HEADER CHROMATIN BINDING PROTEIN/DNA 11-JUN-14 4QLC
TITLE CRYSTAL STRUCTURE OF CHROMATOSOME AT 3.5 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (167-MER);
COMPND 3 CHAIN: I;
COMPND 4 FRAGMENT: 167BP WIDOM 601 DNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: DNA (167-MER);
COMPND 8 CHAIN: J;
COMPND 9 FRAGMENT: 167BP WIDOM 601 DNA;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HISTONE H3;
COMPND 13 CHAIN: A, E;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: HISTONE H4;
COMPND 17 CHAIN: B, F;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: HISTONE H2A;
COMPND 21 CHAIN: C, G;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: HISTONE H2B;
COMPND 25 CHAIN: D, H;
COMPND 26 ENGINEERED: YES;
COMPND 27 MOL_ID: 7;
COMPND 28 MOLECULE: H5;
COMPND 29 CHAIN: U;
COMPND 30 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: DNA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: DNA;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 15 ORGANISM_COMMON: FRUIT FLY;
SOURCE 16 ORGANISM_TAXID: 7227;
SOURCE 17 STRAIN: 7227;
SOURCE 18 GENE: CG31613, CG33803, CG33806, CG33809, CG33812, CG33815, CG33818,
SOURCE 19 CG33821, CG33824, CG33827, CG33830, CG33833, CG33836, CG33839,
SOURCE 20 CG33842, CG33845, CG33848, CG33851, CG33854, CG33857, CG33860,
SOURCE 21 CG33863, CG33866, H3_DROME, HIS3, HIS3:CG31613, HIS3:CG33803,
SOURCE 22 HIS3:CG33806, HIS3:CG33809, HIS3:CG33812, HIS3:CG33815,
SOURCE 23 HIS3:CG33818, HIS3:CG33821, HIS3:CG33824, HIS3:CG33827,
SOURCE 24 HIS3:CG33830, HIS3:CG33833, HIS3:CG33836, HIS3:CG33839,
SOURCE 25 HIS3:CG33842, HIS3:CG33845, HIS3:CG33848, HIS3:CG33851,
SOURCE 26 HIS3:CG33854, HIS3:CG33857, HIS3:CG33860, HIS3:CG33863,
SOURCE 27 HIS3:CG33866;
SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 30 EXPRESSION_SYSTEM_STRAIN: 562;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 33 ORGANISM_COMMON: FRUIT FLY;
SOURCE 34 ORGANISM_TAXID: 7227;
SOURCE 35 STRAIN: 7227;
SOURCE 36 GENE: CG31611, CG3379, CG33869, CG33871, CG33873, CG33875, CG33877,
SOURCE 37 CG33879, CG33881, CG33883, CG33885, CG33887, CG33889, CG33891,
SOURCE 38 CG33893, CG33895, CG33897, CG33899, CG33901, CG33903, CG33905,
SOURCE 39 CG33907, CG33909, H4, H4R, H4_DROME, HIS4, HIS4:CG31611,
SOURCE 40 HIS4:CG33869, HIS4:CG33871, HIS4:CG33873, HIS4:CG33875,
SOURCE 41 HIS4:CG33877, HIS4:CG33879, HIS4:CG33881, HIS4:CG33883,
SOURCE 42 HIS4:CG33885, HIS4:CG33887, HIS4:CG33889, HIS4:CG33891,
SOURCE 43 HIS4:CG33893, HIS4:CG33895, HIS4:CG33897, HIS4:CG33899,
SOURCE 44 HIS4:CG33901, HIS4:CG33903, HIS4:CG33905, HIS4:CG33907,
SOURCE 45 HIS4:CG33909, HIS4R;
SOURCE 46 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 47 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 48 EXPRESSION_SYSTEM_STRAIN: 562;
SOURCE 49 MOL_ID: 5;
