HEADER LIGASE 17-MAR-05 1Z56
TITLE CO-CRYSTAL STRUCTURE OF LIF1P-LIG4P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA LIGASE IV;
COMPND 7 CHAIN: C;
COMPND 8 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE [ATP], DNA
COMPND 9 LIGASE IV HOMOLOG;
COMPND 10 EC: 6.5.1.1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 14 CHAIN: D;
COMPND 15 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 19 CHAIN: E, H;
COMPND 20 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 24 CHAIN: F;
COMPND 25 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 26 ENGINEERED: YES;
COMPND 27 MOL_ID: 6;
COMPND 28 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 29 CHAIN: G;
COMPND 30 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 31 ENGINEERED: YES;
COMPND 32 MOL_ID: 7;
COMPND 33 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 34 CHAIN: I;
COMPND 35 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 36 ENGINEERED: YES;
COMPND 37 MOL_ID: 8;
COMPND 38 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 39 CHAIN: J;
COMPND 40 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 41 ENGINEERED: YES;
COMPND 42 MOL_ID: 9;
COMPND 43 MOLECULE: LIGASE INTERACTING FACTOR 1;
COMPND 44 CHAIN: K;
COMPND 45 FRAGMENT: UNCHARACTERIZED FRAGMENT;
COMPND 46 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: LIF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A+;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: DNL4, LIG4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGAT3;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 GENE: LIF1;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 30 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 31 ORGANISM_TAXID: 4932;
SOURCE 32 GENE: LIF1;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 35 MOL_ID: 5;
SOURCE 36 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 37 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 38 ORGANISM_TAXID: 4932;
SOURCE 39 GENE: LIF1;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 42 MOL_ID: 6;
SOURCE 43 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 44 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 45 ORGANISM_TAXID: 4932;
SOURCE 46 GENE: LIF1;
SOURCE 47 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 48 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 49 MOL_ID: 7;
SOURCE 50 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 51 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 52 ORGANISM_TAXID: 4932;
SOURCE 53 GENE: LIF1;
SOURCE 54 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 55 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 56 MOL_ID: 8;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 4932;
SOURCE 60 GENE: LIF1;
SOURCE 61 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 62 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 63 MOL_ID: 9;
SOURCE 64 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 65 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 66 ORGANISM_TAXID: 4932;
SOURCE 67 GENE: LIF1;
SOURCE 68 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 69 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA REPAIR, BRCT, NHEJ, XRCC4, DNA LIGASE, COILED-COIL
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.DORE,N.FURNHAM,O.R.DAVIES,B.L.SIBANDA,D.Y.CHIRGADZE,
AUTHOR 2 S.P.JACKSON,L.PELLEGRINI,T.L.BLUNDELL
REVDAT 5 24-FEB-09 1Z56 1 VERSN
REVDAT 4 29-AUG-06 1Z56 3 ATOM REMARK
REVDAT 3 08-AUG-06 1Z56 1 JRNL DBREF
REVDAT 2 28-FEB-06 1Z56 1 JRNL
REVDAT 1 31-JAN-06 1Z56 0
JRNL AUTH A.S.DORE,N.FURNHAM,O.R.DAVIES,B.L.SIBANDA,
JRNL AUTH 2 D.Y.CHIRGADZE,S.P.JACKSON,L.PELLEGRINI,T.L.BLUNDELL
JRNL TITL STRUCTURE OF AN XRCC4-DNA LIGASE IV YEAST ORTHOLOG
JRNL TITL 2 COMPLEX REVEALS A NOVEL BRCT INTERACTION MODE.
JRNL REF DNA REPAIR V. 5 362 2006
JRNL REFN ISSN 1568-7864
JRNL PMID 16388993
JRNL DOI 10.1016/J.DNAREP.2005.11.004
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15638
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) : 0.403
REMARK 3 R VALUE (WORKING SET) : 0.400
REMARK 3 FREE R VALUE : 0.467
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 832
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) : 3.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1105
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3610
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.4330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4164
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) : 107.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.31000
REMARK 3 B22 (A**2) : 1.31000
REMARK 3 B33 (A**2) : -1.96000
REMARK 3 B12 (A**2) : 0.65000
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): 0.961
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 70.148
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.750
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.659
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4198 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 8 ; 0.012 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5623 ; 2.130 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16 ; 1.987 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 545 ;10.166 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 158 ;41.914 ;24.241
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 809 ;25.971 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;20.912 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 656 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3049 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 8 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2550 ; 0.330 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 18 ; 0.323 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2748 ; 0.324 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 16 ; 0.254 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 246 ; 0.257 ; 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): 62 ; 0.325 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.218 ; 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): 2848 ; 0.596 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8 ; 0.094 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4463 ; 1.042 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1502 ; 1.203 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1160 ; 2.151 ; 4.500
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 : 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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1Z56 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-05.
