HEADER HYDROLASE 04-AUG-06 2J0U
TITLE THE CRYSTAL STRUCTURE OF EIF4AIII-BARENTSZ COMPLEX AT 3.0 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX48;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 37-410;
COMPND 5 SYNONYM: EIF4AIII RNA-HELICASE, DEAD BOX PROTEIN 48, EUKARYOTIC
COMPND 6 INITIATION FACTOR 4A-LIKE NUK-34, NUCLEAR MATRIX PROTEIN 265, HNMP
COMPND 7 265, EUKARYOTIC TRANSLATION INITIATION FACTOR 4A ISOFORM 3;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX48;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 37-410;
COMPND 13 SYNONYM: EIF4AIII RNA-HELICASE, DEAD BOX PROTEIN 48, EUKARYOTIC
COMPND 14 INITIATION FACTOR 4A-LIKE NUK-34, NUCLEAR MATRIX PROTEIN 265, HNMP
COMPND 15 265, EUKARYOTIC TRANSLATION INITIATION FACTOR 4A ISOFORM 3;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 3;
COMPND 18 MOLECULE: PROTEIN CASC3;
COMPND 19 CHAIN: T;
COMPND 20 FRAGMENT: RESIDUES 137-250;
COMPND 21 SYNONYM: BARENTSZ, CANCER SUSCEPTIBILITY CANDIDATE GENE 3 PROTEIN,
COMPND 22 METASTATIC LYMPH NODE PROTEIN 51, MLN 51 PROTEIN, BARENTSZ PROTEIN,
COMPND 23 BTZ;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PETMCN;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PETMCN;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 23 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 24 EXPRESSION_SYSTEM_VECTOR: PETMCN
KEYWDS HYDROLASE, ATP-BINDING, DNA-BINDING, NUCLEAR PROTEIN, RRNA
KEYWDS 2 PROCESSING, DEAD-BOX HELICASE, NUCLEOTIDE-BINDING, EJC, HELICASE,
KEYWDS 3 RNA-BINDING, ACETYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.BONO,J.EBERT,E.LORENTZEN,E.CONTI
REVDAT 3 13-DEC-23 2J0U 1 REMARK
REVDAT 2 24-FEB-09 2J0U 1 VERSN
REVDAT 1 06-SEP-06 2J0U 0
JRNL AUTH F.BONO,J.EBERT,E.LORENTZEN,E.CONTI
JRNL TITL THE CRYSTAL STRUCTURE OF THE EXON JUNCTION COMPLEX REVEALS
JRNL TITL 2 HOW IT MANTAINS A STABLE GRIP ON MRNA
JRNL REF CELL(CAMBRIDGE,MASS.) V. 126 713 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16923391
JRNL DOI 10.1016/J.CELL.2006.08.006
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : 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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17157
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) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 903
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1118
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3570
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.4340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5139
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.80000
REMARK 3 B22 (A**2) : 1.18000
REMARK 3 B33 (A**2) : -1.98000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.548
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.523
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 62.301
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.879
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.814
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5219 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4975 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7128 ; 1.436 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11376 ; 0.959 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 713 ; 9.886 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;38.067 ;23.676
