HEADER STRUCTURAL PROTEIN/DNA 25-NOV-11 3UT9
TITLE CRYSTAL STRUCTURE OF NUCLEOSOME CORE PARTICLE ASSEMBLED WITH A
TITLE 2 PALINDROMIC WIDOM '601' DERIVATIVE (NCP-601L)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.2;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A;
COMPND 11 CHAIN: C, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H2B 1.1;
COMPND 15 CHAIN: D, H;
COMPND 16 SYNONYM: H2B1.1;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: 145-MER DNA;
COMPND 20 CHAIN: I;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: 145-MER DNA;
COMPND 24 CHAIN: J;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 12 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 13 ORGANISM_TAXID: 8355;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 21 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 22 ORGANISM_TAXID: 8355;
SOURCE 23 GENE: HIST1H2AJ, LOC494591;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 28 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 29 MOL_ID: 4;
SOURCE 30 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 31 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 32 ORGANISM_TAXID: 8355;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 35 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 36 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 37 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 38 MOL_ID: 5;
SOURCE 39 SYNTHETIC: YES;
SOURCE 40 OTHER_DETAILS: SYNTHETIC CONSTRUCT;
SOURCE 41 MOL_ID: 6;
SOURCE 42 SYNTHETIC: YES;
SOURCE 43 OTHER_DETAILS: SYNTHETIC CONSTRUCT
KEYWDS NUCLEOSOME CORE PARTICLE, NCP, 601-SEQUENCE DNA, STRUCTURAL PROTEIN-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.Y.D.CHUA,D.VASUDEVAN,G.E.DAVEY,B.WU,C.A.DAVEY
REVDAT 3 20-MAR-24 3UT9 1 REMARK LINK
REVDAT 2 26-JUN-13 3UT9 1 JRNL
REVDAT 1 11-APR-12 3UT9 0
JRNL AUTH E.Y.D.CHUA,D.VASUDEVAN,G.E.DAVEY,B.WU,C.A.DAVEY
JRNL TITL THE MECHANICS BEHIND DNA SEQUENCE-DEPENDENT PROPERTIES OF
JRNL TITL 2 THE NUCLEOSOME
JRNL REF NUCLEIC ACIDS RES. V. 40 6338 2012
JRNL REFN ISSN 0305-1048
JRNL PMID 22453276
JRNL DOI 10.1093/NAR/GKS261
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 104004
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) : 0.257
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2083
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7351
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3570
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.4030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6068
REMARK 3 NUCLEIC ACID ATOMS : 5939
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.37000
REMARK 3 B22 (A**2) : -4.73000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.244
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.836
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12811 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18543 ; 1.362 ; 2.543
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 754 ; 6.071 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;33.411 ;21.131
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1173 ;18.952 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 89 ;19.361 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2108 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7558 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4701 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7929 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 432 ; 0.158 ; 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): 36 ; 0.290 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.338 ; 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): 3782 ; 0.795 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6085 ; 1.416 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9494 ; 1.256 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12458 ; 1.886 ; 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 : 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 3UT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 0.80
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 92.819
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.50700
REMARK 200 R SYM FOR SHELL (I) : 0.50700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: K-CACODYLATE, KCL, MNCL2, PH 6.0,
REMARK 280 TEMPERATURE 291K, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 53.24700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.41100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.76650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.41100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.24700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.76650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 62460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -531.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 LYS A 37
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 LYS B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 THR C 10
REMARK 465 ARG C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 SER C 123
REMARK 465 LYS C 124
REMARK 465 SER C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 SER C 128
REMARK 465 LYS C 129
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 THR D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 LYS D 122
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 ALA E 135
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 THR G 10
REMARK 465 ARG G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 13
REMARK 465 ALA G 14
REMARK 465 LYS G 15
REMARK 465 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 SER G 123
REMARK 465 LYS G 124
REMARK 465 SER G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 SER G 128
REMARK 465 LYS G 129
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 THR H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
