1 28
HELIX 8 8 THR B 82 GLN B 93 1 12
HELIX 9 9 SER C 17 ALA C 22 1 6
HELIX 10 10 PRO C 27 GLY C 38 1 12
HELIX 11 11 GLY C 47 ASP C 73 1 27
HELIX 12 12 ILE C 80 ASP C 91 1 12
HELIX 13 13 ASP C 91 LEU C 98 1 8
HELIX 14 14 TYR D 40 HIS D 52 1 13
HELIX 15 15 SER D 58 ASN D 87 1 30
HELIX 16 16 SER D 93 LEU D 105 1 13
HELIX 17 17 PRO D 106 THR D 128 1 23
HELIX 18 18 GLY E 44 SER E 57 1 14
HELIX 19 19 ARG E 63 GLN E 76 1 14
HELIX 20 20 GLN E 85 ALA E 114 1 30
HELIX 21 21 GLN E 120 ARG E 131 1 12
HELIX 22 22 ASP F 24 ILE F 29 5 6
HELIX 23 23 THR F 30 GLY F 42 1 13
HELIX 24 24 LEU F 49 ALA F 76 1 28
HELIX 25 25 THR F 82 GLN F 93 1 12
HELIX 26 26 SER G 17 ALA G 22 1 6
HELIX 27 27 PRO G 27 ARG G 37 1 11
HELIX 28 28 GLY G 47 ASP G 73 1 27
HELIX 29 29 ILE G 80 ASP G 91 1 12
HELIX 30 30 ASP G 91 LEU G 98 1 8
HELIX 31 31 TYR H 40 HIS H 52 1 13
HELIX 32 32 SER H 58 ASN H 87 1 30
HELIX 33 33 SER H 93 LEU H 105 1 13
HELIX 34 34 PRO H 106 SER H 127 1 22
HELIX 35 35 THR K 4 ASP K 9 5 6
HELIX 36 36 ARG K 92 LEU K 96 5 5
HELIX 37 37 LYS K 97 ARG K 106 1 10
HELIX 38 38 ARG K 106 GLU K 112 1 7
HELIX 39 39 PRO K 115 VAL K 127 1 13
HELIX 40 40 TRP K 142 LYS K 144 5 3
HELIX 41 41 PRO K 154 ASP K 160 1 7
HELIX 42 42 ASP K 188 MET K 199 1 12
HELIX 43 43 GLU K 200 SER K 212 1 13
HELIX 44 44 LEU L 5 ASP L 9 5 5
HELIX 45 45 LYS L 97 ARG L 106 1 10
HELIX 46 46 ARG L 106 GLU L 112 1 7
HELIX 47 47 PRO L 115 VAL L 127 1 13
HELIX 48 48 TRP L 142 LYS L 144 5 3
HELIX 49 49 PRO L 154 ASP L 160 1 7
HELIX 50 50 ASP L 188 MET L 199 1 12
HELIX 51 51 GLU L 200 SER L 212 1 13
SHEET 1 A 2 ARG A 83 PHE A 84 0
SHEET 2 A 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 B 2 THR A 118 ILE A 119 0
SHEET 2 B 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 C 2 THR B 96 TYR B 98 0
SHEET 2 C 2 VAL G 101 ILE G 103 1 O THR G 102 N TYR B 98
SHEET 1 D 2 ARG C 43 ILE C 44 0
SHEET 2 D 2 THR D 91 ILE D 92 1 O ILE D 92 N ARG C 43
SHEET 1 E 2 ARG C 78 ILE C 79 0
SHEET 2 E 2 GLY D 56 ILE D 57 1 O GLY D 56 N ILE C 79
SHEET 1 F 2 VAL C 101 ILE C 103 0
SHEET 2 F 2 THR F 96 TYR F 98 1 O THR F 96 N THR C 102
SHEET 1 G 2 ARG E 83 PHE E 84 0
SHEET 2 G 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 H 2 THR E 118 ILE E 119 0
SHEET 2 H 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 I 2 ARG G 43 ILE G 44 0
SHEET 2 I 2 THR H 91 ILE H 92 1 O ILE H 92 N ARG G 43