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 719 ;19.879 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;19.633 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 876 ; 0.135 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5992 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1055 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1460 ; 0.258 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5331 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2658 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3207 ; 0.091 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 169 ; 0.186 ; 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): 20 ; 0.183 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 77 ; 0.256 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.170 ; 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): 4525 ; 0.457 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5615 ; 0.533 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1877 ; 0.716 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1513 ; 1.110 ; 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 : 7
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 38 A 138 1
REMARK 3 1 B 38 B 138 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1292 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 1292 ; 0.06 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 150 A 195 1
REMARK 3 1 B 150 B 195 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 523 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 523 ; 0.05 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 280 A 295 1
REMARK 3 1 B 280 B 295 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 212 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 3 A (A**2): 212 ; 0.04 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 316 A 331 1
REMARK 3 1 B 316 B 331 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 A (A): 119 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 4 A (A**2): 119 ; 0.05 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 346 A 365 1
REMARK 3 1 B 346 B 365 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 5 A (A): 340 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 5 A (A**2): 340 ; 0.06 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 199 A 270 1
REMARK 3 1 B 199 B 270 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 6 A (A): 914 ; 0.06 ; 0.05
REMARK 3 TIGHT THERMAL 6 A (A**2): 914 ; 0.07 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 378 A 405 1
REMARK 3 1 B 378 B 405 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 7 A (A): 356 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 7 A (A**2): 356 ; 0.05 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2J0U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1290029574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18221
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.22000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 1FUU, 1FUK, 1P27
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 700 MM DI AMMONIUM TARTRATE, 100 MM NA
REMARK 280 ACETATE PH 4.6
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 121.97500
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 121.97500
