HEADER CHAPERONE/STRUCTURAL PROTEIN 10-OCT-06 2IO5
TITLE CRYSTAL STRUCTURE OF THE CIA- HISTONE H3-H4 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASF1A PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-172;
COMPND 5 SYNONYM: CIA, CCG1-INTERACTING FACTOR A, ANTI SILENCING FUNCTION 1
COMPND 6 HOMOLOG A;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H3.1;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HISTONE H4;
COMPND 14 CHAIN: C;
COMPND 15 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: ASF1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS -RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 13 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 14 ORGANISM_TAXID: 8355;
SOURCE 15 GENE: HISTONE H3.1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 23 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 24 ORGANISM_TAXID: 8355;
SOURCE 25 GENE: HISTONE H4;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS HISTONE, CHAPERONE, CHAPERONE-STRUCTURAL PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.NATSUME,Y.AKAI,M.HORIKOSHI,T.SENDA
REVDAT 5 25-OCT-23 2IO5 1 SEQADV
REVDAT 4 13-JUL-11 2IO5 1 VERSN
REVDAT 3 24-FEB-09 2IO5 1 VERSN
REVDAT 2 20-MAR-07 2IO5 1 JRNL
REVDAT 1 27-FEB-07 2IO5 0
JRNL AUTH R.NATSUME,M.EITOKU,Y.AKAI,N.SANO,M.HORIKOSHI,T.SENDA
JRNL TITL STRUCTURE AND FUNCTION OF THE HISTONE CHAPERONE CIA/ASF1
JRNL TITL 2 COMPLEXED WITH HISTONES H3 AND H4.
JRNL REF NATURE V. 446 338 2007
JRNL REFN ISSN 0028-0836
JRNL PMID 17293877
JRNL DOI 10.1038/NATURE05613
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 11529
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.238
REMARK 3 FREE R VALUE : 0.293
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 604
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 859
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.4520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 51.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.78000
REMARK 3 B22 (A**2) : 2.49000
REMARK 3 B33 (A**2) : 0.29000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.810
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.377
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.276
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.822
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2521 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1750 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3415 ; 1.326 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4235 ; 0.835 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 304 ; 6.786 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 125 ;33.537 ;23.200
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 440 ;20.878 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.405 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 386 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2786 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 534 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 467 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1668 ; 0.195 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1180 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1536 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 39 ; 0.097 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 10 ; 0.149 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.242 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.123 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1987 ; 0.931 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 612 ; 0.087 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2492 ; 1.012 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1141 ; 1.183 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 923 ; 1.844 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 154
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4446 -33.0909 10.9294
REMARK 3 T TENSOR
REMARK 3 T11: -0.0113 T22: 0.0240
REMARK 3 T33: -0.0325 T12: -0.0162
REMARK 3 T13: -0.0382 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 1.0643 L22: 2.7944
REMARK 3 L33: 1.1081 L12: -0.7037
REMARK 3 L13: -0.0143 L23: 0.3035
REMARK 3 S TENSOR
REMARK 3 S11: -0.0716 S12: -0.0513 S13: 0.0329
REMARK 3 S21: -0.0589 S22: 0.0454 S23: 0.0685
REMARK 3 S31: -0.0528 S32: -0.0265 S33: 0.0261
