HEADER TRANSCRIPTION 27-AUG-10 2XPO
TITLE CRYSTAL STRUCTURE OF A SPT6-IWS1(SPN1) COMPLEX FROM ENCEPHALITOZOON
TITLE 2 CUNICULI, FORM II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IWS1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: EVOLUTIONARY CONSERVED DOMAIN, RESIDUES 55-198;
COMPND 5 SYNONYM: ECU08_0440;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CHROMATIN STRUCTURE MODULATOR;
COMPND 9 CHAIN: B, D;
COMPND 10 FRAGMENT: N-TERMINAL FRAGMENT, RESIDUES 53-71;
COMPND 11 SYNONYM: SPT6;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENCEPHALITOZOON CUNICULI;
SOURCE 3 ORGANISM_TAXID: 6035;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET-MCN;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNCS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ENCEPHALITOZOON CUNICULI;
SOURCE 11 ORGANISM_TAXID: 6035;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PET-MCN;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PNEA-TH
KEYWDS TRANSCRIPTION, ELONGATION, HISTONE CHAPERONE, RNA POLYMERASE II, MRNA
KEYWDS 2 EXPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.-L.DIEBOLD,M.KOCH,V.CURA,D.MORAS,J.CAVARELLI,C.ROMIER
REVDAT 3 20-DEC-23 2XPO 1 REMARK
REVDAT 2 21-SEP-11 2XPO 1 JRNL REMARK
REVDAT 1 17-NOV-10 2XPO 0
JRNL AUTH M.-L.DIEBOLD,M.KOCH,E.LOELIGER,V.CURA,F.WINSTON,J.CAVARELLI,
JRNL AUTH 2 C.ROMIER
JRNL TITL THE STRUCTURE OF AN IWS1/SPT6 COMPLEX REVEALS AN INTERACTION
JRNL TITL 2 DOMAIN CONSERVED IN TFIIS, ELONGIN A AND MED26
JRNL REF EMBO J. V. 29 3979 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 21057455
JRNL DOI 10.1038/EMBOJ.2010.272
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 20780
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1124
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1485
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2450
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 : 2
REMARK 3 SOLVENT ATOMS : 151
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.95000
REMARK 3 B22 (A**2) : -0.95000
REMARK 3 B33 (A**2) : 1.42000
REMARK 3 B12 (A**2) : -0.47000
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): 0.203
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.188
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2512 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3369 ; 1.639 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 303 ; 4.835 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;37.164 ;25.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;15.133 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;21.235 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 380 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1800 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1525 ; 0.770 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2472 ; 1.379 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 987 ; 2.754 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 897 ; 4.529 ; 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 : 4
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 54 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0492 -25.2957 0.8511
REMARK 3 T TENSOR
REMARK 3 T11: 0.0704 T22: 0.0600
REMARK 3 T33: 0.0280 T12: -0.0032
REMARK 3 T13: 0.0277 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 2.7098 L22: 2.8649
REMARK 3 L33: 1.9420 L12: 0.1060
REMARK 3 L13: 0.6999 L23: 0.1020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: -0.0352 S13: 0.0328
REMARK 3 S21: 0.0292 S22: 0.0358 S23: 0.1599
REMARK 3 S31: -0.0348 S32: -0.1651 S33: 0.0150
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 53 B 67
REMARK 3 ORIGIN FOR THE GROUP (A): -32.3544 -40.3745 -5.2229
REMARK 3 T TENSOR
REMARK 3 T11: 0.2618 T22: 0.1375
REMARK 3 T33: 0.2272 T12: -0.0472
REMARK 3 T13: 0.0621 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 28.5688 L22: 9.4414
REMARK 3 L33: 3.3933 L12: -3.3124
REMARK 3 L13: 2.0807 L23: 2.0024
REMARK 3 S TENSOR
REMARK 3 S11: -0.0844 S12: 0.4057 S13: -2.1426
REMARK 3 S21: 0.0079 S22: 0.3742 S23: 0.2363
REMARK 3 S31: 0.4457 S32: 0.0163 S33: -0.2898
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 54 C 192
REMARK 3 ORIGIN FOR THE GROUP (A): -35.5234 -15.2284 26.0902
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.0926
REMARK 3 T33: 0.0319 T12: -0.0002
REMARK 3 T13: 0.0021 T23: -0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 2.6941 L22: 3.1223
REMARK 3 L33: 1.8673 L12: -0.2671
REMARK 3 L13: -0.0816 L23: -0.9106
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.0657 S13: -0.1686
REMARK 3 S21: -0.1183 S22: 0.0591 S23: 0.1107
REMARK 3 S31: 0.1469 S32: -0.0948 S33: -0.0815
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 53 D 66
REMARK 3 ORIGIN FOR THE GROUP (A): -50.2780 -11.8690 32.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.5220
REMARK 3 T33: 0.3323 T12: -0.0440
REMARK 3 T13: 0.0296 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 5.1962 L22: 27.5215
REMARK 3 L33: 4.0823 L12: 9.1064
REMARK 3 L13: -2.9860 L23: 0.0294
REMARK 3 S TENSOR
REMARK 3 S11: 0.4880 S12: -0.4894 S13: 0.7440
REMARK 3 S21: 0.2835 S22: -0.5078 S23: 2.1760
REMARK 3 S31: -0.3347 S32: 0.0487 S33: 0.0198
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. U VALUES WITH TLS ADDED. ATOM RECORD CONTAINS SUM OF
REMARK 3 TLS AND RESIDUAL B FACTORS.