REMARK 100 THE RCSB ID CODE IS RCSB032311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.968
REMARK 200 MONOCHROMATOR : SI-111 DOUBLE MONOCHROMATOR
REMARK 200 OPTICS : SI-111 DOUBLE MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16475
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.920
REMARK 200 RESOLUTION RANGE LOW (A) : 49.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.100
REMARK 200 R MERGE (I) : 0.17500
REMARK 200 R SYM (I) : 0.17500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.79900
REMARK 200 R SYM FOR SHELL (I) : 0.79900
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR(AS)
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, SODIUM CHLORIDE,
REMARK 280 DITHIOTHREITOL, PEG 6000, 2-(N-MORPHOLINO)ETHANESULFONIC ACID,
REMARK 280 ETHYLENE GLYCOL, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+2/3
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 32.80533
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 65.61067
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 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 32.80533
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 65.61067
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 32.80533
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 65.61067
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 32.80533
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 65.61067
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K
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 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 LEU A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 PHE A 7
REMARK 465 ILE A 8
REMARK 465 SER A 9
REMARK 465 CYS A 10
REMARK 465 ILE A 11
REMARK 465 PRO A 12
REMARK 465 VAL A 13
REMARK 465 VAL A 14
REMARK 465 ASN A 15
REMARK 465 GLU A 16
REMARK 465 GLU A 17
REMARK 465 GLN A 18
REMARK 465 ASN A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 ASP A 22
REMARK 465 GLU A 23
REMARK 465 ARG A 24
REMARK 465 GLY A 25
REMARK 465 LEU A 26
REMARK 465 CYS A 27
REMARK 465 LYS A 28
REMARK 465 ILE A 29
REMARK 465 GLN A 30
REMARK 465 ILE A 31
REMARK 465 GLU A 32
REMARK 465 ASP A 33
REMARK 465 GLY A 34
REMARK 465 ALA A 35
REMARK 465 MET A 36
REMARK 465 LEU A 37
REMARK 465 GLU A 38
REMARK 465 THR A 39
REMARK 465 LEU A 40
REMARK 465 ASP A 41
REMARK 465 GLU A 42
REMARK 465 ASN A 43
REMARK 465 SER A 44
REMARK 465 LEU A 45
REMARK 465 SER A 46
REMARK 465 GLY A 47
REMARK 465 LEU A 48
REMARK 465 ARG A 49
REMARK 465 ILE A 50
REMARK 465 GLU A 51
REMARK 465 LYS A 52
REMARK 465 MET A 53
REMARK 465 LEU A 54
REMARK 465 VAL A 55
REMARK 465 SER A 56
REMARK 465 GLU A 57
REMARK 465 GLY A 58
REMARK 465 THR A 59
REMARK 465 GLY A 60
REMARK 465 ILE A 61
REMARK 465 PHE A 62
REMARK 465 SER A 63
REMARK 465 LYS A 64
REMARK 465 SER A 65
REMARK 465 SER A 66
REMARK 465 PHE A 67
REMARK 465 GLY A 68
REMARK 465 ILE A 69
REMARK 465 ASN A 70
REMARK 465 ASP A 71
REMARK 465 LEU A 72
REMARK 465 ARG A 73
REMARK 465 ILE A 74
REMARK 465 PHE A 75
REMARK 465 THR A 76
REMARK 465 GLY A 77
REMARK 465 GLU A 78
REMARK 465 ASN A 79
REMARK 465 ILE A 80
REMARK 465 ASP A 81
REMARK 465 GLU A 82
REMARK 465 GLU A 83
