HEADER STRUCTURAL PROTEIN/DNA 31-DEC-15 5B24
TITLE THE CRYSTAL STRUCTURE OF THE NUCLEOSOME CONTAINING CYCLOBUTANE
TITLE 2 PYRIMIDINE DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.1;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: HISTONE H3/A,HISTONE H3/B,HISTONE H3/C,HISTONE H3/D,HISTONE
COMPND 5 H3/F,HISTONE H3/H,HISTONE H3/I,HISTONE H3/J,HISTONE H3/K,HISTONE
COMPND 6 H3/L;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H4;
COMPND 10 CHAIN: B, F;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HISTONE H2A TYPE 1-B/E;
COMPND 14 CHAIN: C, G;
COMPND 15 SYNONYM: HISTONE H2A.2,HISTONE H2A/A,HISTONE H2A/M;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: HISTONE H2B TYPE 1-J;
COMPND 19 CHAIN: D, H;
COMPND 20 SYNONYM: HISTONE H2B.1,HISTONE H2B.R,H2B/R;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: DNA (145-MER);
COMPND 24 CHAIN: I, J;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D,
SOURCE 6 H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H,
SOURCE 7 H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PH3.1;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 GENE: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G,
SOURCE 18 H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C,
SOURCE 19 H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E,
SOURCE 20 H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N,
SOURCE 21 H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 EXPRESSION_SYSTEM_STRAIN: JM109 (DE3);
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 27 MOL_ID: 3;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_COMMON: HUMAN;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 GENE: HIST1H2AB, H2AFM, HIST1H2AE, H2AFA;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 34 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PH2A;
SOURCE 37 MOL_ID: 4;
SOURCE 38 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 39 ORGANISM_COMMON: HUMAN;
SOURCE 40 ORGANISM_TAXID: 9606;
SOURCE 41 GENE: HIST1H2BJ, H2BFR;
SOURCE 42 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 43 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 44 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 45 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 46 EXPRESSION_SYSTEM_PLASMID: PH2B;
SOURCE 47 MOL_ID: 5;
SOURCE 48 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 49 ORGANISM_TAXID: 9606;
SOURCE 50 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 51 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 52 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 53 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 54 EXPRESSION_SYSTEM_PLASMID: PGEM-T EASY
KEYWDS CPD, NUCLEOSOME, PHOTOLESION, STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.HORIKOSHI,H.TACHIWANA,W.KAGAWA,A.OSAKABE,H.KURUMIZAKA
REVDAT 4 08-NOV-23 5B24 1 HETSYN
REVDAT 3 26-FEB-20 5B24 1 JRNL REMARK
REVDAT 2 09-MAR-16 5B24 1 JRNL
REVDAT 1 02-MAR-16 5B24 0
JRNL AUTH N.HORIKOSHI,H.TACHIWANA,W.KAGAWA,A.OSAKABE,S.MATSUMOTO,
JRNL AUTH 2 S.IWAI,K.SUGASAWA,H.KURUMIZAKA
JRNL TITL CRYSTAL STRUCTURE OF THE NUCLEOSOME CONTAINING ULTRAVIOLET
JRNL TITL 2 LIGHT-INDUCED CYCLOBUTANE PYRIMIDINE DIMER
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 471 117 2016
JRNL REFN ESSN 1090-2104
JRNL PMID 26837048
JRNL DOI 10.1016/J.BBRC.2016.01.170
REMARK 2
REMARK 2 RESOLUTION. 3.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1-2155-000
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 22758
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1164
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 34.6414 - 7.1782 0.93 2763 136 0.1646 0.1859
REMARK 3 2 7.1782 - 5.7059 0.95 2701 157 0.2402 0.2674
REMARK 3 3 5.7059 - 4.9870 0.96 2692 136 0.2126 0.2584
REMARK 3 4 4.9870 - 4.5321 0.96 2694 149 0.1915 0.2478
REMARK 3 5 4.5321 - 4.2079 0.97 2691 141 0.1957 0.2381
REMARK 3 6 4.2079 - 3.9602 0.97 2713 131 0.2229 0.3037
REMARK 3 7 3.9602 - 3.7621 0.97 2671 154 0.2466 0.3079
REMARK 3 8 3.7621 - 3.5985 0.97 2669 160 0.2674 0.3236
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 91.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 118.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.004 12786
REMARK 3 ANGLE : 0.746 18529
REMARK 3 CHIRALITY : 0.039 2107
REMARK 3 PLANARITY : 0.004 1334
REMARK 3 DIHEDRAL : 26.791 6654
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 5B24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1300000371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 0.98.701
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22837
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.47500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: PDB ENTRY 3AFA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CACODYLATE, POTASSIUM
