HEADER CHROMATIN BINDING PROTEIN/DNA 02-JUL-17 5WCU
TITLE CRYSTAL STRUCTURE OF 167 BP NUCLEOSOME BOUND TO THE GLOBULAR DOMAIN OF
TITLE 2 LINKER HISTONE H5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3;
COMPND 3 CHAIN: A, E, K, O;
COMPND 4 FRAGMENT: UNP RESIDUES 39-136;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H4;
COMPND 8 CHAIN: B, F, L, P;
COMPND 9 FRAGMENT: UNP RESIDUES 22-103;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HISTONE H2A;
COMPND 13 CHAIN: C, G, M, Q;
COMPND 14 FRAGMENT: UNP RESIDUES 15-118;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: HISTONE H2B;
COMPND 18 CHAIN: D, H, N, R;
COMPND 19 FRAGMENT: UNP RESIDUES 29-122;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: DNA (167-MER);
COMPND 23 CHAIN: I, S;
COMPND 24 ENGINEERED: YES;
COMPND 25 MOL_ID: 6;
COMPND 26 MOLECULE: DNA (167-MER);
COMPND 27 CHAIN: J, T;
COMPND 28 ENGINEERED: YES;
COMPND 29 MOL_ID: 7;
COMPND 30 MOLECULE: HISTONE H5;
COMPND 31 CHAIN: U, V;
COMPND 32 FRAGMENT: UNP RESIDUES 23-98;
COMPND 33 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: HIS3, HIS3:CG31613, CG31613, HIS3:CG33803, CG33803,
SOURCE 6 HIS3:CG33806, CG33806, HIS3:CG33809, CG33809, HIS3:CG33812, CG33812,
SOURCE 7 HIS3:CG33815, CG33815, HIS3:CG33818, CG33818, HIS3:CG33821, CG33821,
SOURCE 8 HIS3:CG33824, CG33824, HIS3:CG33827, CG33827, HIS3:CG33830, CG33830,
SOURCE 9 HIS3:CG33833, CG33833, HIS3:CG33836, CG33836, HIS3:CG33839, CG33839,
SOURCE 10 HIS3:CG33842, CG33842, HIS3:CG33845, CG33845, HIS3:CG33848, CG33848,
SOURCE 11 HIS3:CG33851, CG33851, HIS3:CG33854, CG33854, HIS3:CG33857, CG33857,
SOURCE 12 HIS3:CG33860, CG33860, HIS3:CG33863, CG33863, HIS3:CG33866, CG33866;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 2;
SOURCE 16 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 17 ORGANISM_COMMON: FRUIT FLY;
SOURCE 18 ORGANISM_TAXID: 7227;
SOURCE 19 GENE: HIS4, H4, HIS4R, H4R, CG3379, HIS4:CG31611, CG31611,
SOURCE 20 HIS4:CG33869, CG33869, HIS4:CG33871, CG33871, HIS4:CG33873, CG33873,
SOURCE 21 HIS4:CG33875, CG33875, HIS4:CG33877, CG33877, HIS4:CG33879, CG33879,
SOURCE 22 HIS4:CG33881, CG33881, HIS4:CG33883, CG33883, HIS4:CG33885, CG33885,
SOURCE 23 HIS4:CG33887, CG33887, HIS4:CG33889, CG33889, HIS4:CG33891, CG33891,
SOURCE 24 HIS4:CG33893, CG33893, HIS4:CG33895, CG33895, HIS4:CG33897, CG33897,
SOURCE 25 HIS4:CG33899, CG33899, HIS4:CG33901, CG33901, HIS4:CG33903, CG33903,
SOURCE 26 HIS4:CG33905, CG33905, HIS4:CG33907, CG33907, HIS4:CG33909, CG33909;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 29 MOL_ID: 3;
SOURCE 30 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 31 ORGANISM_COMMON: FRUIT FLY;
SOURCE 32 ORGANISM_TAXID: 7227;
SOURCE 33 GENE: HIS2A, H2A, HIS2A:CG31618, CG31618, HIS2A:CG33808, CG33808,