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 60 B 135
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9025 -25.8079 2.2475
REMARK 3 T TENSOR
REMARK 3 T11: 0.0311 T22: -0.0567
REMARK 3 T33: 0.0116 T12: -0.0147
REMARK 3 T13: 0.0646 T23: -0.0449
REMARK 3 L TENSOR
REMARK 3 L11: 3.4264 L22: 1.5922
REMARK 3 L33: 1.8975 L12: 0.9699
REMARK 3 L13: -1.1355 L23: -1.1713
REMARK 3 S TENSOR
REMARK 3 S11: 0.0526 S12: 0.0893 S13: 0.1849
REMARK 3 S21: -0.0761 S22: -0.0066 S23: 0.0692
REMARK 3 S31: 0.0186 S32: -0.0127 S33: -0.0460
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 24 C 100
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0995 -22.5836 1.6137
REMARK 3 T TENSOR
REMARK 3 T11: 0.0416 T22: 0.0398
REMARK 3 T33: -0.0202 T12: 0.0059
REMARK 3 T13: 0.0357 T23: 0.0254
REMARK 3 L TENSOR
REMARK 3 L11: 2.3494 L22: 0.5651
REMARK 3 L33: 1.4666 L12: 0.5351
REMARK 3 L13: -0.6869 L23: 0.2499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: 0.3385 S13: 0.3174
REMARK 3 S21: -0.0776 S22: -0.0235 S23: -0.0792
REMARK 3 S31: -0.0800 S32: -0.1364 S33: 0.0016
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2IO5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039806.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12148
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 29.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.41300
REMARK 200 R SYM FOR SHELL (I) : 0.41300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1TEY, PDB ENTRY 1KX3 CHAIN A AND B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.05M CADMIUM SULFATE
REMARK 280 HYDRATE, 1.0M SODIUM ACETATE TRYHYDRATE, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.24000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.24000
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 48.68050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 52.39000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 48.68050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 52.39000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.24000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 48.68050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 52.39000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.24000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 48.68050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 52.39000
REMARK 290 SMTRY3 8 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETERO TRIMER OF CIA-H3-H4
REMARK 300 OBSEREVED IN THE ASYMMETRIC UNIT.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ASP A 155
REMARK 465 ASN A 156
REMARK 465 THR A 157
REMARK 465 GLU A 158
REMARK 465 LYS A 159
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 ASP A 162
REMARK 465 ALA A 163
REMARK 465 GLU A 164
REMARK 465 SER A 165
REMARK 465 SER A 166
REMARK 465 ASN A 167
REMARK 465 PRO A 168
REMARK 465 ASN A 169
REMARK 465 LEU A 170
REMARK 465 GLN A 171
REMARK 465 SER A 172
REMARK 465 ALA B 1
REMARK 465 ARG B 2
REMARK 465 THR B 3
REMARK 465 LYS B 4
REMARK 465 GLN B 5
REMARK 465 THR B 6
REMARK 465 ALA B 7
REMARK 465 ARG B 8
REMARK 465 LYS B 9
REMARK 465 SER B 10
REMARK 465 THR B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 LYS B 14
REMARK 465 ALA B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 LYS B 18
REMARK 465 GLN B 19
REMARK 465 LEU B 20
REMARK 465 ALA B 21
REMARK 465 THR B 22
REMARK 465 LYS B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 ARG B 26
REMARK 465 LYS B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 PRO B 30
REMARK 465 ALA B 31
REMARK 465 THR B 32
REMARK 465 GLY B 33
REMARK 465 GLY B 34
REMARK 465 VAL B 35
REMARK 465 LYS B 36
REMARK 465 LYS B 37
REMARK 465 PRO B 38
REMARK 465 HIS B 39
REMARK 465 ARG B 40
REMARK 465 TYR B 41
REMARK 465 ARG B 42
REMARK 465 PRO B 43
REMARK 465 GLY B 44
REMARK 465 THR B 45
REMARK 465 VAL B 46
REMARK 465 ALA B 47
REMARK 465 LEU B 48
REMARK 465 ARG B 49
REMARK 465 GLU B 50
REMARK 465 ILE B 51
REMARK 465 ARG B 52
REMARK 465 ARG B 53
REMARK 465 TYR B 54
REMARK 465 GLN B 55
REMARK 465 LYS B 56
REMARK 465 SER B 57
REMARK 465 THR B 58
REMARK 465 GLU B 59
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 GLY C 9
REMARK 465 LEU C 10
REMARK 465 GLY C 11
REMARK 465 LYS C 12
REMARK 465 GLY C 13
REMARK 465 GLY C 14
REMARK 465 ALA C 15
REMARK 465 LYS C 16