REMARK 280 CHLORIDE, MANGANESE CHLORIDE, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 -1.000000 0.000000 0.000000 52.42400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.02650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.43400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.02650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.42400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.43400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 57380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -387.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 LYS A 37
REMARK 465 ALA A 135
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 LYS B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 ASP B 24
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 ALA C 10
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 HIS C 123
REMARK 465 HIS C 124
REMARK 465 LYS C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 GLY C 128
REMARK 465 LYS C 129
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 PRO D 1
REMARK 465 GLU D 2
REMARK 465 PRO D 3
REMARK 465 ALA D 4
REMARK 465 LYS D 5
REMARK 465 SER D 6
REMARK 465 ALA D 7
REMARK 465 PRO D 8
REMARK 465 ALA D 9
REMARK 465 PRO D 10
REMARK 465 LYS D 11
REMARK 465 LYS D 12
REMARK 465 GLY D 13
REMARK 465 SER D 14
REMARK 465 LYS D 15
REMARK 465 LYS D 16
REMARK 465 ALA D 17
REMARK 465 VAL D 18
REMARK 465 THR D 19
REMARK 465 LYS D 20
REMARK 465 ALA D 21
REMARK 465 GLN D 22
REMARK 465 LYS D 23
REMARK 465 LYS D 24
REMARK 465 ASP D 25
REMARK 465 GLY D 26
REMARK 465 LYS D 27
REMARK 465 LYS D 28
REMARK 465 ARG D 29
REMARK 465 LYS D 30
REMARK 465 ARG D 31
REMARK 465 LYS D 125
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 GLY F -3
REMARK 465 SER F -2
REMARK 465 HIS F -1
REMARK 465 MET F 0
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 LYS F 16
REMARK 465 ARG F 17
REMARK 465 HIS F 18
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 HIS G -1
REMARK 465 MET G 0
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 ALA G 10
REMARK 465 ARG G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 ALA G 14
REMARK 465 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 HIS G 123
REMARK 465 HIS G 124
REMARK 465 LYS G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 GLY G 128
REMARK 465 LYS G 129
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 HIS H -1
REMARK 465 MET H 0
REMARK 465 PRO H 1
REMARK 465 GLU H 2
REMARK 465 PRO H 3
REMARK 465 ALA H 4
REMARK 465 LYS H 5
REMARK 465 SER H 6
REMARK 465 ALA H 7
REMARK 465 PRO H 8
REMARK 465 ALA H 9
REMARK 465 PRO H 10
REMARK 465 LYS H 11
REMARK 465 LYS H 12
REMARK 465 GLY H 13
REMARK 465 SER H 14
REMARK 465 LYS H 15
REMARK 465 LYS H 16
REMARK 465 ALA H 17
REMARK 465 VAL H 18
REMARK 465 THR H 19
REMARK 465 LYS H 20
REMARK 465 ALA H 21
REMARK 465 GLN H 22
REMARK 465 LYS H 23
REMARK 465 LYS H 24
REMARK 465 ASP H 25
REMARK 465 GLY H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 28
REMARK 465 ARG H 29
REMARK 465 LYS H 30
REMARK 465 ARG H 31
REMARK 465 SER H 32
REMARK 465 LYS H 125
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 OH TYR E 99 OE1 GLU E 133 2.05
REMARK 500 NZ LYS F 79 OP1 DG I 100 2.14
REMARK 500 O TYR G 39 OG SER H 78 2.16
REMARK 500 O TYR C 39 OG SER D 78 2.19
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 TTD I 117 O3' - P - OP2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 DA J 152 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG J 203 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC J 224 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 TTD J 262 O3' - P - OP2 ANGL. DEV. = -15.2 DEGREES
REMARK 500 TTD J 262 O3' - P - OP1 ANGL. DEV. = 20.7 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 ASP A 81 69.88 38.38
REMARK 500 ILE B 29 94.77 -64.24
REMARK 500 LEU C 97 51.84 -108.94
REMARK 500 ARG D 33 78.05 59.92
REMARK 500 ASP E 81 74.54 60.28
REMARK 500 ARG E 134 79.55 -166.67
REMARK 500 ARG F 95 56.03 -94.51
REMARK 500 ARG G 99 36.68 -83.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5B24 A 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5B24 B 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5B24 C 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 5B24 D 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 5B24 E 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 5B24 F 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 5B24 G 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 5B24 H 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 5B24 I 1 145 PDB 5B24 5B24 1 145
DBREF 5B24 J 146 290 PDB 5B24 5B24 146 290
SEQADV 5B24 GLY A -3 UNP P68431 EXPRESSION TAG
SEQADV 5B24 SER A -2 UNP P68431 EXPRESSION TAG
SEQADV 5B24 HIS A -1 UNP P68431 EXPRESSION TAG
SEQADV 5B24 GLY B -3 UNP P62805 EXPRESSION TAG
SEQADV 5B24 SER B -2 UNP P62805 EXPRESSION TAG