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 LEU G 55 OG1 THR G 59 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL E 101 CA VAL E 101 CB -0.127
REMARK 500 VAL E 101 CB VAL E 101 CG2 0.222
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 ARG C 88 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 88 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT I -71 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG I -58 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 DG I -52 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I -51 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I -50 O4' - C1' - N1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DG I -49 C3' - C2' - C1' ANGL. DEV. = -5.6 DEGREES
REMARK 500 DT I -47 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT I -43 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG I -41 C3' - O3' - P ANGL. DEV. = 7.4 DEGREES
REMARK 500 DG I -40 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DC I -38 C3' - O3' - P ANGL. DEV. = 7.7 DEGREES
REMARK 500 DT I -36 O4' - C1' - N1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DA I -33 C3' - O3' - P ANGL. DEV. = 8.0 DEGREES
REMARK 500 DC I -32 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DA I -31 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I -29 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC I -27 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I -21 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC I -20 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DC I -18 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC I -10 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC I -8 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC I -4 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DT I 1 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC I 7 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DG I 8 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC I 11 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT I 14 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DA I 16 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG I 20 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG I 20 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 DG I 21 O4' - C1' - N9 ANGL. DEV. = 6.5 DEGREES
REMARK 500 DT I 22 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DG I 23 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG I 29 C3' - C2' - C1' ANGL. DEV. = -8.0 DEGREES
REMARK 500 DG I 29 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DC I 30 O4' - C1' - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DT I 31 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DG I 32 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I 34 C3' - O3' - P ANGL. DEV. = 8.2 DEGREES
REMARK 500 DT I 44 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I 49 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I 52 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DT I 54 C3' - O3' - P ANGL. DEV. = 9.0 DEGREES
REMARK 500 DC I 58 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I 61 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG I 62 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG I 63 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 111 ANGLE DEVIATIONS.
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 HIS A 39 138.13 -179.34
REMARK 500 ASP A 81 77.90 56.96
REMARK 500 ALA A 114 33.69 -98.51
REMARK 500 LYS C 36 34.32 -75.64
REMARK 500 LYS C 74 32.08 74.34
REMARK 500 LEU C 97 40.52 -101.35
REMARK 500 ALA C 103 137.13 -35.91
REMARK 500 ARG D 27 100.85 89.46
REMARK 500 HIS D 46 86.44 -159.01
REMARK 500 SER D 88 -27.71 -39.98
REMARK 500 ARG F 95 38.78 -140.61
REMARK 500 THR F 96 136.09 -36.18
REMARK 500 ASN G 110 104.80 -160.89
REMARK 500 ARG H 27 102.14 -171.95
REMARK 500 LYS H 28 -148.21 65.12
REMARK 500 THR H 29 96.99 97.16
REMARK 500 HIS H 46 73.42 -150.59
REMARK 500 LEU H 98 -74.23 -69.22
REMARK 500 SER H 120 33.14 -95.05
REMARK 500 ALA H 121 -2.39 -149.68
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 ARG H 27 LYS H 28 143.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E1001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 77 OD1
REMARK 620 2 HOH E 145 O 119.6
REMARK 620 3 HOH E 146 O 112.1 83.8
REMARK 620 4 HOH E 150 O 83.2 90.7 164.5
REMARK 620 5 HOH F 115 O 170.5 55.5 76.3 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K I1052 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT I -26 O2
REMARK 620 2 DA I -25 O4' 82.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I1007 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG I 50 N7
REMARK 620 2 HOH I 134 O 73.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J1004 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG J -34 N7
REMARK 620 2 HOH J 106 O 104.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K J1051 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT J -26 O2
REMARK 620 2 DA J -25 O4' 77.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1018
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1021
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1023
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1028
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K I 1052
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1015
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1017
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1024
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1025
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1026
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K J 1051
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNINTENTIONAL MUTATIONS OR VARIATIONS IN GENOMIC SOURCES.