REMARK 465 SER A 84
REMARK 465 LYS A 85
REMARK 465 LYS A 86
REMARK 465 TYR A 87
REMARK 465 VAL A 88
REMARK 465 TRP A 89
REMARK 465 TYR A 90
REMARK 465 GLU A 91
REMARK 465 LEU A 92
REMARK 465 LEU A 93
REMARK 465 LYS A 94
REMARK 465 MET A 95
REMARK 465 LEU A 96
REMARK 465 THR A 97
REMARK 465 GLY A 98
REMARK 465 HIS A 99
REMARK 465 LYS A 100
REMARK 465 VAL A 101
REMARK 465 TYR A 102
REMARK 465 ILE A 103
REMARK 465 ALA A 104
REMARK 465 SER A 105
REMARK 465 LEU A 106
REMARK 465 ASP A 107
REMARK 465 GLU A 108
REMARK 465 LYS A 109
REMARK 465 VAL A 110
REMARK 465 VAL A 111
REMARK 465 PHE A 112
REMARK 465 THR A 113
REMARK 465 LYS A 114
REMARK 465 TRP A 115
REMARK 465 THR A 116
REMARK 465 CYS A 117
REMARK 465 ARG A 118
REMARK 465 MET A 119
REMARK 465 GLN A 120
REMARK 465 ASP A 121
REMARK 465 ASP A 122
REMARK 465 GLU A 123
REMARK 465 VAL A 124
REMARK 465 TRP A 125
REMARK 465 LYS A 126
REMARK 465 VAL A 127
REMARK 465 VAL A 128
REMARK 465 MET A 129
REMARK 465 GLU A 130
REMARK 465 LEU A 131
REMARK 465 GLU A 132
REMARK 465 SER A 133
REMARK 465 SER A 134
REMARK 465 ALA A 135
REMARK 465 ILE A 136
REMARK 465 ILE A 137
REMARK 465 ARG A 138
REMARK 465 LYS A 139
REMARK 465 ILE A 140
REMARK 465 ALA A 141
REMARK 465 GLU A 142
REMARK 465 LEU A 143
REMARK 465 THR A 144
REMARK 465 LEU A 145
REMARK 465 HIS A 146
REMARK 465 PRO A 147
REMARK 465 VAL A 148
REMARK 465 LYS A 149
REMARK 465 LYS A 150
REMARK 465 GLY A 151
REMARK 465 GLU A 152
REMARK 465 ILE A 153
REMARK 465 ASP A 154
REMARK 465 LEU A 155
REMARK 465 PHE A 156
REMARK 465 GLU A 157
REMARK 465 MET A 158
REMARK 465 LYS A 236
REMARK 465 LEU A 237
REMARK 465 SER A 238
REMARK 465 ASP A 239
REMARK 465 ASP A 240
REMARK 465 ASP A 241
REMARK 465 VAL A 242
REMARK 465 LEU A 243
REMARK 465 ASP A 244
REMARK 465 SER A 245
REMARK 465 ALA A 246
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 LEU B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 PHE B 7
REMARK 465 ILE B 8
REMARK 465 SER B 9
REMARK 465 CYS B 10
REMARK 465 ILE B 11
REMARK 465 PRO B 12
REMARK 465 VAL B 13
REMARK 465 VAL B 14
REMARK 465 ASN B 15
REMARK 465 GLU B 16
REMARK 465 GLU B 17
REMARK 465 GLN B 18
REMARK 465 ASN B 19
REMARK 465 GLU B 20
REMARK 465 GLU B 21
REMARK 465 ASP B 22
REMARK 465 GLU B 23
REMARK 465 ARG B 24
REMARK 465 GLY B 25
REMARK 465 LEU B 26
REMARK 465 CYS B 27
REMARK 465 LYS B 28
REMARK 465 ILE B 29
REMARK 465 GLN B 30
REMARK 465 ILE B 31
REMARK 465 GLU B 32
REMARK 465 ASP B 33
REMARK 465 GLY B 34
REMARK 465 ALA B 35
REMARK 465 MET B 36
REMARK 465 LEU B 37
REMARK 465 GLU B 38
REMARK 465 THR B 39
REMARK 465 LEU B 40
REMARK 465 ASP B 41
REMARK 465 GLU B 42
REMARK 465 ASN B 43
REMARK 465 SER B 44
REMARK 465 LEU B 45
REMARK 465 SER B 46
REMARK 465 GLY B 47
REMARK 465 LEU B 48
REMARK 465 ARG B 49
REMARK 465 ILE B 50
REMARK 465 GLU B 51
REMARK 465 LYS B 52
REMARK 465 MET B 53
REMARK 465 LEU B 54
REMARK 465 VAL B 55
REMARK 465 SER B 56
REMARK 465 GLU B 57
REMARK 465 GLY B 58
REMARK 465 THR B 59
REMARK 465 GLY B 60
REMARK 465 ILE B 61
REMARK 465 PHE B 62
REMARK 465 SER B 63
REMARK 465 LYS B 64
REMARK 465 SER B 65
REMARK 465 SER B 66
REMARK 465 PHE B 67
REMARK 465 GLY B 68
REMARK 465 ILE B 69
REMARK 465 ASN B 70
