HEADER DNA BINDING PROTEIN 09-DEC-15 5F99
TITLE X-RAY STRUCTURE OF THE MMTV-A NUCLEOSOME CORE PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.2;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H4;
COMPND 8 CHAIN: B, F;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HISTONE H2A TYPE 1;
COMPND 13 CHAIN: C, G;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: HISTONE H2B 1.1;
COMPND 17 CHAIN: D, H;
COMPND 18 SYNONYM: H2B1.1;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: DNA (147-MER);
COMPND 22 CHAIN: I;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 6;
COMPND 25 MOLECULE: DNA (147-MER);
COMPND 26 CHAIN: J;
COMPND 27 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 11 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 12 ORGANISM_TAXID: 8355;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 19 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 20 ORGANISM_TAXID: 8355;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 23 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 27 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 28 ORGANISM_TAXID: 8355;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 32 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 33 MOL_ID: 5;
SOURCE 34 ORGANISM_SCIENTIFIC: MOUSE MAMMARY TUMOR VIRUS;
SOURCE 35 ORGANISM_TAXID: 11757;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 316385;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: DH10B;
SOURCE 39 EXPRESSION_SYSTEM_PLASMID: PUC57;
SOURCE 40 MOL_ID: 6;
SOURCE 41 ORGANISM_SCIENTIFIC: MOUSE MAMMARY TUMOR VIRUS;
SOURCE 42 ORGANISM_TAXID: 11757;
SOURCE 43 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 44 EXPRESSION_SYSTEM_TAXID: 316385;
SOURCE 45 EXPRESSION_SYSTEM_STRAIN: DH10B;
SOURCE 46 EXPRESSION_SYSTEM_PLASMID: PUC57
KEYWDS NUCLEOSOME CORE PARTICLE HISTONE DNA, DNA BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.FROUWS,T.J.RICHMOND
REVDAT 3 10-JAN-24 5F99 1 LINK
REVDAT 2 10-FEB-16 5F99 1 JRNL
REVDAT 1 03-FEB-16 5F99 0
JRNL AUTH T.D.FROUWS,S.C.DUDA,T.J.RICHMOND
JRNL TITL X-RAY STRUCTURE OF THE MMTV-A NUCLEOSOME CORE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 1214 2016
JRNL REFN ESSN 1091-6490
JRNL PMID 26787910
JRNL DOI 10.1073/PNAS.1524607113
REMARK 2
REMARK 2 RESOLUTION. 2.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 59659
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6379
REMARK 3 NUCLEIC ACID ATOMS : 6029
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 936
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5F99 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59659
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 29.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.33300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1KX5
REMARK 200
REMARK 200 REMARK: HOLLOW HEXAGONAL RODS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SAMPLE WAS MIXED 1:1 WITH 10 MM K
REMARK 280 -CACODYLATE, PH 6.0, 180 MM MGCL2, 50 MM KCL AND EQUILIBRATED
REMARK 280 AGAINST A 1:4 DILUTION OF THE SAME SOLUTION, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
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 53.93650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.53050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 89.45750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.53050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.93650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 89.45750