REMARK 4
REMARK 4 2XPO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1290040929.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21935
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.47
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: PDB ENTRY 2XPL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE 18% PEG1500 0.05
REMARK 280 M MGCL2, PH 5
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 34.32067
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 17.16033
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 25.74050
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 8.58017
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 42.90083
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 LYS A 193
REMARK 465 PRO A 194
REMARK 465 GLU A 195
REMARK 465 GLY A 196
REMARK 465 GLY A 197
REMARK 465 ASP A 198
REMARK 465 GLY B 49
REMARK 465 SER B 50
REMARK 465 HIS B 51
REMARK 465 MET B 52
REMARK 465 GLU B 68
REMARK 465 SER B 69
REMARK 465 ASP B 70
REMARK 465 PRO B 71
REMARK 465 LYS C 193
REMARK 465 PRO C 194
REMARK 465 GLU C 195
REMARK 465 GLY C 196
REMARK 465 GLY C 197
REMARK 465 ASP C 198
REMARK 465 GLY D 49
REMARK 465 SER D 50
REMARK 465 HIS D 51
REMARK 465 MET D 52
REMARK 465 LEU D 67
REMARK 465 GLU D 68
REMARK 465 SER D 69
REMARK 465 ASP D 70
REMARK 465 PRO D 71
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 LYS A 129 -1.18 77.71
REMARK 500 LYS C 129 -3.20 76.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XPN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A SPT6-IWS1(SPN1) COMPLEX FROM ENCEPHALITOZOON
REMARK 900 CUNICULI, FORM I
REMARK 900 RELATED ID: 2XPP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A SPT6-IWS1(SPN1) COMPLEX FROM ENCEPHALITOZOON
REMARK 900 CUNICULI, FORM III
REMARK 900 RELATED ID: 2XPL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF IWS1(SPN1) CONSERVED DOMAIN FROM
REMARK 900 ENCEPHALITOZOON CUNICULI
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 B, D 49-50 PART OF THROMBIN CLEAVAGE SITE.
REMARK 999 B, D 51-52 PART OF NDEI CLONING SITE.
DBREF 2XPO A 55 198 UNP Q8SUS7 Q8SUS7_ENCCU 55 198
DBREF 2XPO B 53 71 UNP Q8SRG7 Q8SRG7_ENCCU 53 71
DBREF 2XPO C 55 198 UNP Q8SUS7 Q8SUS7_ENCCU 55 198
DBREF 2XPO D 53 71 UNP Q8SRG7 Q8SRG7_ENCCU 53 71
SEQADV 2XPO MET A 54 UNP Q8SUS7 EXPRESSION TAG
SEQADV 2XPO GLY B 49 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO SER B 50 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO HIS B 51 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO MET B 52 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO MET C 54 UNP Q8SUS7 EXPRESSION TAG
SEQADV 2XPO GLY D 49 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO SER D 50 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO HIS D 51 UNP Q8SRG7 SEE REMARK 999
SEQADV 2XPO MET D 52 UNP Q8SRG7 SEE REMARK 999
SEQRES 1 A 145 MET ASP PRO GLY THR VAL LEU GLU ILE SER ARG SER LEU