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 35.88000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.59500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.88000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.59500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 121.97500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.88000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.59500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 121.97500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.88000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.59500
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 THR A 274
REMARK 465 LEU A 275
REMARK 465 THR A 276
REMARK 465 GLY A 340
REMARK 465 LEU A 341
REMARK 465 ASP A 409
REMARK 465 LEU A 410
REMARK 465 ILE A 411
REMARK 465 GLY B 142
REMARK 465 GLY B 143
REMARK 465 THR B 144
REMARK 465 ASN B 145
REMARK 465 VAL B 146
REMARK 465 ALA B 300
REMARK 465 ASN B 301
REMARK 465 PHE B 302
REMARK 465 SER B 306
REMARK 465 MET B 307
REMARK 465 HIS B 308
REMARK 465 GLY B 309
REMARK 465 ASP B 310
REMARK 465 MET B 311
REMARK 465 PRO B 312
REMARK 465 ASP B 335
REMARK 465 VAL B 336
REMARK 465 TRP B 337
REMARK 465 ALA B 338
REMARK 465 ARG B 339
REMARK 465 GLY B 340
REMARK 465 LEU B 341
REMARK 465 ASP B 342
REMARK 465 ALA B 408
REMARK 465 ASP B 409
REMARK 465 LEU B 410
REMARK 465 ILE B 411
REMARK 465 ASP T 137
REMARK 465 THR T 138
REMARK 465 LYS T 139
REMARK 465 SER T 140
REMARK 465 THR T 141
REMARK 465 VAL T 142
REMARK 465 THR T 143
REMARK 465 GLY T 144
REMARK 465 GLU T 145
REMARK 465 ARG T 146
REMARK 465 GLN T 147
REMARK 465 SER T 148
REMARK 465 GLY T 149
REMARK 465 ASP T 150
REMARK 465 GLY T 151
REMARK 465 GLN T 152
REMARK 465 GLU T 153
REMARK 465 SER T 154
REMARK 465 THR T 155
REMARK 465 GLU T 156
REMARK 465 PRO T 157
REMARK 465 VAL T 158
REMARK 465 GLU T 159
REMARK 465 ASN T 160
REMARK 465 LYS T 161
REMARK 465 VAL T 162
REMARK 465 GLY T 163
REMARK 465 LYS T 164
REMARK 465 LYS T 165
REMARK 465 GLY T 166
REMARK 465 PRO T 167
REMARK 465 LYS T 168
REMARK 465 HIS T 169
REMARK 465 LEU T 170
REMARK 465 ASP T 171
REMARK 465 ASP T 172
REMARK 465 ASP T 173
REMARK 465 GLU T 174
REMARK 465 ASP T 175
REMARK 465 ARG T 176
REMARK 465 LYS T 177
REMARK 465 ASN T 178
REMARK 465 PRO T 179
REMARK 465 ALA T 180
REMARK 465 TYR T 181
REMARK 465 ILE T 182
REMARK 465 PRO T 183
REMARK 465 ARG T 184
REMARK 465 LYS T 185
REMARK 465 GLY T 186
REMARK 465 LEU T 187
REMARK 465 PHE T 188
REMARK 465 PHE T 189
REMARK 465 GLU T 190
REMARK 465 HIS T 191
REMARK 465 ASP T 192
REMARK 465 LEU T 193
REMARK 465 ARG T 194
REMARK 465 GLY T 195
REMARK 465 GLN T 196
REMARK 465 THR T 197
REMARK 465 GLN T 198
REMARK 465 GLU T 199
REMARK 465 GLU T 200
REMARK 465 GLU T 201
REMARK 465 VAL T 202
REMARK 465 ARG T 203
REMARK 465 PRO T 204
REMARK 465 LYS T 205
REMARK 465 GLY T 206
REMARK 465 ARG T 207
REMARK 465 GLN T 208
REMARK 465 ARG T 209
REMARK 465 LYS T 210
REMARK 465 LEU T 211
REMARK 465 TRP T 212
REMARK 465 LYS T 213
REMARK 465 ASP T 214
REMARK 465 GLU T 215
REMARK 465 GLY T 216
REMARK 465 ASP T 226
REMARK 465 GLU T 227
REMARK 465 GLN T 228
REMARK 465 ALA T 229
REMARK 465 PRO T 230
REMARK 465 LYS T 231
REMARK 465 SER T 232
REMARK 465 ARG T 233
REMARK 465 GLN T 234
REMARK 465 GLU T 235
REMARK 465 LEU T 236
REMARK 465 ILE T 237
REMARK 465 ALA T 238
REMARK 465 LEU T 239
REMARK 465 TYR T 240
REMARK 465 GLY T 241
REMARK 465 TYR T 242
REMARK 465 ASP T 243
REMARK 465 ILE T 244
REMARK 465 ARG T 245
REMARK 465 SER T 246
REMARK 465 ALA T 247
REMARK 465 HIS T 248
REMARK 465 ASN T 249
REMARK 465 PRO T 250
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 THR A 39 OG1 CG2