REMARK 465 ASP B 71
REMARK 465 LEU B 72
REMARK 465 ARG B 73
REMARK 465 ILE B 74
REMARK 465 PHE B 75
REMARK 465 THR B 76
REMARK 465 GLY B 77
REMARK 465 GLU B 78
REMARK 465 ASN B 79
REMARK 465 ILE B 80
REMARK 465 ASP B 81
REMARK 465 GLU B 82
REMARK 465 GLU B 83
REMARK 465 SER B 84
REMARK 465 LYS B 85
REMARK 465 LYS B 86
REMARK 465 TYR B 87
REMARK 465 VAL B 88
REMARK 465 TRP B 89
REMARK 465 TYR B 90
REMARK 465 GLU B 91
REMARK 465 LEU B 92
REMARK 465 LEU B 93
REMARK 465 LYS B 94
REMARK 465 MET B 95
REMARK 465 LEU B 96
REMARK 465 THR B 97
REMARK 465 GLY B 98
REMARK 465 HIS B 99
REMARK 465 LYS B 100
REMARK 465 VAL B 101
REMARK 465 TYR B 102
REMARK 465 ILE B 103
REMARK 465 ALA B 104
REMARK 465 SER B 105
REMARK 465 LEU B 106
REMARK 465 ASP B 107
REMARK 465 GLU B 108
REMARK 465 LYS B 109
REMARK 465 VAL B 110
REMARK 465 VAL B 111
REMARK 465 PHE B 112
REMARK 465 THR B 113
REMARK 465 LYS B 114
REMARK 465 TRP B 115
REMARK 465 THR B 116
REMARK 465 CYS B 117
REMARK 465 ARG B 118
REMARK 465 MET B 119
REMARK 465 GLN B 120
REMARK 465 ASP B 121
REMARK 465 ASP B 122
REMARK 465 GLU B 123
REMARK 465 VAL B 124
REMARK 465 TRP B 125
REMARK 465 LYS B 126
REMARK 465 VAL B 127
REMARK 465 VAL B 128
REMARK 465 MET B 129
REMARK 465 GLU B 130
REMARK 465 LEU B 131
REMARK 465 GLU B 132
REMARK 465 SER B 133
REMARK 465 SER B 134
REMARK 465 ALA B 135
REMARK 465 ILE B 136
REMARK 465 ILE B 137
REMARK 465 ARG B 138
REMARK 465 LYS B 139
REMARK 465 ILE B 140
REMARK 465 ALA B 141
REMARK 465 GLU B 142
REMARK 465 LEU B 143
REMARK 465 THR B 144
REMARK 465 LEU B 145
REMARK 465 HIS B 146
REMARK 465 PRO B 147
REMARK 465 VAL B 148
REMARK 465 LYS B 149
REMARK 465 LYS B 150
REMARK 465 GLY B 151
REMARK 465 GLU B 152
REMARK 465 ILE B 153
REMARK 465 ASP B 154
REMARK 465 LEU B 155
REMARK 465 GLN B 232
REMARK 465 ASN B 233
REMARK 465 ASN B 234
REMARK 465 ILE B 235
REMARK 465 LYS B 236
REMARK 465 LEU B 237
REMARK 465 SER B 238
REMARK 465 ASP B 239
REMARK 465 ASP B 240
REMARK 465 ASP B 241
REMARK 465 VAL B 242
REMARK 465 LEU B 243
REMARK 465 ASP B 244
REMARK 465 SER B 245
REMARK 465 ALA B 246
REMARK 465 PRO C 681
REMARK 465 ILE C 682
REMARK 465 LEU C 839A
REMARK 465 PHE C 839B
REMARK 465 SER C 839C
REMARK 465 ASN C 839D
REMARK 465 ARG C 839E
REMARK 465 ILE C 839F
REMARK 465 ALA C 839G
REMARK 465 TYR C 839H
REMARK 465 VAL C 839I
REMARK 465 PRO C 839J
REMARK 465 ARG C 839K
REMARK 465 ARG C 839L
REMARK 465 LYS C 839M
REMARK 465 ILE C 839N
REMARK 465 SER C 839O
REMARK 465 THR C 839P
REMARK 465 GLU C 839Q
REMARK 465 ASP C 839R
REMARK 465 ASP C 839S
REMARK 465 ILE C 839T
REMARK 465 PRO C 939
REMARK 465 VAL C 940
REMARK 465 VAL C 941
REMARK 465 ASN C 942
REMARK 465 TYR C 943
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 PHE C 839 CG CD1 CD2 CE1 CE2 CZ
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 ND2 ASN C 895 N VAL C 897 1.47
REMARK 500 ND2 ASN C 895 CG2 VAL C 897 1.63
REMARK 500 ND2 ASN C 895 CA VAL C 897 1.97
REMARK 500 O ASN C 895 N VAL C 897 1.99
REMARK 500 ND2 ASN C 895 CB VAL C 897 2.05
REMARK 500 O ASP C 892 CB ASN C 895 2.05
REMARK 500 O ASN C 761 N ASP C 765 2.09
REMARK 500 O PRO C 760 N TRP C 762 2.09
REMARK 500 CG UNK G 4007 O UNK G 4012 2.15