SEQADV 5B24 HIS B -1 UNP P62805 EXPRESSION TAG
SEQADV 5B24 GLY C -3 UNP P04908 EXPRESSION TAG
SEQADV 5B24 SER C -2 UNP P04908 EXPRESSION TAG
SEQADV 5B24 HIS C -1 UNP P04908 EXPRESSION TAG
SEQADV 5B24 GLY D -3 UNP P06899 EXPRESSION TAG
SEQADV 5B24 SER D -2 UNP P06899 EXPRESSION TAG
SEQADV 5B24 HIS D -1 UNP P06899 EXPRESSION TAG
SEQADV 5B24 GLY E -3 UNP P68431 EXPRESSION TAG
SEQADV 5B24 SER E -2 UNP P68431 EXPRESSION TAG
SEQADV 5B24 HIS E -1 UNP P68431 EXPRESSION TAG
SEQADV 5B24 GLY F -3 UNP P62805 EXPRESSION TAG
SEQADV 5B24 SER F -2 UNP P62805 EXPRESSION TAG
SEQADV 5B24 HIS F -1 UNP P62805 EXPRESSION TAG
SEQADV 5B24 GLY G -3 UNP P04908 EXPRESSION TAG
SEQADV 5B24 SER G -2 UNP P04908 EXPRESSION TAG
SEQADV 5B24 HIS G -1 UNP P04908 EXPRESSION TAG
SEQADV 5B24 GLY H -3 UNP P06899 EXPRESSION TAG
SEQADV 5B24 SER H -2 UNP P06899 EXPRESSION TAG
SEQADV 5B24 HIS H -1 UNP P06899 EXPRESSION TAG
SEQRES 1 A 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 A 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 A 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 A 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 A 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 A 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 A 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 A 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 A 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 A 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 A 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 B 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 B 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 B 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 B 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 B 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 B 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 B 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 B 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 B 106 GLY GLY
SEQRES 1 C 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 C 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 C 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 C 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 C 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 C 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 C 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 C 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 C 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 C 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 C 133 LYS GLY LYS
SEQRES 1 D 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 D 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 D 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 D 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 D 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 D 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 D 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 D 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 D 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 D 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 E 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 E 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 E 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 E 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 E 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 E 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 E 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 E 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 E 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 E 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 F 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 F 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 F 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 F 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 F 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 F 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 F 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 F 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 F 106 GLY GLY
SEQRES 1 G 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 G 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 G 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 G 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 G 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 G 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 G 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 G 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 G 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 G 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 G 133 LYS GLY LYS