SOURCE 34 HIS2A:CG33814, CG33814, HIS2A:CG33817, CG33817, HIS2A:CG33820,
SOURCE 35 CG33820, HIS2A:CG33823, CG33823, HIS2A:CG33826, CG33826,
SOURCE 36 HIS2A:CG33829, CG33829, HIS2A:CG33832, CG33832, HIS2A:CG33835,
SOURCE 37 CG33835, HIS2A:CG33838, CG33838, HIS2A:CG33841, CG33841,
SOURCE 38 HIS2A:CG33844, CG33844, HIS2A:CG33847, CG33847, HIS2A:CG33850,
SOURCE 39 CG33850, HIS2A:CG33862, CG33862, HIS2A:CG33865, CG33865;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 42 MOL_ID: 4;
SOURCE 43 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 44 ORGANISM_COMMON: FRUIT FLY;
SOURCE 45 ORGANISM_TAXID: 7227;
SOURCE 46 GENE: HIS2B, HIS2B:CG17949, CG17949, HIS2B:CG33868, CG33868,
SOURCE 47 HIS2B:CG33870, CG33870, HIS2B:CG33872, CG33872, HIS2B:CG33874,
SOURCE 48 CG33874, HIS2B:CG33876, CG33876, HIS2B:CG33878, CG33878,
SOURCE 49 HIS2B:CG33880, CG33880, HIS2B:CG33882, CG33882, HIS2B:CG33884,
SOURCE 50 CG33884, HIS2B:CG33886, CG33886, HIS2B:CG33888, CG33888,
SOURCE 51 HIS2B:CG33890, CG33890, HIS2B:CG33892, CG33892, HIS2B:CG33894,
SOURCE 52 CG33894, HIS2B:CG33896, CG33896, HIS2B:CG33898, CG33898,
SOURCE 53 HIS2B:CG33900, CG33900, HIS2B:CG33902, CG33902, HIS2B:CG33904,
SOURCE 54 CG33904, HIS2B:CG33906, CG33906, HIS2B:CG33908, CG33908,
SOURCE 55 HIS2B:CG33910, CG33910;
SOURCE 56 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 57 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 58 MOL_ID: 5;
SOURCE 59 SYNTHETIC: YES;
SOURCE 60 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 61 ORGANISM_TAXID: 32630;
SOURCE 62 OTHER_DETAILS: 167 BP WIDOM 601 DNA;
SOURCE 63 MOL_ID: 6;
SOURCE 64 SYNTHETIC: YES;
SOURCE 65 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 66 ORGANISM_TAXID: 32630;
SOURCE 67 OTHER_DETAILS: 167 BP WIDOM 601 DNA;
SOURCE 68 MOL_ID: 7;
SOURCE 69 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 70 ORGANISM_COMMON: CHICKEN;
SOURCE 71 ORGANISM_TAXID: 9031;
SOURCE 72 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 73 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEOSOME CORE PARTICLE, HISTONE FOLD, CHROMOSOME, CHROMATIN,
KEYWDS 2 GLOBULAR DOMAIN, HISTONE H5, GH5, 167 BP NUCLEOSOME, CHROMATOSOME,
KEYWDS 3 NUCLEOSOME PACKING, 30 NM CHROMATIN FIBER, LINKER HISTONE H5, LINKER
KEYWDS 4 DNA, NUCLEOSOME BINDING PROTEIN, PROTEIN DNA COMPLEXES, DNA BINDING,
KEYWDS 5 CHROMATIN HIGHER ORDER STRUCTURE, CHROMATIN FOLDING, CHROMATIN
KEYWDS 6 BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.JIANG,B.R.ZHOU
REVDAT 1 31-OCT-18 5WCU 0
JRNL AUTH B.R.ZHOU,J.JIANG,R.GHIRLANDO,D.NOROUZI,K.N.SATHISH YADAV,
JRNL AUTH 2 H.FENG,R.WANG,P.ZHANG,V.ZHURKIN,Y.BAI
JRNL TITL REVISIT OF RECONSTITUTED 30-NM NUCLEOSOME ARRAYS REVEALS AN
JRNL TITL 2 ENSEMBLE OF DYNAMIC STRUCTURES.