REMARK 500 O PHE C 866 N GLY C 868 2.16
REMARK 500 O CYS C 741 CD2 HIS C 759 2.17
REMARK 500 O ILE C 859 N ILE C 863 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE ARG C 916 CG2 ILE C 727 6554 1.96
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 LEU B 200 CA - CB - CG ANGL. DEV. = -17.3 DEGREES
REMARK 500 ARG C 835 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU C 876 CA - CB - CG ANGL. DEV. = 17.8 DEGREES
REMARK 500 UNK J3002 O - C - N ANGL. DEV. = -12.1 DEGREES
REMARK 500 UNK J3003 O - C - N ANGL. DEV. = -12.0 DEGREES
REMARK 500 UNK J3005 O - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 UNK J3008 O - C - N ANGL. DEV. = -36.1 DEGREES
REMARK 500 UNK J3009 O - C - N ANGL. DEV. = -39.6 DEGREES
REMARK 500 UNK J3010 O - C - N ANGL. DEV. = -10.7 DEGREES
REMARK 500 UNK J3011 O - C - N ANGL. DEV. = 14.7 DEGREES
REMARK 500 UNK J3012 O - C - N ANGL. DEV. = -18.4 DEGREES
REMARK 500 UNK J3016 O - C - N ANGL. DEV. = -17.7 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 CYS A 167 -27.16 -37.20
REMARK 500 VAL A 169 10.55 -62.65
REMARK 500 TYR A 173 44.70 -79.65
REMARK 500 ARG A 174 -48.95 -153.08
REMARK 500 LYS A 177 39.45 -99.50
REMARK 500 GLU A 178 -77.91 -165.12
REMARK 500 ASP A 180 -14.16 -144.12
REMARK 500 SER A 181 -101.68 -82.94
REMARK 500 GLU A 188 -40.72 -143.60
REMARK 500 LEU A 190 47.63 -103.04
REMARK 500 ALA A 191 -39.70 -152.54
REMARK 500 GLU A 195 1.14 -69.46
REMARK 500 LEU A 201 8.86 -61.48
REMARK 500 MET A 211 -79.99 -67.65
REMARK 500 MET A 212 -59.17 -26.36
REMARK 500 ASN A 234 150.94 -47.96
REMARK 500 GLU B 157 30.64 -85.46
REMARK 500 TYR B 163 24.87 -66.01
REMARK 500 ILE B 166 -22.00 -23.89
REMARK 500 CYS B 167 -116.18 -75.69
REMARK 500 ARG B 174 -6.17 -50.43
REMARK 500 LYS B 177 -83.30 -37.81
REMARK 500 GLU B 178 4.87 -63.42
REMARK 500 SER B 181 -73.78 -87.75
REMARK 500 GLU B 188 -84.25 -50.56
REMARK 500 ALA B 191 -62.10 -97.15
REMARK 500 ARG B 192 -33.74 -37.72
REMARK 500 GLU B 193 -84.64 -58.81
REMARK 500 GLU B 195 0.34 -54.18
REMARK 500 LEU B 196 13.24 -141.00
REMARK 500 LEU B 197 -88.80 -118.53
REMARK 500 ASP B 198 -67.99 -20.38
REMARK 500 MET B 212 -75.24 -50.35
REMARK 500 VAL B 213 -76.68 -36.77
REMARK 500 LYS B 222 27.06 -72.26
REMARK 500 LEU B 226 -79.01 -37.10
REMARK 500 GLU B 228 55.77 -109.18
REMARK 500 ASN C 684 88.89 57.57
REMARK 500 PHE C 686 -94.84 47.34
REMARK 500 LEU C 690 74.12 -68.65
REMARK 500 VAL C 693 9.44 -174.19
REMARK 500 GLU C 700 161.88 69.72
REMARK 500 THR C 702 -157.20 -142.89
REMARK 500 ILE C 704 -76.83 -82.45
REMARK 500 THR C 707 -152.95 51.11
REMARK 500 GLU C 710 73.91 -118.59
REMARK 500 LEU C 711 -70.53 25.08
REMARK 500 HIS C 718 -40.93 -148.48
REMARK 500 TYR C 724 148.73 167.83
REMARK 500 LEU C 728 115.43 -18.26
REMARK 500 HIS C 731 119.11 -14.30
REMARK 500 SER C 732 -0.76 -145.42
REMARK 500 ILE C 733 21.50 -77.51
REMARK 500 ASP C 735 79.44 -109.12
REMARK 500 VAL C 736 57.74 -108.65
REMARK 500 THR C 744 -81.90 -102.77
REMARK 500 THR C 745 -120.38 17.11
REMARK 500 GLU C 746 -36.06 -28.04
REMARK 500 LYS C 748 -74.80 -11.49
REMARK 500 ALA C 749 4.34 -38.06
REMARK 500 ASP C 752 30.50 -82.54
REMARK 500 ARG C 753 32.00 -154.32
