HEADER STRUCTURAL PROTEIN/DNA 24-FEB-10 3AFA
TITLE THE HUMAN NUCLEOSOME STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.1;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: HISTONE H3/A, HISTONE H3/B, HISTONE H3/C, HISTONE H3/D,
COMPND 5 HISTONE H3/F, HISTONE H3/H, HISTONE H3/I, HISTONE H3/J, HISTONE H3/K,
COMPND 6 HISTONE H3/L;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H4;
COMPND 10 CHAIN: B, F;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HISTONE H2A TYPE 1-B/E;
COMPND 14 CHAIN: C, G;
COMPND 15 SYNONYM: HISTONE H2A/M, HISTONE H2A/A, HISTONE H2A.2;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: HISTONE H2B TYPE 1-J;
COMPND 19 CHAIN: D, H;
COMPND 20 SYNONYM: HISTONE H2B.R, H2B/R, HISTONE H2B.1;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 5;
COMPND 23 MOLECULE: 146-MER DNA;
COMPND 24 CHAIN: I, J;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: H3.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHCE;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: H4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 GENE: H2A;
SOURCE 26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 27 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 30 EXPRESSION_SYSTEM_PLASMID: PHCE;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 33 ORGANISM_COMMON: HUMAN;
SOURCE 34 ORGANISM_TAXID: 9606;
SOURCE 35 GENE: H2B;
SOURCE 36 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 37 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 38 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 39 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 40 EXPRESSION_SYSTEM_PLASMID: PHCE;
SOURCE 41 MOL_ID: 5;
SOURCE 42 SYNTHETIC: YES
KEYWDS HISTONE-FOLD, DNA-BINDING PROTEIN, CHROMOSOMAL PROTEIN,
KEYWDS 2 CITRULLINATION, DNA-BINDING, METHYLATION, NUCLEOSOME CORE, NUCLEUS,
KEYWDS 3 PHOSPHOPROTEIN, ISOPEPTIDE BOND, ANTIBIOTIC, ANTIMICROBIAL,
KEYWDS 4 STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.TACHIWANA,W.KAGAWA,A.OSAKABE,K.KOICHIRO,T.SHIGA,H.KIMURA,
AUTHOR 2 H.KURUMIZAKA
REVDAT 3 18-JUL-12 3AFA 1 ATOM DBREF REMARK VERSN
REVDAT 2 02-JUN-10 3AFA 1 JRNL
REVDAT 1 26-MAY-10 3AFA 0
JRNL AUTH H.TACHIWANA,W.KAGAWA,A.OSAKABE,K.KAWAGUCHI,T.SHIGA,
JRNL AUTH 2 Y.HAYASHI-TAKANAKA,H.KIMURA,H.KURUMIZAKA
JRNL TITL STRUCTURAL BASIS OF INSTABILITY OF THE NUCLEOSOME CONTAINING
JRNL TITL 2 A TESTIS-SPECIFIC HISTONE VARIANT, HUMAN H3T
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 10454 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20498094
JRNL DOI 10.1073/PNAS.1003064107
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 73269
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3693
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE : 0.3900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 371
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 : 6023
REMARK 3 NUCLEIC ACID ATOMS : 5980
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.40
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.35
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.11
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.03
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 3AFA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB029180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73546
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.91800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2CV5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM CACODYLATE, POTASSIUM
REMARK 280 CHLORIDE, MANGANESE CHLORIDE, PH 6.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 52.91950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.45950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.75450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.45950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.91950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.75450
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: 56370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -410.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J, C, D, E, F, G, H
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 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
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 ALA A 135
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 HIS B -1