SEQRES 2 A 145 LYS LYS ARG MET GLN ASP ILE LEU LYS LYS ASP ASN ALA
SEQRES 3 A 145 ASN ASN LEU GLU GLY ARG PRO ALA THR GLY LYS ILE GLU
SEQRES 4 A 145 ASN VAL GLU GLU ILE SER ASP ILE LEU MET SER LYS ALA
SEQRES 5 A 145 LEU GLN GLU SER LEU LEU ASP GLU GLY ILE LEU ASP GLU
SEQRES 6 A 145 ILE LYS GLY TRP LEU GLU PRO LEU PRO ASP LYS SER MET
SEQRES 7 A 145 PRO ASN ILE LYS ILE ARG LYS ARG LEU LEU ASP VAL LEU
SEQRES 8 A 145 LYS THR MET LYS ILE HIS LYS GLU HIS LEU VAL THR SER
SEQRES 9 A 145 GLY VAL GLY LYS ILE VAL TYR PHE TYR SER ILE ASN PRO
SEQRES 10 A 145 LYS GLU SER LYS GLU VAL ARG ALA SER ALA LYS ALA LEU
SEQRES 11 A 145 VAL GLN LYS TRP THR ASN GLU VAL PHE LYS PRO GLU GLY
SEQRES 12 A 145 GLY ASP
SEQRES 1 B 23 GLY SER HIS MET PHE PHE GLU ILE PHE GLY THR GLY GLU
SEQRES 2 B 23 GLU TYR ARG TYR VAL LEU GLU SER ASP PRO
SEQRES 1 C 145 MET ASP PRO GLY THR VAL LEU GLU ILE SER ARG SER LEU
SEQRES 2 C 145 LYS LYS ARG MET GLN ASP ILE LEU LYS LYS ASP ASN ALA
SEQRES 3 C 145 ASN ASN LEU GLU GLY ARG PRO ALA THR GLY LYS ILE GLU
SEQRES 4 C 145 ASN VAL GLU GLU ILE SER ASP ILE LEU MET SER LYS ALA
SEQRES 5 C 145 LEU GLN GLU SER LEU LEU ASP GLU GLY ILE LEU ASP GLU
SEQRES 6 C 145 ILE LYS GLY TRP LEU GLU PRO LEU PRO ASP LYS SER MET
SEQRES 7 C 145 PRO ASN ILE LYS ILE ARG LYS ARG LEU LEU ASP VAL LEU
SEQRES 8 C 145 LYS THR MET LYS ILE HIS LYS GLU HIS LEU VAL THR SER
SEQRES 9 C 145 GLY VAL GLY LYS ILE VAL TYR PHE TYR SER ILE ASN PRO
SEQRES 10 C 145 LYS GLU SER LYS GLU VAL ARG ALA SER ALA LYS ALA LEU
SEQRES 11 C 145 VAL GLN LYS TRP THR ASN GLU VAL PHE LYS PRO GLU GLY
SEQRES 12 C 145 GLY ASP
SEQRES 1 D 23 GLY SER HIS MET PHE PHE GLU ILE PHE GLY THR GLY GLU
SEQRES 2 D 23 GLU TYR ARG TYR VAL LEU GLU SER ASP PRO
HET CL A 200 1
HET CL C 200 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *151(H2 O)
HELIX 1 1 GLY A 57 GLU A 83 1 27
HELIX 2 2 THR A 88 MET A 102 1 15
HELIX 3 3 SER A 103 ALA A 105 5 3
HELIX 4 4 LEU A 106 GLU A 113 1 8
HELIX 5 5 GLY A 114 GLU A 124 1 11
HELIX 6 6 ASN A 133 MET A 147 1 15
HELIX 7 7 HIS A 150 GLY A 158 1 9
HELIX 8 8 GLY A 158 ASN A 169 1 12
HELIX 9 9 SER A 173 PHE A 192 1 20
HELIX 10 10 PHE B 53 GLY B 58 1 6
HELIX 11 11 TYR B 63 LEU B 67 5 5
HELIX 12 12 GLY C 57 GLU C 83 1 27
HELIX 13 13 THR C 88 MET C 102 1 15
HELIX 14 14 SER C 103 ALA C 105 5 3
HELIX 15 15 LEU C 106 GLU C 113 1 8
HELIX 16 16 GLY C 114 GLU C 124 1 11
HELIX 17 17 ASN C 133 MET C 147 1 15
HELIX 18 18 HIS C 150 GLY C 158 1 9
HELIX 19 19 GLY C 158 ASN C 169 1 12
HELIX 20 20 SER C 173 PHE C 192 1 20
HELIX 21 21 PHE D 53 GLY D 58 1 6
SITE 1 AC1 5 PRO A 132 ASN A 133 ILE A 136 HOH A2018
SITE 2 AC1 5 HOH A2022
SITE 1 AC2 5 LYS C 90 ASN C 133 ILE C 136 HOH C2016
SITE 2 AC2 5 HOH C2018
CRYST1 112.578 112.578 51.481 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 0.008883 0.005128 0.000000 0.00000
SCALE2 0.000000 0.010257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019425 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