REMARK 500 HIS C 759 163.38 171.47
REMARK 500 PRO C 760 -98.81 -84.03
REMARK 500 ASN C 761 -65.54 49.94
REMARK 500 TYR C 769 -117.75 77.02
REMARK 500 LEU C 772 33.18 -162.31
REMARK 500 ILE C 773 92.64 -53.53
REMARK 500 LEU C 774 42.93 -54.60
REMARK 500 PRO C 777 101.66 -32.94
REMARK 500 ASN C 778 79.34 -178.01
REMARK 500 CYS C 780 10.25 -141.59
REMARK 500 ASN C 782 107.64 64.51
REMARK 500 SER C 784 -86.01 -40.89
REMARK 500 MET C 787 -46.28 -144.08
REMARK 500 ASP C 796 -166.29 -112.17
REMARK 500 SER C 801 -173.90 -58.70
REMARK 500 GLU C 803 -116.12 -52.13
REMARK 500 ASP C 805 -99.45 20.66
REMARK 500 SER C 813 -82.13 -56.22
REMARK 500 TYR C 815 -54.53 -172.35
REMARK 500 LYS C 816 25.14 -73.96
REMARK 500 LEU C 819 -50.35 -161.74
REMARK 500 LEU C 821 103.43 -164.86
REMARK 500 PRO C 823 -151.75 -48.14
REMARK 500 MET C 824 -164.72 -72.40
REMARK 500 ASP C 830 -120.20 -107.55
REMARK 500 SER C 831 -126.30 -170.30
REMARK 500 LYS C 869 105.11 64.69
REMARK 500 ILE C 870 -126.81 -162.77
REMARK 500 THR C 871 -70.84 156.43
REMARK 500 ASP C 872 -122.24 85.11
REMARK 500 GLN C 873 112.27 95.43
REMARK 500 GLN C 874 38.21 -89.92
REMARK 500 LEU C 876 93.40 -14.75
REMARK 500 ASN C 878 -47.56 21.11
REMARK 500 TYR C 884 173.23 -46.93
REMARK 500 THR C 885 -68.47 121.34
REMARK 500 ASP C 886 -137.25 -120.31
REMARK 500 MET C 894 2.19 -61.68
REMARK 500 ASN C 895 140.43 -25.19
REMARK 500 GLU C 896 -27.73 13.00
REMARK 500 LYS C 900 10.46 -63.26
REMARK 500 LYS C 902 48.43 -84.27
REMARK 500 ALA C 907 -113.60 -76.79
REMARK 500 SER C 908 131.32 -24.10
REMARK 500 ALA C 919 141.45 -35.61
REMARK 500 GLU C 921 -42.99 -14.63
REMARK 500 TRP C 922 -73.21 -59.28
REMARK 500 VAL C 923 -57.94 -26.94
REMARK 500 HIS C 925 3.74 -62.74
REMARK 500 ILE C 927 -21.65 -36.60
REMARK 500 GLU C 929 -69.09 -174.63
REMARK 500 ASN C 930 -138.64 -161.40
REMARK 500 GLN C 932 -166.13 -115.43
REMARK 500 VAL C 933 -44.40 -160.25
REMARK 500 GLU C 935 81.81 -58.76
REMARK 500 GLU C 936 18.91 177.64
REMARK 500 ASP C 937 -138.04 -70.50
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 TYR C 724 ASN C 725 -146.46
REMARK 500 ARG C 771 LEU C 772 148.17
REMARK 500 ASP C 805 ILE C 806 -133.57
REMARK 500 TYR C 884 THR C 885 141.30
REMARK 500 ASN C 895 GLU C 896 118.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 UNK J3001 63.77
REMARK 500 UNK J3002 106.68
REMARK 500 UNK J3003 137.60
REMARK 500 UNK J3004 111.41
REMARK 500 UNK J3005 144.53
REMARK 500 UNK J3006 111.88
REMARK 500 UNK J3007 -136.15
REMARK 500 UNK J3008 150.97
REMARK 500 UNK J3009 92.75
REMARK 500 UNK J3010 -142.00
REMARK 500 UNK J3011 72.36
REMARK 500 UNK J3012 159.80
REMARK 500 UNK J3013 172.45
REMARK 500 UNK J3014 150.43
REMARK 500 UNK J3015 158.64
REMARK 500 UNK J3016 100.12
REMARK 500 UNK J3017 64.75
REMARK 500 UNK J3018 134.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DEFINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DEFINED
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AS STATED BY THE AUTHORS, THE RESIDUES IN CHAINS D,E,
REMARK 999 F,G,H,I,J,K COULD NOT BE ALIGNED WITH ANY REGION OF
REMARK 999 THE TWO CHAINS A AND B DUE TO LOW ELECTRON DENSITY
REMARK 999 AND THEREFORE HAVE BEEN LABELED UNK.