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: 60110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 75870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -422.0 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 MET B 0
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 ARG B 18
REMARK 465 ARG B 19
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 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 ALA D 4
REMARK 465 LYS D 5
REMARK 465 SER D 6
REMARK 465 ALA D 7
REMARK 465 PRO D 8
REMARK 465 ALA D 9
REMARK 465 PRO D 10
REMARK 465 LYS D 11
REMARK 465 LYS D 12
REMARK 465 GLY D 13
REMARK 465 SER D 14
REMARK 465 LYS D 15
REMARK 465 LYS D 16
REMARK 465 ALA D 17
REMARK 465 VAL D 18
REMARK 465 THR D 19
REMARK 465 LYS D 20
REMARK 465 THR D 21
REMARK 465 GLN D 22
REMARK 465 LYS D 23
REMARK 465 LYS D 24
REMARK 465 ASP D 25
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 MET F 0
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 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 ALA H 4
REMARK 465 LYS H 5
REMARK 465 SER H 6
REMARK 465 ALA H 7
REMARK 465 PRO H 8
REMARK 465 ALA H 9
REMARK 465 PRO H 10
REMARK 465 LYS H 11
REMARK 465 LYS H 12
REMARK 465 GLY H 13
REMARK 465 SER H 14
REMARK 465 LYS H 15
REMARK 465 LYS H 16
REMARK 465 ALA H 17
REMARK 465 VAL H 18
REMARK 465 THR H 19
REMARK 465 LYS H 20
REMARK 465 THR H 21
REMARK 465 GLN H 22
REMARK 465 LYS H 23
REMARK 465 LYS H 24
REMARK 465 ASP H 25
REMARK 465 GLY H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 28
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 DA I -73 P DA I -73 OP3 -0.084
REMARK 500 DA J -73 P DA J -73 OP3 -0.085
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 PRO G 26 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO H 103 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 DG I 18 O3' - P - OP2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 DG I 29 C3' - C2' - C1' ANGL. DEV. = -5.2 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 PRO A 38 8.01 -57.40
REMARK 500 HIS A 39 18.84 49.78
REMARK 500 SER A 57 -163.02 -73.91
REMARK 500 THR A 58 -6.33 -168.89
REMARK 500 ASP A 81 96.56 50.73
REMARK 500 PHE A 84 -123.21 -92.75
REMARK 500 GLN A 85 89.13 169.54
REMARK 500 SER A 86 -45.63 -11.79
REMARK 500 VAL A 117 -4.15 -147.23
REMARK 500 LEU B 22 39.43 81.98
REMARK 500 ARG B 23 0.76 -64.12
REMARK 500 ASP B 24 -113.04 -121.93
REMARK 500 ASN B 25 -109.05 57.68
REMARK 500 ILE B 26 -7.64 -54.63
REMARK 500 LYS B 44 -78.60 -91.22
REMARK 500 THR B 96 133.47 -39.86
REMARK 500 PHE B 100 -30.84 -145.47
REMARK 500 LYS C 13 -118.46 39.28
REMARK 500 ALA C 14 123.01 179.84
REMARK 500 ARG C 17 -18.70 -46.28
REMARK 500 PRO C 26 89.26 -69.68
REMARK 500 ASN C 38 75.64 41.15
REMARK 500 ASN C 73 41.41 -101.98
REMARK 500 LYS C 74 47.27 35.59
REMARK 500 ASN C 110 116.49 -168.84
REMARK 500 VAL C 114 -18.21 -47.50
REMARK 500 LYS C 119 49.02 -73.25
REMARK 500 THR C 120 98.53 -163.36
REMARK 500 ARG D 30 79.69 71.15
REMARK 500 THR D 32 150.73 -44.90
REMARK 500 ASP D 51 30.40 -96.48
REMARK 500 LYS D 85 24.49 34.78
REMARK 500 SER D 123 -99.48 -88.36
REMARK 500 ALA D 124 130.35 -36.13
REMARK 500 ARG E 134 -69.51 -94.17