DBREF 3UT9 A 1 135 UNP P84233 H32_XENLA 2 136
DBREF 3UT9 B 1 102 UNP P62799 H4_XENLA 2 103
DBREF 3UT9 C 1 129 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 3UT9 D -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 3UT9 E 1 135 UNP P84233 H32_XENLA 2 136
DBREF 3UT9 F 1 102 UNP P62799 H4_XENLA 2 103
DBREF 3UT9 G 1 129 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 3UT9 H -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 3UT9 I -72 72 PDB 3UT9 3UT9 -72 72
DBREF 3UT9 J -72 72 PDB 3UT9 3UT9 -72 72
SEQADV 3UT9 ALA A 102 UNP P84233 GLY 103 SEE REMARK 999
SEQADV 3UT9 THR D 29 UNP P02281 SER 33 SEE REMARK 999
SEQADV 3UT9 ALA E 102 UNP P84233 GLY 103 SEE REMARK 999
SEQADV 3UT9 THR H 29 UNP P02281 SER 33 SEE REMARK 999
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 129 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 C 129 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 C 129 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 C 129 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 C 129 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 C 129 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 C 129 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 C 129 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 C 129 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 C 129 LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 D 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 D 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 D 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 D 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 D 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 D 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 D 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 D 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 D 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 D 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 129 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 G 129 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 G 129 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 G 129 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 G 129 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 G 129 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 G 129 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 G 129 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 G 129 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 G 129 LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 H 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 H 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 H 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 H 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 H 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 H 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 H 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 H 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 H 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 H 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 145 DA DT DC DA DC DA DA DT DC DC DC DG DG
SEQRES 2 I 145 DT DG DC DC DG DA DG DG DC DC DG DC DT