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 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 ASP B 24
REMARK 465 GLY C -3
REMARK 465 SER C -2
REMARK 465 HIS C -1
REMARK 465 MET C 0
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 ALA C 10
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 HIS C 123
REMARK 465 HIS C 124
REMARK 465 LYS C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 GLY C 128
REMARK 465 LYS C 129
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 HIS D -1
REMARK 465 MET D 0
REMARK 465 PRO D 1
REMARK 465 GLU D 2
REMARK 465 PRO D 3
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 ALA D 21
REMARK 465 GLN D 22
REMARK 465 LYS D 23
REMARK 465 LYS D 24
REMARK 465 ASP D 25
REMARK 465 GLY D 26
REMARK 465 LYS D 27
REMARK 465 LYS D 28
REMARK 465 ARG D 29
REMARK 465 GLY E -3
REMARK 465 SER E -2
REMARK 465 HIS E -1
REMARK 465 MET E 0
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 GLY F -3
REMARK 465 SER F -2
REMARK 465 HIS F -1
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 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 LYS F 16
REMARK 465 ARG F 17
REMARK 465 HIS F 18
REMARK 465 GLY G -3
REMARK 465 SER G -2
REMARK 465 HIS G -1
REMARK 465 MET G 0
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 ALA 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 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 HIS G 123
REMARK 465 HIS G 124
REMARK 465 LYS G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 GLY G 128
REMARK 465 LYS G 129
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 HIS H -1
REMARK 465 MET H 0
REMARK 465 PRO H 1
REMARK 465 GLU H 2
REMARK 465 PRO H 3
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 ALA 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 465 ARG H 29
REMARK 465 LYS H 30
REMARK 465 ARG H 31
REMARK 465 SER H 32
REMARK 465 LYS H 125
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 THR B 96 129.21 -37.45
REMARK 500 ASN C 110 111.09 -162.38
REMARK 500 SER D 32 72.84 80.51
REMARK 500 LYS D 85 24.24 45.83
REMARK 500 SER D 123 12.69 -64.06
REMARK 500 ALA D 124 -19.25 68.12
REMARK 500 ARG E 134 33.27 -167.65
REMARK 500 ASP F 24 19.65 54.75
REMARK 500 LYS H 34 76.91 73.50
REMARK 500 SER H 123 -70.71 -60.18
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 D 201 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 301 O
REMARK 620 2 VAL D 48 O 78.6
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 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 MN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 304
DBREF 3AFA A 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 3AFA B 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 3AFA C 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 3AFA D 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 3AFA E 0 135 UNP P68431 H31_HUMAN 1 136
DBREF 3AFA F 0 102 UNP P62805 H4_HUMAN 1 103
DBREF 3AFA G 0 129 UNP P04908 H2A1B_HUMAN 1 130
DBREF 3AFA H 0 125 UNP P06899 H2B1J_HUMAN 1 126
DBREF 3AFA I 1 146 PDB 3AFA 3AFA 1 146
DBREF 3AFA J 147 292 PDB 3AFA 3AFA 147 292
SEQADV 3AFA GLY A -3 UNP P68431 EXPRESSION TAG
SEQADV 3AFA SER A -2 UNP P68431 EXPRESSION TAG
SEQADV 3AFA HIS A -1 UNP P68431 EXPRESSION TAG
SEQADV 3AFA GLY B -3 UNP P62805 EXPRESSION TAG
SEQADV 3AFA SER B -2 UNP P62805 EXPRESSION TAG
SEQADV 3AFA HIS B -1 UNP P62805 EXPRESSION TAG
SEQADV 3AFA GLY C -3 UNP P04908 EXPRESSION TAG
SEQADV 3AFA SER C -2 UNP P04908 EXPRESSION TAG
SEQADV 3AFA HIS C -1 UNP P04908 EXPRESSION TAG
SEQADV 3AFA GLY D -3 UNP P06899 EXPRESSION TAG
SEQADV 3AFA SER D -2 UNP P06899 EXPRESSION TAG
SEQADV 3AFA HIS D -1 UNP P06899 EXPRESSION TAG
SEQADV 3AFA GLY E -3 UNP P68431 EXPRESSION TAG
SEQADV 3AFA SER E -2 UNP P68431 EXPRESSION TAG
SEQADV 3AFA HIS E -1 UNP P68431 EXPRESSION TAG
SEQADV 3AFA GLY F -3 UNP P62805 EXPRESSION TAG
SEQADV 3AFA SER F -2 UNP P62805 EXPRESSION TAG
SEQADV 3AFA HIS F -1 UNP P62805 EXPRESSION TAG
SEQADV 3AFA GLY G -3 UNP P04908 EXPRESSION TAG
SEQADV 3AFA SER G -2 UNP P04908 EXPRESSION TAG
SEQADV 3AFA HIS G -1 UNP P04908 EXPRESSION TAG
SEQADV 3AFA GLY H -3 UNP P06899 EXPRESSION TAG
SEQADV 3AFA SER H -2 UNP P06899 EXPRESSION TAG
SEQADV 3AFA HIS H -1 UNP P06899 EXPRESSION TAG