JRNL REF J. MOL. BIOL. V. 430 3093 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 29959925
JRNL DOI 10.1016/J.JMB.2018.06.020
REMARK 2
REMARK 2 RESOLUTION. 5.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.930
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 15266
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1548
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 45.4439 - 12.2422 0.87 1238 140 0.1363 0.1725
REMARK 3 2 12.2422 - 9.7485 0.88 1241 136 0.1373 0.1392
REMARK 3 3 9.7485 - 8.5255 0.88 1268 141 0.1596 0.2009
REMARK 3 4 8.5255 - 7.7502 0.88 1247 138 0.1722 0.2220
REMARK 3 5 7.7502 - 7.1970 0.88 1252 137 0.2024 0.2800
REMARK 3 6 7.1970 - 6.7741 0.88 1263 143 0.2240 0.2862
REMARK 3 7 6.7741 - 6.4359 0.88 1237 135 0.2239 0.3535
REMARK 3 8 6.4359 - 6.1564 0.89 1278 142 0.2683 0.3730
REMARK 3 9 6.1564 - 5.9199 0.89 1260 136 0.2854 0.4027
REMARK 3 10 5.9199 - 5.7161 0.87 1229 137 0.3003 0.3789
REMARK 3 11 5.7161 - 5.5376 0.87 1220 136 0.3327 0.3545
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 176.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.005 28441
REMARK 3 ANGLE : 0.751 41235
REMARK 3 CHIRALITY : 0.041 4678
REMARK 3 PLANARITY : 0.004 2928
REMARK 3 DIHEDRAL : 24.504 14822
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 5WCU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000228670.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15268
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.530
REMARK 200 RESOLUTION RANGE LOW (A) : 49.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.08900
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) : 5.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 5.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 1.70600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4QLC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NH4NO3, 10% MPD (V/V), PH 4.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: UNDECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: UNDECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 82510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -404.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: U
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: UNDECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: UNDECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 61970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -384.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O, P, Q, R, S, T,
REMARK 350 AND CHAINS: V
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 VAL B 21
REMARK 465 LEU B 22
REMARK 465 ALA E 135
REMARK 465 LYS G 15
REMARK 465 ARG H 28
REMARK 465 DG I 165
REMARK 465 DA I 166
REMARK 465 DT I 167
REMARK 465 VAL L 21
REMARK 465 LEU L 22
REMARK 465 ALA O 135
REMARK 465 LYS Q 15
REMARK 465 ARG R 28
REMARK 465 DG S 165
REMARK 465 DA S 166
REMARK 465 DT S 167
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 PRO A 38 CG CD
REMARK 470 HIS A 39 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 61 CG CD1 CD2
REMARK 470 THR C 76 OG1 CG2
REMARK 470 LEU G 63 CG CD1 CD2
REMARK 470 GLU H 73 CG CD OE1 OE2
REMARK 470 THR P 80 OG1 CG2
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 N 37 OP1 DG T 132 2.18
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 150 O3' DC I 150 C3' -0.041
REMARK 500 DC I 153 O3' DC I 153 C3' -0.047
REMARK 500 DA J 22 O3' DA J 22 C3' -0.040
REMARK 500 DA J 24 O3' DA J 24 C3' -0.041
REMARK 500 DC J 75 O3' DC J 75 C3' -0.039
REMARK 500 DG J 86 O3' DG J 86 C3' -0.042
REMARK 500 DG J 88 O3' DG J 88 C3' -0.037
REMARK 500 DA J 131 O3' DA J 131 C3' -0.042
REMARK 500 DC J 152 O3' DC J 152 C3' -0.038
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. = 2.7 DEGREES