SOURCE 50 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 51 ORGANISM_COMMON: FRUIT FLY;
SOURCE 52 ORGANISM_TAXID: 7227;
SOURCE 53 STRAIN: 7227;
SOURCE 54 GENE: CG31618, CG33808, CG33814, CG33817, CG33820, CG33823, CG33826,
SOURCE 55 CG33829, CG33832, CG33835, CG33838, CG33841, CG33844, CG33847,
SOURCE 56 CG33850, CG33862, CG33865, H2A, H2A_DROME, HIS2A, HIS2A:CG31618,
SOURCE 57 HIS2A:CG33808, HIS2A:CG33814, HIS2A:CG33817, HIS2A:CG33820,
SOURCE 58 HIS2A:CG33823, HIS2A:CG33826, HIS2A:CG33829, HIS2A:CG33832,
SOURCE 59 HIS2A:CG33835, HIS2A:CG33838, HIS2A:CG33841, HIS2A:CG33844,
SOURCE 60 HIS2A:CG33847, HIS2A:CG33850, HIS2A:CG33862, HIS2A:CG33865;
SOURCE 61 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 62 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 63 EXPRESSION_SYSTEM_STRAIN: 562;
SOURCE 64 MOL_ID: 6;
SOURCE 65 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 66 ORGANISM_COMMON: FRUIT FLY;
SOURCE 67 ORGANISM_TAXID: 7227;
SOURCE 68 STRAIN: 7227;
SOURCE 69 GENE: CG17949, CG33868, CG33870, CG33872, CG33874, CG33876, CG33878,
SOURCE 70 CG33880, CG33882, CG33884, CG33886, CG33888, CG33890, CG33892,
SOURCE 71 CG33894, CG33896, CG33898, CG33900, CG33902, CG33904, CG33906,
SOURCE 72 CG33908, CG33910, H2B_DROME, HIS2B, HIS2B:CG17949, HIS2B:CG33868,
SOURCE 73 HIS2B:CG33870, HIS2B:CG33872, HIS2B:CG33874, HIS2B:CG33876,
SOURCE 74 HIS2B:CG33878, HIS2B:CG33880, HIS2B:CG33882, HIS2B:CG33884,
SOURCE 75 HIS2B:CG33886, HIS2B:CG33888, HIS2B:CG33890, HIS2B:CG33892,
SOURCE 76 HIS2B:CG33894, HIS2B:CG33896, HIS2B:CG33898, HIS2B:CG33900,
SOURCE 77 HIS2B:CG33902, HIS2B:CG33904, HIS2B:CG33906, HIS2B:CG33908,
SOURCE 78 HIS2B:CG33910;
SOURCE 79 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 80 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 81 EXPRESSION_SYSTEM_STRAIN: 562;
SOURCE 82 MOL_ID: 7;
SOURCE 83 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 84 ORGANISM_TAXID: 9031;
SOURCE 85 STRAIN: 9031;
SOURCE 86 GENE: H5_CHICK;
SOURCE 87 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 88 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 89 EXPRESSION_SYSTEM_STRAIN: 562
KEYWDS NUCLEOSOME CORE PARTICLE, HISTONE FOLD, CHROMOSOME, CHROMATIN, GLOBAL
KEYWDS 2 HISTONE H5, GH5, NCP167, REGULATION, SEGREGATION, CHROMATOSOME, GH1,
KEYWDS 3 LIKER HISTONE H5, LINKER DNA, PROTEIN-DNA COMPLEXES, DNA BINDING
KEYWDS 4 PROTEIN-DNA COMPLEX, CHROMATIN BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.JIANG,B.R.ZHOU,T.S.XIAO,Y.W.BAI
REVDAT 5 20-SEP-23 4QLC 1 REMARK
REVDAT 4 22-NOV-17 4QLC 1 REMARK
REVDAT 3 12-AUG-15 4QLC 1 JRNL
REVDAT 2 29-JUL-15 4QLC 1 JRNL REMARK
REVDAT 1 22-JUL-15 4QLC 0
JRNL AUTH B.R.ZHOU,J.JIANG,H.FENG,R.GHIRLANDO,T.S.XIAO,Y.BAI
JRNL TITL STRUCTURAL MECHANISMS OF NUCLEOSOME RECOGNITION BY LINKER
JRNL TITL 2 HISTONES.