REMARK 470 GLU A 47 CG CD OE1 OE2
REMARK 470 ARG A 51 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 LYS A 60 CG CD CE NZ
REMARK 470 SER A 84 OG
REMARK 470 CYS A 99 SG
REMARK 470 ASP A 101 CG OD1 OD2
REMARK 470 GLN A 103 CG CD OE1 NE2
REMARK 470 VAL A 104 CG1 CG2
REMARK 470 ARG A 105 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 ARG A 116 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 134 CG OD1 ND2
REMARK 470 VAL A 135 CG1 CG2
REMARK 470 GLN A 136 CG CD OE1 NE2
REMARK 470 ILE A 141 CG1 CG2 CD1
REMARK 470 THR A 144 OG1 CG2
REMARK 470 ASN A 145 CG OD1 ND2
REMARK 470 VAL A 146 CG1 CG2
REMARK 470 GLU A 148 CG CD OE1 OE2
REMARK 470 ILE A 150 CG1 CG2 CD1
REMARK 470 ARG A 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 152 CG CD CE NZ
REMARK 470 TYR A 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 169 CG OD1 OD2
REMARK 470 ARG A 173 CG CD NE CZ NH1 NH2
REMARK 470 SER A 175 OG
REMARK 470 ARG A 177 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 179 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 182 CG CD CE NZ
REMARK 470 ASP A 190 CG OD1 OD2
REMARK 470 GLU A 191 CG CD OE1 OE2
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 GLU A 224 CG CD OE1 OE2
REMARK 470 GLU A 227 CG CD OE1 OE2
REMARK 470 LYS A 231 CG CD CE NZ
REMARK 470 LYS A 242 CG CD CE NZ
REMARK 470 THR A 247 OG1 CG2
REMARK 470 GLU A 249 CG CD OE1 OE2
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 ARG A 260 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 262 CG CD OE1 OE2
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 PHE A 265 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 279 CG CD OE1 NE2
REMARK 470 LYS A 287 CG CD CE NZ
REMARK 470 ARG A 288 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 LYS A 296 CG CD CE NZ
REMARK 470 MET A 297 CG SD CE
REMARK 470 PHE A 302 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 310 CG OD1 OD2
REMARK 470 GLN A 313 CG CD OE1 NE2
REMARK 470 LYS A 314 CG CD CE NZ
REMARK 470 GLU A 322 CG CD OE1 OE2
REMARK 470 PHE A 323 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 324 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 336 CG1 CG2
REMARK 470 TRP A 337 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 337 CZ3 CH2
REMARK 470 ARG A 339 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 342 CG OD1 OD2
REMARK 470 ARG A 373 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 374 CG CD CE NZ
REMARK 470 ASP A 385 CG OD1 OD2
REMARK 470 ARG A 390 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 399 CG CD OE1 NE2
REMARK 470 MET A 405 CG SD CE
REMARK 470 ASN A 406 CG OD1 ND2
REMARK 470 VAL A 407 CG1 CG2
REMARK 470 THR B 39 OG1 CG2
REMARK 470 GLU B 47 CG CD OE1 OE2
REMARK 470 ASP B 48 CG OD1 OD2
REMARK 470 ARG B 51 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 SER B 84 OG
REMARK 470 GLN B 103 CG CD OE1 NE2
REMARK 470 VAL B 104 CG1 CG2
REMARK 470 ARG B 105 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 THR B 115 OG1 CG2
REMARK 470 GLU B 117 CG CD OE1 OE2
REMARK 470 GLN B 121 CG CD OE1 NE2
REMARK 470 ASN B 134 CG OD1 ND2
REMARK 470 VAL B 135 CG1 CG2
REMARK 470 CYS B 140 SG
REMARK 470 ILE B 141 CG1 CG2 CD1
REMARK 470 GLU B 148 CG CD OE1 OE2
REMARK 470 ASP B 149 CG OD1 OD2
REMARK 470 ILE B 150 CG1 CG2 CD1
REMARK 470 ARG B 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 152 CG CD CE NZ
REMARK 470 LEU B 153 CG CD1 CD2