REMARK 500 DC I 9 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC I 34 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC I 63 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC I 64 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC I 89 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT I 122 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT I 127 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG I 136 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG I 155 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT I 163 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC J 3 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC J 10 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J 15 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT J 27 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA J 71 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG J 122 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA J 127 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC J 136 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG J 141 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC J 144 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT J 150 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC J 163 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DC J 164 O4' - C1' - N1 ANGL. DEV. = 2.1 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 PRO C 109 99.32 -68.86
REMARK 500 THR E 45 -51.02 -126.74
REMARK 500 PRO G 109 99.61 -68.87
REMARK 500 ASP H 48 51.23 -95.61
REMARK 500 ILE H 51 119.46 -170.97
REMARK 500 SER H 120 -90.17 -62.33
REMARK 500 PRO M 109 99.50 -68.75
REMARK 500 TYR N 34 68.85 -117.67
REMARK 500 PRO Q 109 99.43 -68.79
REMARK 500 PRO U 26 -163.17 -69.17
REMARK 500 ARG U 74 -72.74 -80.81
REMARK 500 LEU U 75 7.56 -65.17
REMARK 500 LYS U 85 88.12 63.34
REMARK 500 HIS V 25 154.58 178.70
REMARK 500 PRO V 26 -169.97 -70.17
REMARK 500 ASN V 63 2.93 -68.06
REMARK 500 ARG V 74 -60.12 -99.73
REMARK 500 LYS V 85 113.41 77.43
REMARK 500 ALA V 89 41.71 -91.28
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5WCU A 38 135 UNP P02299 H3_DROME 39 136
DBREF 5WCU B 21 102 UNP P84040 H4_DROME 22 103
DBREF 5WCU C 15 118 UNP P84051 H2A_DROME 15 118
DBREF 5WCU D 28 121 UNP P02283 H2B_DROME 29 122
DBREF 5WCU E 38 135 UNP P02299 H3_DROME 39 136
DBREF 5WCU F 21 102 UNP P84040 H4_DROME 22 103
DBREF 5WCU G 15 118 UNP P84051 H2A_DROME 15 118
DBREF 5WCU H 28 121 UNP P02283 H2B_DROME 29 122
DBREF 5WCU I 1 167 PDB 5WCU 5WCU 1 167
DBREF 5WCU J 1 167 PDB 5WCU 5WCU 1 167
DBREF 5WCU K 38 135 UNP P02299 H3_DROME 39 136
DBREF 5WCU L 21 102 UNP P84040 H4_DROME 22 103
DBREF 5WCU M 15 118 UNP P84051 H2A_DROME 15 118
DBREF 5WCU N 28 121 UNP P02283 H2B_DROME 29 122
DBREF 5WCU O 38 135 UNP P02299 H3_DROME 39 136
DBREF 5WCU P 21 102 UNP P84040 H4_DROME 22 103
DBREF 5WCU Q 15 118 UNP P84051 H2A_DROME 15 118
DBREF 5WCU R 28 121 UNP P02283 H2B_DROME 29 122
DBREF 5WCU S 1 167 PDB 5WCU 5WCU 1 167
DBREF 5WCU T 1 167 PDB 5WCU 5WCU 1 167
DBREF 5WCU U 22 97 UNP P02259 H5_CHICK 23 98
DBREF 5WCU V 22 97 UNP P02259 H5_CHICK 23 98
SEQRES 1 A 98 PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU
SEQRES 2 A 98 ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG
SEQRES 3 A 98 LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN
SEQRES 4 A 98 ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL
SEQRES 5 A 98 MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY
SEQRES 6 A 98 LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS
SEQRES 7 A 98 ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG
SEQRES 8 A 98 ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 B 82 VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA
SEQRES 2 B 82 ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE
SEQRES 3 B 82 SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS
SEQRES 4 B 82 VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR
SEQRES 5 B 82 THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP
SEQRES 6 B 82 VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR
SEQRES 7 B 82 GLY PHE GLY GLY
SEQRES 1 C 104 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 2 C 104 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 3 C 104 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 4 C 104 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 5 C 104 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 C 104 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 7 C 104 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 8 C 104 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 1 D 94 ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS
SEQRES 2 D 94 VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER
SEQRES 3 D 94 LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE
SEQRES 4 D 94 PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS
SEQRES 5 D 94 TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN
SEQRES 6 D 94 THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS
SEQRES 7 D 94 HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR
SEQRES 8 D 94 THR SER SER
SEQRES 1 E 98 PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU
SEQRES 2 E 98 ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG
SEQRES 3 E 98 LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN
SEQRES 4 E 98 ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL
SEQRES 5 E 98 MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY
SEQRES 6 E 98 LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS
SEQRES 7 E 98 ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG
SEQRES 8 E 98 ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 F 82 VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA
SEQRES 2 F 82 ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE
SEQRES 3 F 82 SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS
SEQRES 4 F 82 VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR
SEQRES 5 F 82 THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP
SEQRES 6 F 82 VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR
SEQRES 7 F 82 GLY PHE GLY GLY
SEQRES 1 G 104 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 2 G 104 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 3 G 104 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 4 G 104 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 5 G 104 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 G 104 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 7 G 104 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 8 G 104 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 1 H 94 ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS
SEQRES 2 H 94 VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER
SEQRES 3 H 94 LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE
SEQRES 4 H 94 PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS
SEQRES 5 H 94 TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN
SEQRES 6 H 94 THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS
SEQRES 7 H 94 HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR
SEQRES 8 H 94 THR SER SER
SEQRES 1 I 167 DA DT DC DG DG DC DC DG DC DC DA DT DC
SEQRES 2 I 167 DG DA DG DA DA DT DC DC DC DG DG DT DG
SEQRES 3 I 167 DC DC DG DA DG DG DC DC DG DC DT DC DA
SEQRES 4 I 167 DA DT DT DG DG DT DC DG DT DA DG DA DC
SEQRES 5 I 167 DA DG DC DT DC DT DA DG DC DA DC DC DG
SEQRES 6 I 167 DC DT DT DA DA DA DC DG DC DA DC DG DT
SEQRES 7 I 167 DA DC DG DC DG DC DT DG DT DC DC DC DC
SEQRES 8 I 167 DC DG DC DG DT DT DT DT DA DA DC DC DG
SEQRES 9 I 167 DC DC DA DA DG DG DG DG DA DT DT DA DC
SEQRES 10 I 167 DT DC DC DC DT DA DG DT DC DT DC DC DA
SEQRES 11 I 167 DG DG DC DA DC DG DT DG DT DC DA DG DA