JRNL REF MOL.CELL V.PL 1 2 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26212454
JRNL DOI 10.1016/J.MOLCEL.2015.06.025
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1690)
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 87833
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 4443
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 43.6930 - 9.4824 0.90 3991 209 0.1486 0.1354
REMARK 3 2 9.4824 - 7.5390 0.93 4143 221 0.1579 0.1608
REMARK 3 3 7.5390 - 6.5897 0.93 4156 222 0.2007 0.2159
REMARK 3 4 6.5897 - 5.9889 0.94 4178 221 0.2196 0.2543
REMARK 3 5 5.9889 - 5.5605 0.94 4190 217 0.2283 0.2711
REMARK 3 6 5.5605 - 5.2332 0.94 4159 218 0.2163 0.2320
REMARK 3 7 5.2332 - 4.9715 0.94 4204 217 0.2190 0.2339
REMARK 3 8 4.9715 - 4.7554 0.94 4154 222 0.2161 0.2531
REMARK 3 9 4.7554 - 4.5725 0.94 4164 220 0.2219 0.2511
REMARK 3 10 4.5725 - 4.4149 0.94 4195 217 0.2230 0.2952
REMARK 3 11 4.4149 - 4.2770 0.94 4201 221 0.2226 0.2729
REMARK 3 12 4.2770 - 4.1548 0.94 4171 220 0.2422 0.2715
REMARK 3 13 4.1548 - 4.0455 0.94 4223 225 0.2421 0.2621
REMARK 3 14 4.0455 - 3.9469 0.94 4220 225 0.2577 0.3179
REMARK 3 15 3.9469 - 3.8572 0.94 4150 216 0.2621 0.3172
REMARK 3 16 3.8572 - 3.7752 0.94 4218 223 0.2759 0.3239
REMARK 3 17 3.7752 - 3.6997 0.94 4193 218 0.2825 0.3084
REMARK 3 18 3.6997 - 3.6299 0.94 4201 216 0.2842 0.3634
REMARK 3 19 3.6299 - 3.5651 0.94 4191 225 0.2894 0.3345
REMARK 3 20 3.5651 - 3.5047 0.93 4128 213 0.3003 0.3074
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) : 30.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 91.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 137.1
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 14280
REMARK 3 ANGLE : 0.757 20705
REMARK 3 CHIRALITY : 0.033 2341
REMARK 3 PLANARITY : 0.004 1471
REMARK 3 DIHEDRAL : 26.823 5889
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 : 4
REMARK 3 NCS GROUP : 1
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : NULL
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : NULL
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : NULL
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ZERO OCCUPANCY ATOMS REPRESENT ATOMS
REMARK 3 FOR WHICH NO ELECTRON DENSITY OBSERVED
REMARK 4
REMARK 4 4QLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000086199.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 274
REMARK 200 PH : 3.75
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45664
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 45.393
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 1.00200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 4INM, 1HST
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 MM CITRIC ACID, 0.1MM POTASSIUM
REMARK 280 CHLORIDE, AND 10% MPD, PH 3.75, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 61.19333
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 30.59667
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 45.89500
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 15.29833
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 76.49167
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: UNDECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: UNDECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 61600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 82790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -380.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, C, D, E, F, G, H,
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 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 DT I 167
REMARK 465 DT J 167
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 THR 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 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 GLY C 6
REMARK 465 GLY C 7
REMARK 465 LYS C 8
REMARK 465 VAL C 9
REMARK 465 LYS C 10
REMARK 465 GLY C 11
REMARK 465 LYS C 12
REMARK 465 ALA C 13
REMARK 465 LYS C 118
REMARK 465 THR C 119
REMARK 465 GLU C 120
REMARK 465 LYS C 121
REMARK 465 LYS C 122
REMARK 465 ALA C 123
REMARK 465 PRO D 1
REMARK 465 PRO D 2
REMARK 465 LYS D 3
REMARK 465 THR D 4
REMARK 465 SER D 5
REMARK 465 GLY D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 LYS D 10
REMARK 465 LYS D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 LYS D 14
REMARK 465 ALA D 15
REMARK 465 GLN D 16
REMARK 465 LYS D 17
REMARK 465 ASN D 18
REMARK 465 ILE D 19
REMARK 465 THR D 20
REMARK 465 LYS D 21
REMARK 465 THR D 22