REMARK 470 ASP B 154 CG OD1 OD2
REMARK 470 TYR B 155 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 166 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 169 CG OD1 OD2
REMARK 470 ARG B 172 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 173 CG CD NE CZ NH1 NH2
REMARK 470 SER B 175 OG
REMARK 470 ARG B 177 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 179 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 182 CG CD CE NZ
REMARK 470 ASP B 190 CG OD1 OD2
REMARK 470 GLU B 191 CG CD OE1 OE2
REMARK 470 LEU B 193 CG CD1 CD2
REMARK 470 ASN B 194 CG OD1 ND2
REMARK 470 LYS B 195 CG CD CE NZ
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 GLU B 199 CG CD OE1 OE2
REMARK 470 GLU B 224 CG CD OE1 OE2
REMARK 470 LEU B 226 CG CD1 CD2
REMARK 470 GLU B 227 CG CD OE1 OE2
REMARK 470 ASN B 230 CG OD1 ND2
REMARK 470 LYS B 231 CG CD CE NZ
REMARK 470 ARG B 238 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 242 CG CD CE NZ
REMARK 470 ASP B 244 CG OD1 OD2
REMARK 470 GLU B 245 CG CD OE1 OE2
REMARK 470 THR B 247 OG1 CG2
REMARK 470 LEU B 248 CG CD1 CD2
REMARK 470 GLU B 249 CG CD OE1 OE2
REMARK 470 LYS B 252 CG CD CE NZ
REMARK 470 GLU B 259 CG CD OE1 OE2
REMARK 470 ARG B 260 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 262 CG CD OE1 OE2
REMARK 470 LYS B 264 CG CD CE NZ
REMARK 470 LEU B 268 CG CD1 CD2
REMARK 470 LEU B 271 CG CD1 CD2
REMARK 470 THR B 276 OG1 CG2
REMARK 470 THR B 278 OG1 CG2
REMARK 470 GLN B 279 CG CD OE1 NE2
REMARK 470 ASN B 285 CG OD1 ND2
REMARK 470 LYS B 287 CG CD CE NZ
REMARK 470 ARG B 288 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 289 CG CD CE NZ
REMARK 470 GLU B 295 CG CD OE1 OE2
REMARK 470 LYS B 296 CG CD CE NZ
REMARK 470 MET B 297 CG SD CE
REMARK 470 VAL B 304 CG1 CG2
REMARK 470 SER B 305 OG
REMARK 470 GLN B 313 CG CD OE1 NE2
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 GLU B 315 CG CD OE1 OE2
REMARK 470 ARG B 316 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 317 CG CD OE1 OE2
REMARK 470 LYS B 321 CG CD CE NZ
REMARK 470 GLU B 322 CG CD OE1 OE2
REMARK 470 PHE B 323 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 324 CG CD NE CZ NH1 NH2
REMARK 470 SER B 325 OG
REMARK 470 ARG B 329 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 331 CG CD1 CD2
REMARK 470 ILE B 332 CG1 CG2 CD1
REMARK 470 VAL B 343 CG1 CG2
REMARK 470 GLN B 345 CG CD OE1 NE2
REMARK 470 SER B 368 OG
REMARK 470 ARG B 370 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 373 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 374 CG CD CE NZ
REMARK 470 LYS B 382 CG CD CE NZ
REMARK 470 ASP B 385 CG OD1 OD2
REMARK 470 ARG B 387 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 390 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 391 CG OD1 OD2
REMARK 470 GLN B 399 CG CD OE1 NE2
REMARK 470 GLU B 402 CG CD OE1 OE2
REMARK 470 MET B 405 CG SD CE
REMARK 470 ARG T 217 CG CD NE CZ NH1 NH2
REMARK 470 LYS T 222 CG CD CE NZ
REMARK 470 ARG T 224 CG CD NE CZ NH1 NH2
REMARK 470 GLU T 225 CG CD OE1 OE2
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 O ARG B 370 N GLY B 372 2.02
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 LYS A 60 134.98 -19.33
REMARK 500 THR A 86 -83.38 -9.73
REMARK 500 VAL A 104 99.91 -64.39
REMARK 500 ARG A 105 40.09 -90.47
REMARK 500 HIS A 138 141.41 -170.04
REMARK 500 CYS A 140 92.37 -67.14
REMARK 500 ALA A 211 94.81 -53.65
REMARK 500 MET A 228 -56.22 -22.02