SEQRES 12 I 167 DT DA DT DA DT DA DC DA DT DC DC DG DA
SEQRES 13 I 167 DT DG DC DA DT DG DT DA DG DA DT
SEQRES 1 J 167 DA DT DC DT DA DC DA DT DG DC DA DT DC
SEQRES 2 J 167 DG DG DA DT DG DT DA DT DA DT DA DT DC
SEQRES 3 J 167 DT DG DA DC DA DC DG DT DG DC DC DT DG
SEQRES 4 J 167 DG DA DG DA DC DT DA DG DG DG DA DG DT
SEQRES 5 J 167 DA DA DT DC DC DC DC DT DT DG DG DC DG
SEQRES 6 J 167 DG DT DT DA DA DA DA DC DG DC DG DG DG
SEQRES 7 J 167 DG DG DA DC DA DG DC DG DC DG DT DA DC
SEQRES 8 J 167 DG DT DG DC DG DT DT DT DA DA DG DC DG
SEQRES 9 J 167 DG DT DG DC DT DA DG DA DG DC DT DG DT
SEQRES 10 J 167 DC DT DA DC DG DA DC DC DA DA DT DT DG
SEQRES 11 J 167 DA DG DC DG DG DC DC DT DC DG DG DC DA
SEQRES 12 J 167 DC DC DG DG DG DA DT DT DC DT DC DG DA
SEQRES 13 J 167 DT DG DG DC DG DG DC DC DG DA DT
SEQRES 1 K 98 PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU
SEQRES 2 K 98 ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG
SEQRES 3 K 98 LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN
SEQRES 4 K 98 ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL
SEQRES 5 K 98 MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY
SEQRES 6 K 98 LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS
SEQRES 7 K 98 ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG
SEQRES 8 K 98 ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 L 82 VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA
SEQRES 2 L 82 ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE
SEQRES 3 L 82 SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS
SEQRES 4 L 82 VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR
SEQRES 5 L 82 THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP
SEQRES 6 L 82 VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR
SEQRES 7 L 82 GLY PHE GLY GLY
SEQRES 1 M 104 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 2 M 104 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 3 M 104 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 4 M 104 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 5 M 104 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 M 104 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 7 M 104 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 8 M 104 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 1 N 94 ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS
SEQRES 2 N 94 VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER
SEQRES 3 N 94 LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE
SEQRES 4 N 94 PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS
SEQRES 5 N 94 TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN
SEQRES 6 N 94 THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS
SEQRES 7 N 94 HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR
SEQRES 8 N 94 THR SER SER
SEQRES 1 O 98 PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU
SEQRES 2 O 98 ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG
SEQRES 3 O 98 LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN
SEQRES 4 O 98 ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL
SEQRES 5 O 98 MET ALA LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY
SEQRES 6 O 98 LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS
SEQRES 7 O 98 ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG
SEQRES 8 O 98 ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 P 82 VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA
SEQRES 2 P 82 ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE
SEQRES 3 P 82 SER GLY LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS
SEQRES 4 P 82 VAL PHE LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR
SEQRES 5 P 82 THR GLU HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP
SEQRES 6 P 82 VAL VAL TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR
SEQRES 7 P 82 GLY PHE GLY GLY