REMARK 500 ALA F 15 -85.20 -67.68
REMARK 500 LYS F 16 -51.13 173.80
REMARK 500 ARG F 17 126.40 75.34
REMARK 500 THR G 10 35.42 -74.85
REMARK 500 ARG G 11 146.92 55.00
REMARK 500 ALA G 14 -157.71 143.37
REMARK 500 LYS G 15 99.65 61.31
REMARK 500 ARG G 20 -4.52 -57.96
REMARK 500 PRO G 26 80.89 -62.45
REMARK 500 ASN G 68 -2.90 -57.02
REMARK 500 ARG G 71 -45.50 -172.30
REMARK 500 ASN G 73 12.42 -143.33
REMARK 500 LYS G 74 143.75 58.52
REMARK 500 LYS G 75 158.21 125.74
REMARK 500 VAL G 107 -158.98 -120.72
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 41 0.08 SIDE CHAIN
REMARK 500 DG I 26 0.06 SIDE CHAIN
REMARK 500 DA I 28 0.06 SIDE CHAIN
REMARK 500 DT J -13 0.07 SIDE CHAIN
REMARK 500 DG J -12 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 240 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH C 385 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH D 289 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH D 290 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH E 395 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH F 299 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH F 300 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH F 301 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH F 302 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH G 359 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH G 360 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH H 255 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH H 256 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH I 275 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH I 276 DISTANCE = 9.48 ANGSTROMS
REMARK 525 HOH J 289 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH J 290 DISTANCE = 8.34 ANGSTROMS
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 MG E 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 346 O
REMARK 620 2 VAL D 48 O 94.4
REMARK 620 3 ASP E 77 OD1 79.7 81.3
REMARK 620 4 HOH E 301 O 162.4 79.1 83.1
REMARK 620 5 HOH E 324 O 93.9 4.0 85.1 80.7
REMARK 620 6 HOH F 205 O 134.3 98.7 145.5 63.2 96.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 201
DBREF 5F99 A 1 135 UNP P84233 H32_XENLA 2 136
DBREF 5F99 B 0 102 UNP P62799 H4_XENLA 1 103
DBREF 5F99 C 1 129 UNP P06897 H2A1_XENLA 2 130
DBREF 5F99 D 4 125 UNP P02281 H2B11_XENLA 5 126
DBREF 5F99 E 1 135 UNP P84233 H32_XENLA 2 136
DBREF 5F99 F 0 102 UNP P62799 H4_XENLA 1 103
DBREF 5F99 G 1 129 UNP P06897 H2A1_XENLA 2 130
DBREF 5F99 H 4 125 UNP P02281 H2B11_XENLA 5 126
DBREF 5F99 I -73 73 PDB 5F99 5F99 -73 73
DBREF 5F99 J -73 73 PDB 5F99 5F99 -73 73
SEQADV 5F99 ALA A 102 UNP P84233 GLY 103 CONFLICT
SEQADV 5F99 ALA A 110 UNP P84233 CYS 111 CONFLICT
SEQADV 5F99 ARG B 18 UNP P62799 HIS 19 ENGINEERED MUTATION
SEQADV 5F99 ARG C 99 UNP P06897 GLY 100 CONFLICT
SEQADV 5F99 SER C 123 UNP P06897 ALA 124 CONFLICT
SEQADV 5F99 THR D 32 UNP P02281 SER 33 CONFLICT
SEQADV 5F99 ALA E 102 UNP P84233 GLY 103 CONFLICT
SEQADV 5F99 ALA E 110 UNP P84233 CYS 111 CONFLICT
SEQADV 5F99 ARG F 18 UNP P62799 HIS 19 ENGINEERED MUTATION
SEQADV 5F99 ARG G 99 UNP P06897 GLY 100 CONFLICT
SEQADV 5F99 SER G 123 UNP P06897 ALA 124 CONFLICT
SEQADV 5F99 THR H 32 UNP P02281 SER 33 CONFLICT