REMARK 500 ASP A 235 54.99 32.20
REMARK 500 ALA A 257 99.08 -65.56
REMARK 500 GLU A 262 69.18 -150.32
REMARK 500 THR A 278 -137.97 -89.76
REMARK 500 ASP A 310 44.30 -75.58
REMARK 500 ALA A 327 0.57 -56.31
REMARK 500 VAL A 336 -69.12 34.53
REMARK 500 PRO A 344 116.89 -31.52
REMARK 500 GLN A 345 108.64 -44.79
REMARK 500 ARG A 367 153.18 -45.09
REMARK 500 SER A 368 -67.58 -176.42
REMARK 500 ARG A 370 -106.62 -66.53
REMARK 500 TYR A 371 -57.65 51.25
REMARK 500 MET A 405 65.32 67.15
REMARK 500 LYS B 60 136.15 -21.87
REMARK 500 THR B 86 -82.03 -13.18
REMARK 500 VAL B 104 98.87 -64.67
REMARK 500 ARG B 105 43.19 -91.33
REMARK 500 GLU B 148 45.95 -95.21
REMARK 500 ARG B 166 0.41 -65.74
REMARK 500 ALA B 211 81.73 -28.72
REMARK 500 MET B 228 -58.20 -24.83
REMARK 500 ASP B 235 56.00 36.48
REMARK 500 GLU B 259 51.63 -141.88
REMARK 500 GLN B 279 139.00 90.26
REMARK 500 VAL B 304 -150.44 -150.30
REMARK 500 LYS B 314 -33.77 157.27
REMARK 500 ALA B 327 -1.21 -58.34
REMARK 500 SER B 333 -155.74 -84.16
REMARK 500 SER B 368 -11.99 137.80
REMARK 500 ARG B 370 -129.31 -62.39
REMARK 500 TYR B 371 3.44 24.68
REMARK 500 LYS B 374 159.75 -49.80
REMARK 500 MET B 405 69.40 71.55
REMARK 500 ASN B 406 146.03 -174.27
REMARK 500 ASP T 221 -175.05 -59.42
REMARK 500 ARG T 224 123.02 -174.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 210 ALA A 211 -79.62
REMARK 500 GLU A 261 GLU A 262 96.73
REMARK 500 VAL A 343 PRO A 344 -140.41
REMARK 500 GLY A 366 ARG A 367 146.29
REMARK 500 ARG A 370 TYR A 371 129.10
REMARK 500 PRO B 210 ALA B 211 -112.77
REMARK 500 GLU B 261 GLU B 262 65.37
REMARK 500 GLY B 369 ARG B 370 147.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2J0U A 38 411 UNP P38919 DDX48_HUMAN 37 410
DBREF 2J0U B 38 411 UNP P38919 DDX48_HUMAN 37 410
DBREF 2J0U T 137 250 UNP O15234 CASC3_HUMAN 137 250
SEQADV 2J0U VAL A 94 UNP P38919 ILE 93 CONFLICT
SEQADV 2J0U VAL A 122 UNP P38919 ILE 121 CONFLICT
SEQADV 2J0U VAL A 378 UNP P38919 ILE 377 CONFLICT
SEQADV 2J0U VAL A 388 UNP P38919 ILE 387 CONFLICT
SEQADV 2J0U VAL B 94 UNP P38919 ILE 93 CONFLICT
SEQADV 2J0U VAL B 122 UNP P38919 ILE 121 CONFLICT
SEQADV 2J0U SER B 137 UNP P38919 CYS 136 CONFLICT
SEQADV 2J0U VAL B 225 UNP P38919 ILE 224 CONFLICT
SEQADV 2J0U VAL B 378 UNP P38919 ILE 377 CONFLICT
SEQADV 2J0U VAL B 388 UNP P38919 ILE 387 CONFLICT
SEQRES 1 A 374 PRO THR PHE ASP THR MET GLY LEU ARG GLU ASP LEU LEU
SEQRES 2 A 374 ARG GLY ILE TYR ALA TYR GLY PHE GLU LYS PRO SER ALA
SEQRES 3 A 374 ILE GLN GLN ARG ALA ILE LYS GLN ILE ILE LYS GLY ARG
SEQRES 4 A 374 ASP VAL ILE ALA GLN SER GLN SER GLY THR GLY LYS THR
SEQRES 5 A 374 ALA THR PHE SER VAL SER VAL LEU GLN CYS LEU ASP ILE
SEQRES 6 A 374 GLN VAL ARG GLU THR GLN ALA LEU ILE LEU ALA PRO THR
SEQRES 7 A 374 ARG GLU LEU ALA VAL GLN VAL GLN LYS GLY LEU LEU ALA
SEQRES 8 A 374 LEU GLY ASP TYR MET ASN VAL GLN CYS HIS ALA CYS ILE
SEQRES 9 A 374 GLY GLY THR ASN VAL GLY GLU ASP ILE ARG LYS LEU ASP
SEQRES 10 A 374 TYR GLY GLN HIS VAL VAL ALA GLY THR PRO GLY ARG VAL
SEQRES 11 A 374 PHE ASP MET ILE ARG ARG ARG SER LEU ARG THR ARG ALA
SEQRES 12 A 374 ILE LYS MET LEU VAL LEU ASP GLU ALA ASP GLU MET LEU
SEQRES 13 A 374 ASN LYS GLY PHE LYS GLU GLN ILE TYR ASP VAL TYR ARG
SEQRES 14 A 374 TYR LEU PRO PRO ALA THR GLN VAL VAL LEU ILE SER ALA
SEQRES 15 A 374 THR LEU PRO HIS GLU ILE LEU GLU MET THR ASN LYS PHE
SEQRES 16 A 374 MET THR ASP PRO ILE ARG ILE LEU VAL LYS ARG ASP GLU