SEQRES 3 I 145 DC DA DA DT DT DG DG DT DC DG DT DA DG
SEQRES 4 I 145 DA DC DA DG DC DT DC DT DA DG DC DA DC
SEQRES 5 I 145 DC DG DC DT DT DA DA DA DC DG DC DA DC
SEQRES 6 I 145 DG DT DA DC DG DG DA DA DT DC DC DG DT
SEQRES 7 I 145 DA DC DG DT DG DC DG DT DT DT DA DA DG
SEQRES 8 I 145 DC DG DG DT DG DC DT DA DG DA DG DC DT
SEQRES 9 I 145 DG DT DC DT DA DC DG DA DC DC DA DA DT
SEQRES 10 I 145 DT DG DA DG DC DG DG DC DC DT DC DG DG
SEQRES 11 I 145 DC DA DC DC DG DG DG DA DT DT DG DT DG
SEQRES 12 I 145 DA DT
SEQRES 1 J 145 DA DT DC DA DC DA DA DT DC DC DC DG DG
SEQRES 2 J 145 DT DG DC DC DG DA DG DG DC DC DG DC DT
SEQRES 3 J 145 DC DA DA DT DT DG DG DT DC DG DT DA DG
SEQRES 4 J 145 DA DC DA DG DC DT DC DT DA DG DC DA DC
SEQRES 5 J 145 DC DG DC DT DT DA DA DA DC DG DC DA DC
SEQRES 6 J 145 DG DT DA DC DG DG DA DT DT DC DC DG DT
SEQRES 7 J 145 DA DC DG DT DG DC DG DT DT DT DA DA DG
SEQRES 8 J 145 DC DG DG DT DG DC DT DA DG DA DG DC DT
SEQRES 9 J 145 DG DT DC DT DA DC DG DA DC DC DA DA DT
SEQRES 10 J 145 DT DG DA DG DC DG DG DC DC DT DC DG DG
SEQRES 11 J 145 DC DA DC DC DG DG DG DA DT DT DG DT DG
SEQRES 12 J 145 DA DT
HET CL C1102 1
HET MN E1001 1
HET CL G1101 1
HET MN I1003 1
HET MN I1005 1
HET MN I1006 1
HET MN I1007 1
HET MN I1011 1
HET MN I1013 1
HET MN I1014 1
HET MN I1016 1
HET MN I1018 1
HET MN I1019 1
HET MN I1021 1
HET MN I1023 1
HET MN I1027 1
HET MN I1028 1
HET K I1052 1
HET MN J1002 1
HET MN J1004 1
HET MN J1008 1
HET MN J1009 1
HET MN J1010 1
HET MN J1012 1
HET MN J1015 1
HET MN J1017 1
HET MN J1020 1
HET MN J1022 1
HET MN J1024 1
HET MN J1025 1
HET MN J1026 1
HET MN J1029 1
HET K J1051 1
HETNAM CL CHLORIDE ION
HETNAM MN MANGANESE (II) ION
HETNAM K POTASSIUM ION
FORMUL 11 CL 2(CL 1-)
FORMUL 12 MN 29(MN 2+)
FORMUL 28 K 2(K 1+)
FORMUL 44 HOH *140(H2 O)
HELIX 1 1 GLY A 44 GLN A 55 1 12
HELIX 2 2 ARG A 63 ASP A 77 1 15
HELIX 3 3 GLN A 85 ALA A 114 1 30
HELIX 4 4 MET A 120 ARG A 131 1 12
HELIX 5 5 ASN B 25 ILE B 29 5 5
HELIX 6 6 THR B 30 GLY B 41 1 12
HELIX 7 7 LEU B 49 ALA B 76 1 28
HELIX 8 8 THR B 82 GLN B 93 1 12
HELIX 9 9 PRO C 26 LYS C 36 1 11
HELIX 10 10 GLY C 46 ASN C 73 1 28
HELIX 11 11 ILE C 79 ASP C 90 1 12
HELIX 12 12 ASP C 90 LEU C 97 1 8
HELIX 13 13 GLN C 112 LEU C 116 5 5
HELIX 14 14 TYR D 34 HIS D 46 1 13
HELIX 15 15 SER D 52 ASN D 81 1 30
HELIX 16 16 THR D 87 LEU D 99 1 13
HELIX 17 17 PRO D 100 ALA D 121 1 22
HELIX 18 18 GLY E 44 SER E 57 1 14
HELIX 19 19 ARG E 63 ASP E 77 1 15
HELIX 20 20 GLN E 85 ALA E 114 1 30
HELIX 21 21 MET E 120 ARG E 131 1 12
HELIX 22 22 ASP F 24 ILE F 29 5 6
HELIX 23 23 THR F 30 ARG F 40 1 11
HELIX 24 24 LEU F 49 ALA F 76 1 28
HELIX 25 25 THR F 82 GLN F 93 1 12
HELIX 26 26 ARG G 17 GLY G 22 1 6
HELIX 27 27 PRO G 26 GLY G 37 1 12
HELIX 28 28 GLY G 46 ASN G 73 1 28
HELIX 29 29 ILE G 79 ASP G 90 1 12
HELIX 30 30 ASP G 90 LEU G 97 1 8
HELIX 31 31 GLN G 112 LEU G 116 5 5
HELIX 32 32 TYR H 34 HIS H 46 1 13
HELIX 33 33 SER H 52 ASN H 81 1 30
HELIX 34 34 THR H 87 LEU H 99 1 13
HELIX 35 35 PRO H 100 SER H 120 1 21
SHEET 1 A 2 ARG A 83 PHE A 84 0
SHEET 2 A 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 B 2 THR A 118 ILE A 119 0