SEQRES 1 H 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 H 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 H 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 H 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 H 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 H 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 H 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 H 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 H 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 H 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 145 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 I 145 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 I 145 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 I 145 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 I 145 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 I 145 DC DA DG DC DT DG DA DA DT DT DC DA DG
SEQRES 7 I 145 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 I 145 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 I 145 DT DT DC DC DA DA DA DT DA DC DA DC TTD
SEQRES 10 I 145 DT DT DG DG DT DA DG DA DA DT DC DT DG
SEQRES 11 I 145 DC DA DG DG DT DG DG DA DT DA DT DT DG
SEQRES 12 I 145 DA DT
SEQRES 1 J 145 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 J 145 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 J 145 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 J 145 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 J 145 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 J 145 DC DA DG DC DT DG DA DA DT DT DC DA DG
SEQRES 7 J 145 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 J 145 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 J 145 DT DT DC DC DA DA DA DT DA DC DA DC TTD
SEQRES 10 J 145 DT DT DG DG DT DA DG DA DA DT DC DT DG
SEQRES 11 J 145 DC DA DG DG DT DG DG DA DT DA DT DT DG
SEQRES 12 J 145 DA DT
HET TTD I 117 40
HET TTD J 262 40
HETNAM TTD CIS-SYN CYCLOBUTANE THYMINE DIMER
HETSYN TTD [(3S,4S,9S,10R,12R,15AR,18BS,18CS)-3,7-DIHYDROXY-15A,
HETSYN 2 TTD 15B-DIMETHYL-7-OXIDO-13,15,16,18-
HETSYN 3 TTD TETRAOXOHEXADECAHYDRO-1H-1,4-EPOX Y-9,12-METHANO-6,8,
HETSYN 4 TTD 11-TRIOXA-12A,14,17,18A-TETRAAZA-7-
HETSYN 5 TTD PHOSPHACYCLOHEXADECA[1,2,3,4-DEF]BIPHENYLEN-10-
HETSYN 6 TTD YL]METHYL DIHYDROGEN PHOSPHATE
FORMUL 9 TTD 2(C20 H28 N4 O15 P2)
HELIX 1 AA1 GLY A 44 GLN A 55 1 12
HELIX 2 AA2 ARG A 63 ASP A 77 1 15
HELIX 3 AA3 GLN A 85 ALA A 114 1 30
HELIX 4 AA4 MET A 120 GLY A 132 1 13
HELIX 5 AA5 ASN B 25 ILE B 29 5 5
HELIX 6 AA6 THR B 30 GLY B 41 1 12
HELIX 7 AA7 LEU B 49 ALA B 76 1 28
HELIX 8 AA8 THR B 82 GLN B 93 1 12
HELIX 9 AA9 THR C 16 ALA C 21 1 6
HELIX 10 AB1 PRO C 26 LYS C 36 1 11
HELIX 11 AB2 GLY C 46 ASN C 73 1 28
HELIX 12 AB3 ILE C 79 ASP C 90 1 12
HELIX 13 AB4 ASP C 90 LEU C 97 1 8
HELIX 14 AB5 TYR D 37 HIS D 49 1 13
HELIX 15 AB6 SER D 55 ASN D 84 1 30
HELIX 16 AB7 THR D 90 LEU D 102 1 13
HELIX 17 AB8 PRO D 103 ALA D 124 1 22
HELIX 18 AB9 GLY E 44 SER E 57 1 14
HELIX 19 AC1 ARG E 63 ASP E 77 1 15
HELIX 20 AC2 GLN E 85 ALA E 114 1 30
HELIX 21 AC3 MET E 120 ARG E 131 1 12
HELIX 22 AC4 ASN F 25 ILE F 29 5 5
HELIX 23 AC5 THR F 30 GLY F 41 1 12
HELIX 24 AC6 LEU F 49 ALA F 76 1 28
HELIX 25 AC7 THR F 82 GLY F 94 1 13
HELIX 26 AC8 THR G 16 GLY G 22 1 7
HELIX 27 AC9 PRO G 26 LYS G 36 1 11
HELIX 28 AD1 GLY G 46 ASP G 72 1 27
HELIX 29 AD2 ILE G 79 ASP G 90 1 12
HELIX 30 AD3 ASP G 90 LEU G 97 1 8
HELIX 31 AD4 TYR H 37 HIS H 49 1 13
HELIX 32 AD5 SER H 55 ASN H 84 1 30
HELIX 33 AD6 THR H 90 LEU H 102 1 13
HELIX 34 AD7 GLY H 104 ALA H 124 1 21
SHEET 1 AA1 2 ARG A 83 PHE A 84 0
SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 AA2 2 THR A 118 ILE A 119 0
SHEET 2 AA2 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 AA3 2 THR B 96 TYR B 98 0
SHEET 2 AA3 2 VAL G 100 ILE G 102 1 O THR G 101 N TYR B 98
SHEET 1 AA4 2 ARG C 42 VAL C 43 0
SHEET 2 AA4 2 THR D 88 ILE D 89 1 O ILE D 89 N ARG C 42
SHEET 1 AA5 2 ARG C 77 ILE C 78 0
SHEET 2 AA5 2 GLY D 53 ILE D 54 1 O GLY D 53 N ILE C 78
SHEET 1 AA6 2 VAL C 100 ILE C 102 0
SHEET 2 AA6 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 AA7 2 ARG E 83 PHE E 84 0
SHEET 2 AA7 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA8 2 THR E 118 ILE E 119 0
SHEET 2 AA8 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA9 2 ARG G 42 VAL G 43 0
SHEET 2 AA9 2 THR H 88 ILE H 89 1 O ILE H 89 N ARG G 42
SHEET 1 AB1 2 ARG G 77 ILE G 78 0
SHEET 2 AB1 2 GLY H 53 ILE H 54 1 O GLY H 53 N ILE G 78
LINK O3' DC I 116 P TTD I 117 1555 1555 1.60
LINK O3' TTD I 117 P DT I 118 1555 1555 1.60
LINK O3' DC J 261 P TTD J 262 1555 1555 1.61
LINK O3' TTD J 262 P DT J 263 1555 1555 1.60
CISPEP 1 LYS E 37 PRO E 38 0 -10.79
CRYST1 104.848 108.868 174.053 90.00 90.00 90.00 P 21 21 21 8
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 0.009538 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009185 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