DBREF 1Z56 A 1 246 UNP P53150 LIF1_YEAST 1 246
DBREF 1Z56 B 1 246 UNP P53150 LIF1_YEAST 1 246
DBREF 1Z56 C 681 942 UNP Q08387 DNL4_YEAST 681 944
DBREF 1Z56 D 1000 1007 PDB 1Z56 1Z56 1000 1007
DBREF 1Z56 E 2000 2006 PDB 1Z56 1Z56 2000 2006
DBREF 1Z56 F 3000 3044 PDB 1Z56 1Z56 3000 3044
DBREF 1Z56 G 4000 4036 PDB 1Z56 1Z56 4000 4036
DBREF 1Z56 H 1000 1006 PDB 1Z56 1Z56 1000 1006
DBREF 1Z56 I 2000 2029 PDB 1Z56 1Z56 2000 2029
DBREF 1Z56 J 3000 3019 PDB 1Z56 1Z56 3000 3019
DBREF 1Z56 K 4000 4012 PDB 1Z56 1Z56 4000 4012
SEQRES 1 A 246 MET SER GLN LEU THR GLU PHE ILE SER CYS ILE PRO VAL
SEQRES 2 A 246 VAL ASN GLU GLU GLN ASN GLU GLU ASP GLU ARG GLY LEU
SEQRES 3 A 246 CYS LYS ILE GLN ILE GLU ASP GLY ALA MET LEU GLU THR
SEQRES 4 A 246 LEU ASP GLU ASN SER LEU SER GLY LEU ARG ILE GLU LYS
SEQRES 5 A 246 MET LEU VAL SER GLU GLY THR GLY ILE PHE SER LYS SER
SEQRES 6 A 246 SER PHE GLY ILE ASN ASP LEU ARG ILE PHE THR GLY GLU
SEQRES 7 A 246 ASN ILE ASP GLU GLU SER LYS LYS TYR VAL TRP TYR GLU
SEQRES 8 A 246 LEU LEU LYS MET LEU THR GLY HIS LYS VAL TYR ILE ALA
SEQRES 9 A 246 SER LEU ASP GLU LYS VAL VAL PHE THR LYS TRP THR CYS
SEQRES 10 A 246 ARG MET GLN ASP ASP GLU VAL TRP LYS VAL VAL MET GLU
SEQRES 11 A 246 LEU GLU SER SER ALA ILE ILE ARG LYS ILE ALA GLU LEU
SEQRES 12 A 246 THR LEU HIS PRO VAL LYS LYS GLY GLU ILE ASP LEU PHE
SEQRES 13 A 246 GLU MET ALA ASP LYS LEU TYR LYS ASP ILE CYS CYS VAL
SEQRES 14 A 246 ASN ASP SER TYR ARG ASN ILE LYS GLU SER ASP SER SER
SEQRES 15 A 246 ASN ARG ASN ARG VAL GLU GLN LEU ALA ARG GLU ARG GLU
SEQRES 16 A 246 LEU LEU ASP LYS LEU LEU GLU THR ARG ASP GLU ARG THR
SEQRES 17 A 246 ARG ALA MET MET VAL THR LEU LEU ASN GLU LYS LYS LYS
SEQRES 18 A 246 LYS ILE ARG GLU LEU HIS GLU ILE LEU ARG GLN ASN ASN
SEQRES 19 A 246 ILE LYS LEU SER ASP ASP ASP VAL LEU ASP SER ALA
SEQRES 1 B 246 MET SER GLN LEU THR GLU PHE ILE SER CYS ILE PRO VAL
SEQRES 2 B 246 VAL ASN GLU GLU GLN ASN GLU GLU ASP GLU ARG GLY LEU
SEQRES 3 B 246 CYS LYS ILE GLN ILE GLU ASP GLY ALA MET LEU GLU THR
SEQRES 4 B 246 LEU ASP GLU ASN SER LEU SER GLY LEU ARG ILE GLU LYS
SEQRES 5 B 246 MET LEU VAL SER GLU GLY THR GLY ILE PHE SER LYS SER
SEQRES 6 B 246 SER PHE GLY ILE ASN ASP LEU ARG ILE PHE THR GLY GLU
SEQRES 7 B 246 ASN ILE ASP GLU GLU SER LYS LYS TYR VAL TRP TYR GLU
SEQRES 8 B 246 LEU LEU LYS MET LEU THR GLY HIS LYS VAL TYR ILE ALA
SEQRES 9 B 246 SER LEU ASP GLU LYS VAL VAL PHE THR LYS TRP THR CYS
SEQRES 10 B 246 ARG MET GLN ASP ASP GLU VAL TRP LYS VAL VAL MET GLU
SEQRES 11 B 246 LEU GLU SER SER ALA ILE ILE ARG LYS ILE ALA GLU LEU
SEQRES 12 B 246 THR LEU HIS PRO VAL LYS LYS GLY GLU ILE ASP LEU PHE
SEQRES 13 B 246 GLU MET ALA ASP LYS LEU TYR LYS ASP ILE CYS CYS VAL
SEQRES 14 B 246 ASN ASP SER TYR ARG ASN ILE LYS GLU SER ASP SER SER
SEQRES 15 B 246 ASN ARG ASN ARG VAL GLU GLN LEU ALA ARG GLU ARG GLU
SEQRES 16 B 246 LEU LEU ASP LYS LEU LEU GLU THR ARG ASP GLU ARG THR
SEQRES 17 B 246 ARG ALA MET MET VAL THR LEU LEU ASN GLU LYS LYS LYS
SEQRES 18 B 246 LYS ILE ARG GLU LEU HIS GLU ILE LEU ARG GLN ASN ASN
SEQRES 19 B 246 ILE LYS LEU SER ASP ASP ASP VAL LEU ASP SER ALA
SEQRES 1 C 264 PRO ILE SER ASN ILE PHE ALA GLY LEU LEU PHE TYR VAL
SEQRES 2 C 264 LEU SER ASP TYR VAL THR GLU ASP THR GLY ILE ARG ILE