SEQRES 1 Q 104 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 2 Q 104 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 3 Q 104 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 4 Q 104 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 5 Q 104 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 6 Q 104 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 7 Q 104 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 8 Q 104 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 1 R 94 ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR LYS
SEQRES 2 R 94 VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER SER
SEQRES 3 R 94 LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP ILE
SEQRES 4 R 94 PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA HIS
SEQRES 5 R 94 TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE GLN
SEQRES 6 R 94 THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA LYS
SEQRES 7 R 94 HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS TYR
SEQRES 8 R 94 THR SER SER
SEQRES 1 S 167 DA DT DC DG DG DC DC DG DC DC DA DT DC
SEQRES 2 S 167 DG DA DG DA DA DT DC DC DC DG DG DT DG
SEQRES 3 S 167 DC DC DG DA DG DG DC DC DG DC DT DC DA
SEQRES 4 S 167 DA DT DT DG DG DT DC DG DT DA DG DA DC
SEQRES 5 S 167 DA DG DC DT DC DT DA DG DC DA DC DC DG
SEQRES 6 S 167 DC DT DT DA DA DA DC DG DC DA DC DG DT
SEQRES 7 S 167 DA DC DG DC DG DC DT DG DT DC DC DC DC
SEQRES 8 S 167 DC DG DC DG DT DT DT DT DA DA DC DC DG
SEQRES 9 S 167 DC DC DA DA DG DG DG DG DA DT DT DA DC
SEQRES 10 S 167 DT DC DC DC DT DA DG DT DC DT DC DC DA
SEQRES 11 S 167 DG DG DC DA DC DG DT DG DT DC DA DG DA
SEQRES 12 S 167 DT DA DT DA DT DA DC DA DT DC DC DG DA
SEQRES 13 S 167 DT DG DC DA DT DG DT DA DG DA DT
SEQRES 1 T 167 DA DT DC DT DA DC DA DT DG DC DA DT DC
SEQRES 2 T 167 DG DG DA DT DG DT DA DT DA DT DA DT DC
SEQRES 3 T 167 DT DG DA DC DA DC DG DT DG DC DC DT DG
SEQRES 4 T 167 DG DA DG DA DC DT DA DG DG DG DA DG DT
SEQRES 5 T 167 DA DA DT DC DC DC DC DT DT DG DG DC DG
SEQRES 6 T 167 DG DT DT DA DA DA DA DC DG DC DG DG DG
SEQRES 7 T 167 DG DG DA DC DA DG DC DG DC DG DT DA DC
SEQRES 8 T 167 DG DT DG DC DG DT DT DT DA DA DG DC DG
SEQRES 9 T 167 DG DT DG DC DT DA DG DA DG DC DT DG DT
SEQRES 10 T 167 DC DT DA DC DG DA DC DC DA DA DT DT DG
SEQRES 11 T 167 DA DG DC DG DG DC DC DT DC DG DG DC DA
SEQRES 12 T 167 DC DC DG DG DG DA DT DT DC DT DC DG DA
SEQRES 13 T 167 DT DG DG DC DG DG DC DC DG DA DT
SEQRES 1 U 76 SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA
SEQRES 2 U 76 ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG
SEQRES 3 U 76 GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL
SEQRES 4 U 76 GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG
SEQRES 5 U 76 ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY
SEQRES 6 U 76 VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS
SEQRES 1 V 76 SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA
SEQRES 2 V 76 ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG
SEQRES 3 V 76 GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL
SEQRES 4 V 76 GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG
SEQRES 5 V 76 ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY
SEQRES 6 V 76 VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 LYS A 79 1 17
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 42 1 13
HELIX 7 AA7 LEU B 49 ALA B 76 1 28
HELIX 8 AA8 THR B 82 GLY B 94 1 13
HELIX 9 AA9 SER C 16 GLY C 22 1 7
HELIX 10 AB1 PRO C 26 GLY C 37 1 12
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 34 HIS D 46 1 13
HELIX 15 AB6 SER D 52 ASN D 81 1 30
HELIX 16 AB7 THR D 87 LEU D 99 1 13
HELIX 17 AB8 PRO D 100 SER D 121 1 22
HELIX 18 AB9 THR E 45 SER E 57 1 13
HELIX 19 AC1 ARG E 63 LYS E 79 1 17
HELIX 20 AC2 GLN E 85 ALA E 114 1 30