SHEET 1 J 2 ARG G 78 ILE G 79 0
SHEET 2 J 2 GLY H 56 ILE H 57 1 O GLY H 56 N ILE G 79
SHEET 1 K 4 VAL K 22 ILE K 23 0
SHEET 2 K 4 TRP K 11 THR K 16 -1 N ILE K 15 O ILE K 23
SHEET 3 K 4 ASN K 38 ARG K 43 -1 O PHE K 40 N ILE K 14
SHEET 4 K 4 SER K 49 PHE K 50 -1 O PHE K 50 N LEU K 41
SHEET 1 L 7 PHE K 146 VAL K 149 0
SHEET 2 L 7 SER K 55 ASP K 60 -1 N ILE K 57 O ALA K 148
SHEET 3 L 7 THR K 65 LEU K 76 -1 O TYR K 69 N VAL K 56
SHEET 4 L 7 VAL K 83 LEU K 91 -1 O GLU K 84 N ARG K 75
SHEET 5 L 7 GLU K 131 ILE K 141 -1 O TYR K 133 N LEU K 91
SHEET 6 L 7 ASP K 170 ALA K 176 1 O LEU K 172 N LEU K 132
SHEET 7 L 7 GLN K 151 ILE K 152 1 N GLN K 151 O PHE K 171
SHEET 1 M 7 PHE K 146 VAL K 149 0
SHEET 2 M 7 SER K 55 ASP K 60 -1 N ILE K 57 O ALA K 148
SHEET 3 M 7 THR K 65 LEU K 76 -1 O TYR K 69 N VAL K 56
SHEET 4 M 7 VAL K 83 LEU K 91 -1 O GLU K 84 N ARG K 75
SHEET 5 M 7 GLU K 131 ILE K 141 -1 O TYR K 133 N LEU K 91
SHEET 6 M 7 ASP K 170 ALA K 176 1 O LEU K 172 N LEU K 132
SHEET 7 M 7 VAL K 185 PRO K 186 -1 O VAL K 185 N ALA K 176
SHEET 1 N 4 VAL L 22 ILE L 23 0
SHEET 2 N 4 TRP L 11 THR L 16 -1 N ILE L 15 O ILE L 23
SHEET 3 N 4 ASN L 38 ARG L 43 -1 O LYS L 42 N GLN L 12
SHEET 4 N 4 SER L 49 PHE L 50 -1 O PHE L 50 N LEU L 41
SHEET 1 O 7 PHE L 146 VAL L 149 0
SHEET 2 O 7 SER L 55 ASP L 60 -1 N ILE L 57 O ALA L 148
SHEET 3 O 7 THR L 65 LEU L 76 -1 O SER L 67 N PHE L 58
SHEET 4 O 7 VAL L 83 LEU L 91 -1 O GLU L 84 N ARG L 75
SHEET 5 O 7 GLU L 131 ILE L 141 -1 O TYR L 133 N LEU L 91
SHEET 6 O 7 ASP L 170 ALA L 176 1 O LEU L 172 N LEU L 132
SHEET 7 O 7 GLN L 151 ILE L 152 1 N GLN L 151 O PHE L 171
SHEET 1 P 7 PHE L 146 VAL L 149 0
SHEET 2 P 7 SER L 55 ASP L 60 -1 N ILE L 57 O ALA L 148
SHEET 3 P 7 THR L 65 LEU L 76 -1 O SER L 67 N PHE L 58
SHEET 4 P 7 VAL L 83 LEU L 91 -1 O GLU L 84 N ARG L 75
SHEET 5 P 7 GLU L 131 ILE L 141 -1 O TYR L 133 N LEU L 91
SHEET 6 P 7 ASP L 170 ALA L 176 1 O LEU L 172 N LEU L 132
SHEET 7 P 7 VAL L 185 PRO L 186 -1 O VAL L 185 N ALA L 176
LINK C AYA K 2 N LYS K 3 1555 1555 1.33
LINK C AYA L 2 N LYS L 3 1555 1555 1.33
CRYST1 108.330 108.330 498.920 90.00 90.00 120.00 P 61 12
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 0.009231 0.005330 0.000000 0.00000
SCALE2 0.000000 0.010659 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002004 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