REMARK 465 ASP D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 LYS D 26
REMARK 465 LYS D 27
REMARK 465 ARG D 28
REMARK 465 LYS D 122
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 THR 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 ARG F 19
REMARK 465 LYS F 20
REMARK 465 VAL F 21
REMARK 465 LEU F 22
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 GLY G 6
REMARK 465 GLY G 7
REMARK 465 LYS G 8
REMARK 465 VAL G 9
REMARK 465 LYS G 10
REMARK 465 GLY G 11
REMARK 465 LYS G 12
REMARK 465 LYS G 117
REMARK 465 LYS G 118
REMARK 465 THR G 119
REMARK 465 GLU G 120
REMARK 465 LYS G 121
REMARK 465 LYS G 122
REMARK 465 ALA G 123
REMARK 465 PRO H 1
REMARK 465 PRO H 2
REMARK 465 LYS H 3
REMARK 465 THR H 4
REMARK 465 SER H 5
REMARK 465 GLY H 6
REMARK 465 LYS H 7
REMARK 465 ALA H 8
REMARK 465 ALA H 9
REMARK 465 LYS H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 GLY H 13
REMARK 465 LYS H 14
REMARK 465 ALA H 15
REMARK 465 GLN H 16
REMARK 465 LYS H 17
REMARK 465 ASN H 18
REMARK 465 ILE H 19
REMARK 465 THR H 20
REMARK 465 LYS H 21
REMARK 465 THR H 22
REMARK 465 ASP H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 LYS H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 122
REMARK 465 SER U 98
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 TYR H 80 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR H 80 OH
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 U 41 O GLY U 44 2.14
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 DT I 48 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DA I 49 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I 64 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA I 69 C3' - C2' - C1' ANGL. DEV. = -4.8 DEGREES
REMARK 500 DA I 69 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC I 72 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA I 113 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA J 1 O4' - C1' - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG J 78 O4' - C4' - C3' ANGL. DEV. = -2.8 DEGREES
REMARK 500 DT J 99 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DA J 100 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DC J 108 O4' - C1' - N1 ANGL. DEV. = 3.3 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 TYR A 41 -148.37 56.29
REMARK 500 HIS D 46 84.27 -152.02
REMARK 500 TYR E 41 -146.35 54.31
REMARK 500 PHE F 100 -4.77 -149.12
REMARK 500 ARG U 42 -79.63 -63.16
REMARK 500 THR U 84 -70.41 -122.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DC I 64 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 CIT G 202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT G 202
DBREF 4QLC A 1 135 UNP P02299 H3_DROME 2 136
DBREF 4QLC B 1 102 UNP P84040 H4_DROME 2 103
DBREF 4QLC C 1 123 UNP P84051 H2A_DROME 2 124
DBREF 4QLC D 1 122 UNP P02283 H2B_DROME 2 123
DBREF 4QLC E 1 135 UNP P02299 H3_DROME 2 136
DBREF 4QLC F 1 102 UNP P84040 H4_DROME 2 103
DBREF 4QLC G 1 123 UNP P84051 H2A_DROME 2 124
DBREF 4QLC H 1 122 UNP P02283 H2B_DROME 2 123
DBREF 4QLC U 22 98 UNP P02259 H5_CHICK 23 99
DBREF 4QLC I 1 167 PDB 4QLC 4QLC 1 167
DBREF 4QLC J 1 167 PDB 4QLC 4QLC 1 167
SEQRES 1 I 167 DA DC DT DG DG DC DC DG DC DC DC DT DG
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 DT DG
SEQRES 13 I 167 DT DG DC DA DT DG DT DA DA DG DT
SEQRES 1 J 167 DA DC DT DT DA DC DA DT DG DC DA DC DA
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 DC DA
SEQRES 13 J 167 DG DG DG DC DG DG DC DC DA DG DT
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 123 SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA
SEQRES 2 C 123 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 3 C 123 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 4 C 123 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 5 C 123 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 6 C 123 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 7 C 123 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 8 C 123 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 9 C 123 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 10 C 123 LYS THR GLU LYS LYS ALA
SEQRES 1 D 122 PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY
SEQRES 2 D 122 LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS
SEQRES 3 D 122 LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR
SEQRES 4 D 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 D 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 D 122 ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA
SEQRES 7 D 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 D 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 D 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 D 122 TYR THR SER SER LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 THR GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 123 SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA
SEQRES 2 G 123 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 3 G 123 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 4 G 123 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 5 G 123 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 6 G 123 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 7 G 123 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 8 G 123 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 9 G 123 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 10 G 123 LYS THR GLU LYS LYS ALA
SEQRES 1 H 122 PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY
SEQRES 2 H 122 LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS
SEQRES 3 H 122 LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE TYR
SEQRES 4 H 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 H 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 H 122 ILE PHE GLU ARG ILE ALA ALA GLU ALA SER ARG LEU ALA
SEQRES 7 H 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 H 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 H 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 H 122 TYR THR SER SER LYS
SEQRES 1 U 77 SER ALA SER HIS PRO THR TYR SER GLU MET ILE ALA ALA
SEQRES 2 U 77 ALA ILE ARG ALA GLU LYS SER ARG GLY GLY SER SER ARG
SEQRES 3 U 77 GLN SER ILE GLN LYS TYR ILE LYS SER HIS TYR LYS VAL
SEQRES 4 U 77 GLY HIS ASN ALA ASP LEU GLN ILE LYS LEU SER ILE ARG
SEQRES 5 U 77 ARG LEU LEU ALA ALA GLY VAL LEU LYS GLN THR LYS GLY
SEQRES 6 U 77 VAL GLY ALA SER GLY SER PHE ARG LEU ALA LYS SER
HET CIT A 201 13
HET CIT G 201 13
HET CIT G 202 13
HETNAM CIT CITRIC ACID
FORMUL 12 CIT 3(C6 H8 O7)
HELIX 1 1 GLY A 44 SER A 57 1 14
HELIX 2 2 ARG A 63 ASP A 77 1 15
HELIX 3 3 GLN A 85 ALA A 114 1 30
HELIX 4 4 MET A 120 GLY A 132 1 13
HELIX 5 5 ASN B 25 ILE B 29 5 5
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 15 ALA C 20 1 6
HELIX 10 10 PRO C 25 LYS C 35 1 11
HELIX 11 11 ALA C 44 ASN C 72 1 29
HELIX 12 12 ILE C 78 ASP C 89 1 12
HELIX 13 13 ASP C 89 LEU C 96 1 8
HELIX 14 14 GLN C 111 LEU C 115 5 5
HELIX 15 15 TYR D 34 HIS D 46 1 13
HELIX 16 16 SER D 52 ASN D 81 1 30
HELIX 17 17 THR D 87 LEU D 99 1 13
HELIX 18 18 PRO D 100 SER D 120 1 21
HELIX 19 19 GLY E 44 SER E 57 1 14
HELIX 20 20 ARG E 63 ASP E 77 1 15
HELIX 21 21 GLN E 85 ALA E 114 1 30
HELIX 22 22 MET E 120 GLY E 132 1 13
HELIX 23 23 ASP F 24 ILE F 29 5 6
HELIX 24 24 THR F 30 GLY F 41 1 12
HELIX 25 25 LEU F 49 ALA F 76 1 28
HELIX 26 26 THR F 82 GLN F 93 1 12
HELIX 27 27 SER G 15 ALA G 20 1 6
HELIX 28 28 PRO G 25 LYS G 35 1 11
HELIX 29 29 ALA G 44 ASP G 71 1 28
HELIX 30 30 ILE G 78 ASN G 88 1 11
HELIX 31 31 ASP G 89 LEU G 96 1 8
HELIX 32 32 GLN G 111 LEU G 115 5 5
HELIX 33 33 TYR H 34 HIS H 46 1 13
HELIX 34 34 SER H 52 ASN H 81 1 30
HELIX 35 35 THR H 87 LEU H 99 1 13
HELIX 36 36 PRO H 100 SER H 120 1 21
HELIX 37 37 THR U 27 ALA U 38 1 12
HELIX 38 38 ARG U 47 TYR U 58 1 12
HELIX 39 39 ASN U 63 ALA U 78 1 16
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 99 ILE G 101 1 O THR G 100 N THR B 96
SHEET 1 D 2 ARG C 41 VAL C 42 0
SHEET 2 D 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 41
SHEET 1 E 2 ARG C 76 ILE C 77 0
SHEET 2 E 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 77
SHEET 1 F 2 VAL C 99 ILE C 101 0
SHEET 2 F 2 THR F 96 TYR F 98 1 O THR F 96 N THR C 100
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 41 VAL G 42 0
SHEET 2 I 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 41
SHEET 1 J 2 ARG G 76 ILE G 77 0
SHEET 2 J 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 77
SHEET 1 K 3 SER U 45 SER U 46 0
SHEET 2 K 3 GLY U 91 LEU U 95 -1 O PHE U 93 N SER U 45
SHEET 3 K 3 LEU U 81 GLY U 86 -1 N LYS U 82 O ARG U 94
SITE 1 AC1 2 ARG A 129 ARG A 134
SITE 1 AC2 2 GLU G 60 GLU G 63
SITE 1 AC3 2 LYS A 64 GLN G 103
CRYST1 262.870 262.870 91.790 90.00 90.00 120.00 P 65 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 0.003804 0.002196 0.000000 0.00000
SCALE2 0.000000 0.004393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010894 0.00000
(ATOM LINES ARE NOT SHOWN.)
END