REMARK 465 ARG C 17
REMARK 465 HIS C 18
REMARK 465 ARG C 19
REMARK 465 LYS C 20
REMARK 465 VAL C 21
REMARK 465 LEU C 22
REMARK 465 ARG C 23
REMARK 465 GLY C 101
REMARK 465 GLY C 102
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 13 53.87 33.57
REMARK 500 SER A 35 -63.12 -102.94
REMARK 500 THR A 93 -151.33 -130.21
REMARK 500 ASN A 125 76.59 -105.34
REMARK 500 LEU B 82 136.21 -171.78
REMARK 500 PHE B 84 -151.60 -111.85
REMARK 500 ALA B 114 -169.79 -78.32
REMARK 500 LYS C 77 -8.73 69.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2IO5 A 1 172 UNP Q6IA08 Q6IA08_HUMAN 1 172
DBREF 2IO5 B 1 135 UNP P84233 H31_XENLA 1 135
DBREF 2IO5 C 1 102 UNP P62799 H4_XENLA 1 102
SEQADV 2IO5 GLY A -2 UNP Q6IA08 CLONING ARTIFACT
SEQADV 2IO5 SER A -1 UNP Q6IA08 CLONING ARTIFACT
SEQADV 2IO5 HIS A 0 UNP Q6IA08 CLONING ARTIFACT
SEQRES 1 A 175 GLY SER HIS MET ALA LYS VAL GLN VAL ASN ASN VAL VAL
SEQRES 2 A 175 VAL LEU ASP ASN PRO SER PRO PHE TYR ASN PRO PHE GLN
SEQRES 3 A 175 PHE GLU ILE THR PHE GLU CYS ILE GLU ASP LEU SER GLU
SEQRES 4 A 175 ASP LEU GLU TRP LYS ILE ILE TYR VAL GLY SER ALA GLU
SEQRES 5 A 175 SER GLU GLU TYR ASP GLN VAL LEU ASP SER VAL LEU VAL
SEQRES 6 A 175 GLY PRO VAL PRO ALA GLY ARG HIS MET PHE VAL PHE GLN
SEQRES 7 A 175 ALA ASP ALA PRO ASN PRO GLY LEU ILE PRO ASP ALA ASP
SEQRES 8 A 175 ALA VAL GLY VAL THR VAL VAL LEU ILE THR CYS THR TYR
SEQRES 9 A 175 ARG GLY GLN GLU PHE ILE ARG VAL GLY TYR TYR VAL ASN
SEQRES 10 A 175 ASN GLU TYR THR GLU THR GLU LEU ARG GLU ASN PRO PRO
SEQRES 11 A 175 VAL LYS PRO ASP PHE SER LYS LEU GLN ARG ASN ILE LEU
SEQRES 12 A 175 ALA SER ASN PRO ARG VAL THR ARG PHE HIS ILE ASN TRP
SEQRES 13 A 175 GLU ASP ASN THR GLU LYS LEU GLU ASP ALA GLU SER SER
SEQRES 14 A 175 ASN PRO ASN LEU GLN SER
SEQRES 1 B 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 B 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 B 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 B 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 B 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 B 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 B 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 B 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL GLY LEU PHE
SEQRES 9 B 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 B 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 B 135 ARG GLY GLU ARG ALA
SEQRES 1 C 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 C 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 C 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 C 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 C 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 C 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 C 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 C 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
HELIX 1 1 SER A 50 GLU A 52 5 3
HELIX 2 2 ASN A 80 ILE A 84 5 5
HELIX 3 3 PRO A 85 VAL A 90 1 6
HELIX 4 4 GLU A 119 ASN A 125 1 7
HELIX 5 5 ASP A 131 SER A 133 5 3
HELIX 6 6 ARG B 63 LYS B 79 1 17
HELIX 7 7 GLN B 85 ALA B 114 1 30
HELIX 8 8 MET B 120 GLY B 132 1 13
HELIX 9 9 THR C 30 GLY C 41 1 12
HELIX 10 10 LEU C 49 HIS C 75 1 27
HELIX 11 11 THR C 82 ARG C 92 1 11
SHEET 1 A 3 VAL A 4 VAL A 11 0
SHEET 2 A 3 PHE A 22 CYS A 30 -1 O GLU A 29 N GLN A 5
SHEET 3 A 3 GLY A 68 ALA A 76 -1 O GLY A 68 N CYS A 30
SHEET 1 B 6 SER A 16 PRO A 17 0
SHEET 2 B 6 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 B 6 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 B 6 GLY A 91 TYR A 101 -1 N ILE A 97 O VAL A 109
SHEET 5 B 6 LEU A 38 VAL A 45 -1 N VAL A 45 O VAL A 94
SHEET 6 B 6 ASP A 54 VAL A 62 -1 O VAL A 60 N TRP A 40
SHEET 1 C 5 SER A 16 PRO A 17 0
SHEET 2 C 5 LEU A 135 ILE A 139 -1 O ARG A 137 N SER A 16
SHEET 3 C 5 GLN A 104 TYR A 117 -1 N GLU A 116 O GLN A 136
SHEET 4 C 5 ARG A 145 ARG A 148 -1 O THR A 147 N ARG A 108
SHEET 5 C 5 ARG C 95 LEU C 97 -1 O LEU C 97 N VAL A 146
SHEET 1 D 2 THR B 118 ILE B 119 0
SHEET 2 D 2 ARG C 45 ILE C 46 1 O ARG C 45 N ILE B 119
CISPEP 1 ASN A 14 PRO A 15 0 -3.66
CISPEP 2 GLY A 63 PRO A 64 0 -8.22
CRYST1 97.361 104.780 86.480 90.00 90.00 90.00 C 2 2 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 0.010271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009544 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