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 LEU F 49 ALA F 76 1 28
HELIX 25 AC7 THR F 82 GLY F 94 1 13
HELIX 26 AC8 ARG G 17 GLY G 22 1 6
HELIX 27 AC9 PRO G 26 GLY G 37 1 12
HELIX 28 AD1 GLY G 46 ASN G 73 1 28
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 34 HIS H 46 1 13
HELIX 32 AD5 SER H 52 ASN H 81 1 30
HELIX 33 AD6 THR H 87 LEU H 99 1 13
HELIX 34 AD7 PRO H 100 SER H 121 1 22
HELIX 35 AD8 GLY K 44 SER K 57 1 14
HELIX 36 AD9 ARG K 63 LYS K 79 1 17
HELIX 37 AE1 GLN K 85 ALA K 114 1 30
HELIX 38 AE2 MET K 120 GLY K 132 1 13
HELIX 39 AE3 ASN L 25 ILE L 29 5 5
HELIX 40 AE4 THR L 30 GLY L 42 1 13
HELIX 41 AE5 LEU L 49 ALA L 76 1 28
HELIX 42 AE6 THR L 82 GLY L 94 1 13
HELIX 43 AE7 SER M 16 GLY M 22 1 7
HELIX 44 AE8 PRO M 26 GLY M 37 1 12
HELIX 45 AE9 GLY M 46 ASN M 73 1 28
HELIX 46 AF1 ILE M 79 ASP M 90 1 12
HELIX 47 AF2 ASP M 90 LEU M 97 1 8
HELIX 48 AF3 GLN M 112 LEU M 116 5 5
HELIX 49 AF4 ALA N 35 HIS N 46 1 12
HELIX 50 AF5 SER N 52 ASN N 81 1 30
HELIX 51 AF6 THR N 87 LEU N 99 1 13
HELIX 52 AF7 PRO N 100 SER N 121 1 22
HELIX 53 AF8 GLY O 44 SER O 57 1 14
HELIX 54 AF9 ARG O 63 LYS O 79 1 17
HELIX 55 AG1 GLN O 85 ALA O 114 1 30
HELIX 56 AG2 MET O 120 GLY O 132 1 13
HELIX 57 AG3 ASN P 25 ILE P 29 5 5
HELIX 58 AG4 THR P 30 GLY P 42 1 13
HELIX 59 AG5 LEU P 49 ALA P 76 1 28
HELIX 60 AG6 THR P 82 GLY P 94 1 13
HELIX 61 AG7 ARG Q 17 GLY Q 22 1 6
HELIX 62 AG8 PRO Q 26 GLY Q 37 1 12
HELIX 63 AG9 GLY Q 46 ASN Q 73 1 28
HELIX 64 AH1 ILE Q 79 ASP Q 90 1 12
HELIX 65 AH2 ASP Q 90 LEU Q 97 1 8
HELIX 66 AH3 TYR R 34 HIS R 46 1 13
HELIX 67 AH4 SER R 52 ASN R 81 1 30
HELIX 68 AH5 THR R 87 LEU R 99 1 13
HELIX 69 AH6 PRO R 100 SER R 121 1 22
HELIX 70 AH7 THR U 27 GLU U 39 1 13
HELIX 71 AH8 SER U 46 TYR U 58 1 13
HELIX 72 AH9 ASN U 63 ALA U 78 1 16
HELIX 73 AI1 THR V 27 GLU V 39 1 13
HELIX 74 AI2 ARG V 47 TYR V 58 1 12
HELIX 75 AI3 ASN V 63 LEU V 75 1 13
HELIX 76 AI4 VAL V 87 SER V 90 5 4
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 THR B 96
SHEET 1 AA4 2 ARG C 42 VAL C 43 0
SHEET 2 AA4 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 AA5 2 VAL C 100 ILE C 102 0
SHEET 2 AA5 2 THR F 96 TYR F 98 1 O THR F 96 N THR C 101
SHEET 1 AA6 2 ARG E 83 PHE E 84 0
SHEET 2 AA6 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA7 2 THR E 118 ILE E 119 0
SHEET 2 AA7 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA8 2 ARG G 42 VAL G 43 0
SHEET 2 AA8 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 AA9 2 ARG G 77 ILE G 78 0
SHEET 2 AA9 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
SHEET 1 AB1 2 ARG K 83 PHE K 84 0
SHEET 2 AB1 2 THR L 80 VAL L 81 1 O VAL L 81 N ARG K 83
SHEET 1 AB2 2 THR K 118 ILE K 119 0
SHEET 2 AB2 2 ARG L 45 ILE L 46 1 O ARG L 45 N ILE K 119
SHEET 1 AB3 2 THR L 96 TYR L 98 0
SHEET 2 AB3 2 VAL Q 100 ILE Q 102 1 O THR Q 101 N THR L 96
SHEET 1 AB4 2 ARG M 77 ILE M 78 0
SHEET 2 AB4 2 GLY N 50 ILE N 51 1 O GLY N 50 N ILE M 78
SHEET 1 AB5 2 VAL M 100 THR M 101 0
SHEET 2 AB5 2 THR P 96 LEU P 97 1 O THR P 96 N THR M 101
SHEET 1 AB6 2 ARG O 83 PHE O 84 0
SHEET 2 AB6 2 THR P 80 VAL P 81 1 O VAL P 81 N ARG O 83
SHEET 1 AB7 2 THR O 118 ILE O 119 0
SHEET 2 AB7 2 ARG P 45 ILE P 46 1 O ARG P 45 N ILE O 119
SHEET 1 AB8 2 ARG Q 42 VAL Q 43 0
SHEET 2 AB8 2 THR R 85 ILE R 86 1 O ILE R 86 N ARG Q 42
SHEET 1 AB9 2 ARG Q 77 ILE Q 78 0
SHEET 2 AB9 2 GLY R 50 ILE R 51 1 O GLY R 50 N ILE Q 78
SHEET 1 AC1 2 LEU U 81 GLN U 83 0
SHEET 2 AC1 2 PHE U 93 LEU U 95 -1 O ARG U 94 N LYS U 82
SHEET 1 AC2 3 SER V 45 SER V 46 0
SHEET 2 AC2 3 SER V 92 LEU V 95 -1 O PHE V 93 N SER V 45
SHEET 3 AC2 3 LEU V 81 GLN V 83 -1 N LYS V 82 O ARG V 94
CRYST1 65.926 108.543 180.770 100.79 90.08 89.94 P 1 4
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 0.015169 -0.000016 0.000019 0.00000
SCALE2 0.000000 0.009213 0.001756 0.00000
SCALE3 0.000000 0.000000 0.005631 0.00000
(ATOM LINES ARE NOT SHOWN.)
END