SHEET 2 B 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 C 2 THR B 96 TYR B 98 0
SHEET 2 C 2 VAL G 100 ILE G 102 1 O THR G 101 N TYR B 98
SHEET 1 D 2 ARG C 42 VAL C 43 0
SHEET 2 D 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 E 2 ARG C 77 ILE C 78 0
SHEET 2 E 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 78
SHEET 1 F 2 THR C 101 ILE C 102 0
SHEET 2 F 2 LEU F 97 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 G 2 ARG E 83 PHE E 84 0
SHEET 2 G 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 H 2 THR E 118 ILE E 119 0
SHEET 2 H 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 I 2 ARG G 42 VAL G 43 0
SHEET 2 I 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 J 2 ARG G 77 ILE G 78 0
SHEET 2 J 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
LINK OD1 ASP E 77 MN MN E1001 1555 1555 2.22
LINK O HOH E 145 MN MN E1001 1555 1555 2.65
LINK O HOH E 146 MN MN E1001 1555 1555 1.79
LINK O HOH E 150 MN MN E1001 1555 1555 1.77
LINK MN MN E1001 O HOH F 115 1555 1555 2.11
LINK N7 DG I -61 MN MN I1003 1555 1555 2.32
LINK N7 DG I -53 MN MN I1016 1555 1555 2.61
LINK N7 DG I -34 MN MN I1011 1555 1555 2.75
LINK O2 DT I -26 K K I1052 1555 1555 2.95
LINK O4' DA I -25 K K I1052 1555 1555 3.49
LINK N7 DG I -3 MN MN I1005 1555 1555 2.43
LINK N7 DG I 27 MN MN I1018 1555 1555 2.66
LINK N7 DG I 38 MN MN I1006 1555 1555 2.61
LINK N7 DG I 50 MN MN I1007 1555 1555 2.48
LINK N7 DG I 63 MN MN I1023 1555 1555 2.45
LINK O HOH I 132 MN MN I1021 1555 1555 2.59
LINK O HOH I 134 MN MN I1007 1555 1555 2.28
LINK N7 DG J -61 MN MN J1017 1555 1555 2.35
LINK N7 DG J -53 MN MN J1022 1555 1555 2.69
LINK N7 DG J -34 MN MN J1004 1555 1555 2.19
LINK O2 DT J -26 K K J1051 1555 1555 3.03
LINK O4' DA J -25 K K J1051 1555 1555 3.30
LINK N7 DG J -3 MN MN J1002 1555 1555 2.68
LINK N7 DG J 20 MN MN J1015 1555 1555 2.73
LINK N7 DG J 27 MN MN J1009 1555 1555 2.66
LINK O6 DG J 29 MN MN J1024 1555 1555 2.65
LINK N7 DG J 38 MN MN J1012 1555 1555 2.67
LINK N7 DG J 62 MN MN J1010 1555 1555 2.35
LINK O HOH J 106 MN MN J1004 1555 1555 2.42
SITE 1 AC1 4 ALA C 45 GLY C 46 THR D 87 SER D 88
SITE 1 AC2 6 VAL D 45 ASP E 77 HOH E 145 HOH E 146
SITE 2 AC2 6 HOH E 150 HOH F 115
SITE 1 AC3 5 GLY G 44 GLY G 46 ALA G 47 THR H 87
SITE 2 AC3 5 SER H 88
SITE 1 AC4 1 DG I -61
SITE 1 AC5 2 DG I -3 DG I -2
SITE 1 AC6 1 DG I 38
SITE 1 AC7 3 DG I 50 DG I 51 HOH I 134
SITE 1 AC8 1 DG I -34
SITE 1 AC9 1 DG I 29
SITE 1 BC1 1 DG I -49
SITE 1 BC2 1 DG I -53
SITE 1 BC3 1 DG I 27
SITE 1 BC4 2 DG I 20 HOH I 132
SITE 1 BC5 2 DG I 62 DG I 63
SITE 1 BC6 1 DC I 3
SITE 1 BC7 2 DT I -26 DA I -25
SITE 1 BC8 1 DG J -3
SITE 1 BC9 2 DG J -34 HOH J 106
SITE 1 CC1 1 DG J 50
SITE 1 CC2 1 DG J 27
SITE 1 CC3 2 DG J 62 HOH J 129
SITE 1 CC4 1 DG J 38
SITE 1 CC5 2 DG J 20 DG J 21
SITE 1 CC6 2 DC J -62 DG J -61
SITE 1 CC7 1 DG J -49
SITE 1 CC8 1 DG J -53
SITE 1 CC9 1 DG J 29
SITE 1 DC1 1 DA J 36
SITE 1 DC2 1 DG J 63
SITE 1 DC3 2 DA J -25 DT J -26
CRYST1 106.494 109.533 174.822 90.00 90.00 90.00 P 21 21 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 0.009390 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009130 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005720 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