SEQRES 3 C 264 THR ARG ALA GLU LEU GLU LYS THR ILE VAL GLU HIS GLY
SEQRES 4 C 264 GLY LYS LEU ILE TYR ASN VAL ILE LEU LYS ARG HIS SER
SEQRES 5 C 264 ILE GLY ASP VAL ARG LEU ILE SER CYS LYS THR THR THR
SEQRES 6 C 264 GLU CYS LYS ALA LEU ILE ASP ARG GLY TYR ASP ILE LEU
SEQRES 7 C 264 HIS PRO ASN TRP VAL LEU ASP CYS ILE ALA TYR LYS ARG
SEQRES 8 C 264 LEU ILE LEU ILE GLU PRO ASN TYR CYS PHE ASN VAL SER
SEQRES 9 C 264 GLN LYS MET ARG ALA VAL ALA GLU LYS ARG VAL ASP CYS
SEQRES 10 C 264 LEU GLY ASP SER PHE GLU ASN ASP ILE SER GLU THR LYS
SEQRES 11 C 264 LEU SER SER LEU TYR LYS SER GLN LEU SER LEU PRO PRO
SEQRES 12 C 264 MET GLY GLU LEU GLU ILE ASP SER GLU VAL ARG ARG PHE
SEQRES 13 C 264 PRO LEU PHE LEU PHE SER ASN ARG ILE ALA TYR VAL PRO
SEQRES 14 C 264 ARG ARG LYS ILE SER THR GLU ASP ASP ILE ILE GLU MET
SEQRES 15 C 264 LYS ILE LYS LEU PHE GLY GLY LYS ILE THR ASP GLN GLN
SEQRES 16 C 264 SER LEU CYS ASN LEU ILE ILE ILE PRO TYR THR ASP PRO
SEQRES 17 C 264 ILE LEU ARG LYS ASP CYS MET ASN GLU VAL HIS GLU LYS
SEQRES 18 C 264 ILE LYS GLU GLN ILE LYS ALA SER ASP THR ILE PRO LYS
SEQRES 19 C 264 ILE ALA ARG VAL VAL ALA PRO GLU TRP VAL ASP HIS SER
SEQRES 20 C 264 ILE ASN GLU ASN CYS GLN VAL PRO GLU GLU ASP PHE PRO
SEQRES 21 C 264 VAL VAL ASN TYR
SEQRES 1 D 8 UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 E 7 UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 F 45 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 F 45 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 F 45 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 4 F 45 UNK UNK UNK UNK UNK UNK
SEQRES 1 G 37 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 G 37 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 G 37 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 H 7 UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 I 30 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 I 30 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 3 I 30 UNK UNK UNK UNK
SEQRES 1 J 20 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 J 20 UNK UNK UNK UNK UNK UNK UNK
SEQRES 1 K 13 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
HELIX 1 1 ALA A 159 ARG A 231 1 73
HELIX 2 2 PHE B 156 ILE B 229 1 74
HELIX 3 3 GLU C 710 GLY C 720 1 11
HELIX 4 4 GLU C 746 ILE C 751 1 6
HELIX 5 5 ASN C 761 ALA C 768 1 8
HELIX 6 6 LYS C 786 ASP C 796 1 11
HELIX 7 7 SER C 807 LYS C 816 1 10
HELIX 8 8 LYS C 862 GLY C 868 1 7
HELIX 9 9 LEU C 889 SER C 908 1 20
HELIX 10 10 PRO C 920 ILE C 927 1 8
SHEET 1 A 4 SER C 695 THR C 699 0
SHEET 2 A 4 TYR C 724 VAL C 726 1 O ASN C 725 N SER C 695
SHEET 3 A 4 ARG C 737 CYS C 741 1 O LEU C 738 N TYR C 724
SHEET 4 A 4 ASP C 756 HIS C 759 1 O ILE C 757 N ARG C 737
SHEET 1 B 6 VAL C 795 CYS C 797 0
SHEET 2 B 6 GLY C 799 SER C 801 1 O ASP C 800 N VAL C 795
SHEET 1 C10 PRO C 837 PHE C 839 0
SHEET 2 C10 THR C 871 GLN C 874 1 O ASP C 872 N PRO C 837
SHEET 3 C10 ASN C 878 ILE C 881 1 O LEU C 879 N THR C 871
SHEET 4 C10 ALA C 915 VAL C 918 1 O ARG C 916 N ASN C 878
CISPEP 1 HIS C 759 PRO C 760 0 -27.11
CRYST1 247.617 247.617 98.416 90.00 90.00 120.00 P 64 2 2 24
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 0.004038 0.002332 0.000000 0.00000
SCALE2 0.000000 0.004663 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