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 ALA 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 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 B 103 GLY GLY ALA LYS ARG ARG ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 B 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 B 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 B 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 B 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 B 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 B 103 LYS 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 122 ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS
SEQRES 2 D 122 ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG
SEQRES 3 D 122 ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR
SEQRES 4 D 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 D 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 D 122 VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA
SEQRES 7 D 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 D 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 D 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 D 122 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 ALA 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 103 MET SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS
SEQRES 2 F 103 GLY GLY ALA LYS ARG ARG ARG LYS VAL LEU ARG ASP ASN
SEQRES 3 F 103 ILE GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA
SEQRES 4 F 103 ARG ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR
SEQRES 5 F 103 GLU GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN
SEQRES 6 F 103 VAL ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS
SEQRES 7 F 103 ARG LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU
SEQRES 8 F 103 LYS 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 122 ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS
SEQRES 2 H 122 ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG
SEQRES 3 H 122 ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR
SEQRES 4 H 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 H 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 H 122 VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA
SEQRES 7 H 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 H 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 H 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 H 122 TYR THR SER ALA LYS
SEQRES 1 I 147 DA DT DC DT DG DC DA DA DC DA DG DT DC
SEQRES 2 I 147 DC DT DA DA DC DA DT DT DC DA DC DC DT
SEQRES 3 I 147 DC DT DT DG DT DG DT DG DT DT DT DG DT
SEQRES 4 I 147 DG DT DC DT DG DT DT DC DG DC DC DA DT
SEQRES 5 I 147 DC DC DC DG DT DC DT DC DC DG DC DT DC
SEQRES 6 I 147 DG DT DC DA DC DT DT DA DT DC DC DT DT
SEQRES 7 I 147 DC DA DC DT DT DT DC DC DA DG DA DG DG
SEQRES 8 I 147 DG DT DC DC DC DC DC DC DG DC DA DG DA
SEQRES 9 I 147 DC DC DC DC DG DG DC DG DA DC DC DC DT
SEQRES 10 I 147 DC DA DG DG DT DC DG DG DC DC DG DA DC
SEQRES 11 I 147 DT DG DC DG DG DC DA DC DA DG DT DT DT
SEQRES 12 I 147 DT DG DA DT
SEQRES 1 J 147 DA DT DC DA DA DA DA DC DT DG DT DG DC
SEQRES 2 J 147 DC DG DC DA DG DT DC DG DG DC DC DG DA
SEQRES 3 J 147 DC DC DT DG DA DG DG DG DT DC DG DC DC
SEQRES 4 J 147 DG DG DG DG DT DC DT DG DC DG DG DG DG
SEQRES 5 J 147 DG DG DA DC DC DC DT DC DT DG DG DA DA
SEQRES 6 J 147 DA DG DT DG DA DA DG DG DA DT DA DA DG
SEQRES 7 J 147 DT DG DA DC DG DA DG DC DG DG DA DG DA