SEQRES 17 A 374 LEU THR LEU GLU GLY ILE LYS GLN PHE PHE VAL ALA VAL
SEQRES 18 A 374 GLU ARG GLU GLU TRP LYS PHE ASP THR LEU CYS ASP LEU
SEQRES 19 A 374 TYR ASP THR LEU THR ILE THR GLN ALA VAL ILE PHE CYS
SEQRES 20 A 374 ASN THR LYS ARG LYS VAL ASP TRP LEU THR GLU LYS MET
SEQRES 21 A 374 ARG GLU ALA ASN PHE THR VAL SER SER MET HIS GLY ASP
SEQRES 22 A 374 MET PRO GLN LYS GLU ARG GLU SER ILE MET LYS GLU PHE
SEQRES 23 A 374 ARG SER GLY ALA SER ARG VAL LEU ILE SER THR ASP VAL
SEQRES 24 A 374 TRP ALA ARG GLY LEU ASP VAL PRO GLN VAL SER LEU ILE
SEQRES 25 A 374 ILE ASN TYR ASP LEU PRO ASN ASN ARG GLU LEU TYR ILE
SEQRES 26 A 374 HIS ARG ILE GLY ARG SER GLY ARG TYR GLY ARG LYS GLY
SEQRES 27 A 374 VAL ALA VAL ASN PHE VAL LYS ASN ASP ASP ILE ARG VAL
SEQRES 28 A 374 LEU ARG ASP ILE GLU GLN TYR TYR SER THR GLN ILE ASP
SEQRES 29 A 374 GLU MET PRO MET ASN VAL ALA ASP LEU ILE
SEQRES 1 B 374 PRO THR PHE ASP THR MET GLY LEU ARG GLU ASP LEU LEU
SEQRES 2 B 374 ARG GLY ILE TYR ALA TYR GLY PHE GLU LYS PRO SER ALA
SEQRES 3 B 374 ILE GLN GLN ARG ALA ILE LYS GLN ILE ILE LYS GLY ARG
SEQRES 4 B 374 ASP VAL ILE ALA GLN SER GLN SER GLY THR GLY LYS THR
SEQRES 5 B 374 ALA THR PHE SER VAL SER VAL LEU GLN CYS LEU ASP ILE
SEQRES 6 B 374 GLN VAL ARG GLU THR GLN ALA LEU ILE LEU ALA PRO THR
SEQRES 7 B 374 ARG GLU LEU ALA VAL GLN VAL GLN LYS GLY LEU LEU ALA
SEQRES 8 B 374 LEU GLY ASP TYR MET ASN VAL GLN SER HIS ALA CYS ILE
SEQRES 9 B 374 GLY GLY THR ASN VAL GLY GLU ASP ILE ARG LYS LEU ASP
SEQRES 10 B 374 TYR GLY GLN HIS VAL VAL ALA GLY THR PRO GLY ARG VAL
SEQRES 11 B 374 PHE ASP MET ILE ARG ARG ARG SER LEU ARG THR ARG ALA
SEQRES 12 B 374 ILE LYS MET LEU VAL LEU ASP GLU ALA ASP GLU MET LEU
SEQRES 13 B 374 ASN LYS GLY PHE LYS GLU GLN ILE TYR ASP VAL TYR ARG
SEQRES 14 B 374 TYR LEU PRO PRO ALA THR GLN VAL VAL LEU ILE SER ALA
SEQRES 15 B 374 THR LEU PRO HIS GLU VAL LEU GLU MET THR ASN LYS PHE
SEQRES 16 B 374 MET THR ASP PRO ILE ARG ILE LEU VAL LYS ARG ASP GLU
SEQRES 17 B 374 LEU THR LEU GLU GLY ILE LYS GLN PHE PHE VAL ALA VAL
SEQRES 18 B 374 GLU ARG GLU GLU TRP LYS PHE ASP THR LEU CYS ASP LEU
SEQRES 19 B 374 TYR ASP THR LEU THR ILE THR GLN ALA VAL ILE PHE CYS
SEQRES 20 B 374 ASN THR LYS ARG LYS VAL ASP TRP LEU THR GLU LYS MET
SEQRES 21 B 374 ARG GLU ALA ASN PHE THR VAL SER SER MET HIS GLY ASP
SEQRES 22 B 374 MET PRO GLN LYS GLU ARG GLU SER ILE MET LYS GLU PHE
SEQRES 23 B 374 ARG SER GLY ALA SER ARG VAL LEU ILE SER THR ASP VAL
SEQRES 24 B 374 TRP ALA ARG GLY LEU ASP VAL PRO GLN VAL SER LEU ILE
SEQRES 25 B 374 ILE ASN TYR ASP LEU PRO ASN ASN ARG GLU LEU TYR ILE
SEQRES 26 B 374 HIS ARG ILE GLY ARG SER GLY ARG TYR GLY ARG LYS GLY
SEQRES 27 B 374 VAL ALA VAL ASN PHE VAL LYS ASN ASP ASP ILE ARG VAL
SEQRES 28 B 374 LEU ARG ASP ILE GLU GLN TYR TYR SER THR GLN ILE ASP
SEQRES 29 B 374 GLU MET PRO MET ASN VAL ALA ASP LEU ILE
SEQRES 1 T 114 ASP THR LYS SER THR VAL THR GLY GLU ARG GLN SER GLY
SEQRES 2 T 114 ASP GLY GLN GLU SER THR GLU PRO VAL GLU ASN LYS VAL
SEQRES 3 T 114 GLY LYS LYS GLY PRO LYS HIS LEU ASP ASP ASP GLU ASP
SEQRES 4 T 114 ARG LYS ASN PRO ALA TYR ILE PRO ARG LYS GLY LEU PHE
SEQRES 5 T 114 PHE GLU HIS ASP LEU ARG GLY GLN THR GLN GLU GLU GLU
SEQRES 6 T 114 VAL ARG PRO LYS GLY ARG GLN ARG LYS LEU TRP LYS ASP
SEQRES 7 T 114 GLU GLY ARG TRP GLU HIS ASP LYS PHE ARG GLU ASP GLU
SEQRES 8 T 114 GLN ALA PRO LYS SER ARG GLN GLU LEU ILE ALA LEU TYR
SEQRES 9 T 114 GLY TYR ASP ILE ARG SER ALA HIS ASN PRO