SEQRES 8 J 147 DC DG DG DG DA DT DG DG DC DG DA DA DC
SEQRES 9 J 147 DA DG DA DC DA DC DA DA DA DC DA DC DA
SEQRES 10 J 147 DC DA DA DG DA DG DG DT DG DA DA DT DG
SEQRES 11 J 147 DT DT DA DG DG DA DC DT DG DT DT DG DC
SEQRES 12 J 147 DA DG DA DT
HET CL A 201 1
HET CL C 201 1
HET CL E 201 1
HET MG E 202 1
HET CL G 201 1
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 11 CL 4(CL 1-)
FORMUL 14 MG MG 2+
FORMUL 16 HOH *936(H2 O)
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 ASP A 77 1 15
HELIX 3 AA3 GLN A 85 ALA A 114 1 30
HELIX 4 AA4 PRO A 121 ARG A 131 1 11
HELIX 5 AA5 ASP B 24 GLY B 28 5 5
HELIX 6 AA6 THR B 30 GLY B 41 1 12
HELIX 7 AA7 LEU B 49 ALA B 76 1 28
HELIX 8 AA8 THR B 82 GLN B 93 1 12
HELIX 9 AA9 THR C 16 GLY C 22 1 7
HELIX 10 AB1 PRO C 26 GLY C 37 1 12
HELIX 11 AB2 GLY C 46 ASN C 73 1 28
HELIX 12 AB3 ILE C 79 ASN C 89 1 11
HELIX 13 AB4 ASP C 90 LEU C 97 1 8
HELIX 14 AB5 GLN C 112 LEU C 116 5 5
HELIX 15 AB6 TYR D 37 HIS D 49 1 13
HELIX 16 AB7 SER D 55 ASN D 84 1 30
HELIX 17 AB8 THR D 90 LEU D 102 1 13
HELIX 18 AB9 PRO D 103 SER D 123 1 21
HELIX 19 AC1 GLY E 44 SER E 57 1 14
HELIX 20 AC2 ARG E 63 ASP E 77 1 15
HELIX 21 AC3 GLN E 85 ALA E 114 1 30
HELIX 22 AC4 MET E 120 ARG E 131 1 12
HELIX 23 AC5 ASP F 24 ILE F 29 5 6
HELIX 24 AC6 THR F 30 GLY F 41 1 12
HELIX 25 AC7 LEU F 49 ALA F 76 1 28
HELIX 26 AC8 THR F 82 GLN F 93 1 12
HELIX 27 AC9 PRO G 26 GLY G 37 1 12
HELIX 28 AD1 ALA G 45 ASN G 68 1 24
HELIX 29 AD2 ILE G 79 ASP G 90 1 12
HELIX 30 AD3 ASP G 90 LEU G 97 1 8
HELIX 31 AD4 TYR H 37 HIS H 49 1 13
HELIX 32 AD5 SER H 56 ASN H 84 1 29
HELIX 33 AD6 THR H 90 LEU H 102 1 13
HELIX 34 AD7 PRO H 103 SER H 123 1 21
SHEET 1 AA1 2 THR A 118 ILE A 119 0
SHEET 2 AA1 2 ARG B 45 ILE B 46 1 O ARG B 45 N ILE A 119
SHEET 1 AA2 2 THR B 96 TYR B 98 0
SHEET 2 AA2 2 VAL G 100 ILE G 102 1 O THR G 101 N THR B 96
SHEET 1 AA3 2 ARG C 42 VAL C 43 0
SHEET 2 AA3 2 THR D 88 ILE D 89 1 O ILE D 89 N ARG C 42
SHEET 1 AA4 2 ARG C 77 ILE C 78 0
SHEET 2 AA4 2 GLY D 53 ILE D 54 1 O GLY D 53 N ILE C 78
SHEET 1 AA5 2 VAL C 100 ILE C 102 0
SHEET 2 AA5 2 THR F 96 TYR F 98 1 O TYR F 98 N THR C 101
SHEET 1 AA6 2 ARG E 83 PHE E 84 0
SHEET 2 AA6 2 THR F 80 VAL F 81 1 O VAL F 81 N ARG E 83
SHEET 1 AA7 2 THR E 118 ILE E 119 0
SHEET 2 AA7 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA8 2 ARG G 42 VAL G 43 0
SHEET 2 AA8 2 THR H 88 ILE H 89 1 O ILE H 89 N ARG G 42
SHEET 1 AA9 2 ARG G 77 ILE G 78 0
SHEET 2 AA9 2 GLY H 53 ILE H 54 1 O GLY H 53 N ILE G 78
LINK O HOH C 346 MG MG E 202 2554 1555 2.93
LINK O VAL D 48 MG MG E 202 1555 2555 2.33
LINK OD1 ASP E 77 MG MG E 202 1555 1555 2.47
LINK MG MG E 202 O HOH E 301 1555 1555 2.53
LINK MG MG E 202 O HOH E 324 1555 1555 2.30
LINK MG MG E 202 O HOH F 205 1555 1555 2.42
SITE 1 AC1 3 MET A 120 PRO A 121 LYS A 122
SITE 1 AC2 6 GLY C 44 ALA C 45 GLY C 46 ALA C 47
SITE 2 AC2 6 THR D 90 SER D 91
SITE 1 AC3 4 MET E 120 PRO E 121 LYS E 122 HOH F 294
SITE 1 AC4 7 GLU C 64 HOH C 346 VAL D 48 ASP E 77
SITE 2 AC4 7 HOH E 301 HOH E 324 HOH F 205
SITE 1 AC5 4 GLY G 46 ALA G 47 THR H 90 SER H 91
CRYST1 107.873 178.915 109.061 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 0.009270 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005589 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009169 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