HELIX 1 1 PHE A 40 GLY A 44 5 5
HELIX 2 2 ARG A 46 TYR A 56 1 11
HELIX 3 3 SER A 62 GLY A 75 1 14
HELIX 4 4 THR A 89 LEU A 100 1 12
HELIX 5 5 THR A 115 ASP A 131 1 17
HELIX 6 6 ASN A 145 TYR A 155 1 11
HELIX 7 7 THR A 163 ARG A 173 1 11
HELIX 8 8 GLU A 188 ASN A 194 1 7
HELIX 9 9 PHE A 197 TYR A 207 1 11
HELIX 10 10 PRO A 222 MET A 233 1 12
HELIX 11 11 TRP A 263 TYR A 272 1 10
HELIX 12 12 THR A 286 ALA A 300 1 15
HELIX 13 13 PRO A 312 GLY A 326 1 15
HELIX 14 14 GLU A 359 ILE A 365 1 7
HELIX 15 15 LYS A 382 ASP A 384 5 3
HELIX 16 16 ASP A 385 SER A 397 1 13
HELIX 17 17 PHE B 40 GLY B 44 5 5
HELIX 18 18 ARG B 46 TYR B 56 1 11
HELIX 19 19 SER B 62 LYS B 74 1 13
HELIX 20 20 THR B 89 LEU B 100 1 12
HELIX 21 21 THR B 115 ASP B 131 1 17
HELIX 22 22 ASP B 149 TYR B 155 1 7
HELIX 23 23 THR B 163 ARG B 173 1 11
HELIX 24 24 GLU B 188 LEU B 193 1 6
HELIX 25 25 PHE B 197 TYR B 207 1 11
HELIX 26 26 PRO B 222 MET B 233 1 12
HELIX 27 27 TRP B 263 LEU B 271 1 9
HELIX 28 28 LEU B 271 GLN B 279 1 9
HELIX 29 29 THR B 286 ARG B 298 1 13
HELIX 30 30 GLU B 315 GLY B 326 1 12
HELIX 31 31 LEU B 360 ILE B 365 1 6
HELIX 32 32 LYS B 382 ASP B 384 5 3
HELIX 33 33 ASP B 385 SER B 397 1 13
SHEET 1 AA 7 ALA A 139 CYS A 140 0
SHEET 2 AA 7 VAL A 159 GLY A 162 1 O ALA A 161 N CYS A 140
SHEET 3 AA 7 ALA A 109 LEU A 112 1 O ALA A 109 N VAL A 160
SHEET 4 AA 7 MET A 183 LEU A 186 1 O MET A 183 N LEU A 110
SHEET 5 AA 7 GLN A 213 SER A 218 1 O GLN A 213 N LEU A 184
SHEET 6 AA 7 VAL A 78 GLN A 81 1 O VAL A 78 N LEU A 216
SHEET 7 AA 7 ILE A 237 ILE A 239 1 O ILE A 237 N ILE A 79
SHEET 1 AB 7 VAL A 304 MET A 307 0
SHEET 2 AB 7 VAL A 330 SER A 333 1 O VAL A 330 N SER A 305
SHEET 3 AB 7 ALA A 280 PHE A 283 1 O ALA A 280 N LEU A 331
SHEET 4 AB 7 LEU A 348 ASN A 351 1 O LEU A 348 N VAL A 281
SHEET 5 AB 7 VAL A 376 VAL A 381 1 O VAL A 376 N ILE A 349
SHEET 6 AB 7 LYS A 252 ALA A 257 1 O LYS A 252 N ALA A 377
SHEET 7 AB 7 ASP A 401 GLU A 402 1 O ASP A 401 N PHE A 255
SHEET 1 BA 7 SER B 137 ALA B 139 0
SHEET 2 BA 7 VAL B 159 GLY B 162 1 O VAL B 159 N HIS B 138
SHEET 3 BA 7 ALA B 109 LEU B 112 1 O ALA B 109 N VAL B 160
SHEET 4 BA 7 MET B 183 LEU B 186 1 O MET B 183 N LEU B 110
SHEET 5 BA 7 GLN B 213 ILE B 217 1 O GLN B 213 N LEU B 184
SHEET 6 BA 7 VAL B 78 ALA B 80 1 O VAL B 78 N LEU B 216
SHEET 7 BA 7 ILE B 237 ILE B 239 1 O ILE B 237 N ILE B 79
SHEET 1 BB 6 VAL B 330 LEU B 331 0
SHEET 2 BB 6 ALA B 280 PHE B 283 1 O ALA B 280 N LEU B 331
SHEET 3 BB 6 LEU B 348 ASN B 351 1 O LEU B 348 N VAL B 281
SHEET 4 BB 6 GLY B 375 VAL B 381 1 O VAL B 376 N ILE B 349
SHEET 5 BB 6 ILE B 251 ALA B 257 1 O LYS B 252 N ALA B 377
SHEET 6 BB 6 ASP B 401 GLU B 402 1 O ASP B 401 N PHE B 255
CISPEP 1 GLY A 142 GLY A 143 0 10.35
CISPEP 2 THR A 144 ASN A 145 0 13.86
CISPEP 3 VAL A 258 GLU A 259 0 0.87
CISPEP 4 ASP A 342 VAL A 343 0 3.32
CISPEP 5 ARG A 367 SER A 368 0 9.61
CISPEP 6 SER A 368 GLY A 369 0 6.04
CISPEP 7 VAL B 258 GLU B 259 0 -1.15
CISPEP 8 ARG B 367 SER B 368 0 11.39
CISPEP 9 SER B 368 GLY B 369 0 -18.61
CRYST1 71.760 107.190 243.950 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 0.013935 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009329 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004099 0.00000
MTRIX1 1 -0.035270 -0.966270 -0.255110 0.46485 1
MTRIX2 1 -0.997980 0.020560 0.060110 -9.18389 1
MTRIX3 1 -0.052840 0.256720 -0.965040 61.89357 1
(ATOM LINES ARE NOT SHOWN.)
END