SEQRES 1 A 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 A 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 A 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 A 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 A 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 A 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 A 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 A 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 A 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 A 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 A 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 B 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 B 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 B 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 B 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 B 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 B 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 B 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 B 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 B 106 GLY GLY
SEQRES 1 C 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 C 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 C 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 C 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 C 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 C 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 C 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 C 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 C 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 C 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 C 133 LYS GLY LYS
SEQRES 1 D 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 D 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 D 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 D 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 D 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 D 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 D 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 D 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 D 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 D 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 139 GLY SER HIS MET ALA ARG THR LYS GLN THR ALA ARG LYS
SEQRES 2 E 139 SER THR GLY GLY LYS ALA PRO ARG LYS GLN LEU ALA THR
SEQRES 3 E 139 LYS ALA ALA ARG LYS SER ALA PRO ALA THR GLY GLY VAL
SEQRES 4 E 139 LYS LYS PRO HIS ARG TYR ARG PRO GLY THR VAL ALA LEU
SEQRES 5 E 139 ARG GLU ILE ARG ARG TYR GLN LYS SER THR GLU LEU LEU
SEQRES 6 E 139 ILE ARG LYS LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE
SEQRES 7 E 139 ALA GLN ASP PHE LYS THR ASP LEU ARG PHE GLN SER SER
SEQRES 8 E 139 ALA VAL MET ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU
SEQRES 9 E 139 VAL GLY LEU PHE GLU ASP THR ASN LEU CYS ALA ILE HIS
SEQRES 10 E 139 ALA LYS ARG VAL THR ILE MET PRO LYS ASP ILE GLN LEU
SEQRES 11 E 139 ALA ARG ARG ILE ARG GLY GLU ARG ALA
SEQRES 1 F 106 GLY SER HIS MET SER GLY ARG GLY LYS GLY GLY LYS GLY
SEQRES 2 F 106 LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG LYS VAL LEU
SEQRES 3 F 106 ARG ASP ASN ILE GLN GLY ILE THR LYS PRO ALA ILE ARG
SEQRES 4 F 106 ARG LEU ALA ARG ARG GLY GLY VAL LYS ARG ILE SER GLY
SEQRES 5 F 106 LEU ILE TYR GLU GLU THR ARG GLY VAL LEU LYS VAL PHE
SEQRES 6 F 106 LEU GLU ASN VAL ILE ARG ASP ALA VAL THR TYR THR GLU
SEQRES 7 F 106 HIS ALA LYS ARG LYS THR VAL THR ALA MET ASP VAL VAL
SEQRES 8 F 106 TYR ALA LEU LYS ARG GLN GLY ARG THR LEU TYR GLY PHE
SEQRES 9 F 106 GLY GLY
SEQRES 1 G 133 GLY SER HIS MET SER GLY ARG GLY LYS GLN GLY GLY LYS
SEQRES 2 G 133 ALA ARG ALA LYS ALA LYS THR ARG SER SER ARG ALA GLY
SEQRES 3 G 133 LEU GLN PHE PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG
SEQRES 4 G 133 LYS GLY ASN TYR SER GLU ARG VAL GLY ALA GLY ALA PRO
SEQRES 5 G 133 VAL TYR LEU ALA ALA VAL LEU GLU TYR LEU THR ALA GLU
SEQRES 6 G 133 ILE LEU GLU LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS
SEQRES 7 G 133 LYS THR ARG ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE
SEQRES 8 G 133 ARG ASN ASP GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL
SEQRES 9 G 133 THR ILE ALA GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA
SEQRES 10 G 133 VAL LEU LEU PRO LYS LYS THR GLU SER HIS HIS LYS ALA
SEQRES 11 G 133 LYS GLY LYS
SEQRES 1 H 129 GLY SER HIS MET PRO GLU PRO ALA LYS SER ALA PRO ALA
SEQRES 2 H 129 PRO LYS LYS GLY SER LYS LYS ALA VAL THR LYS ALA GLN
SEQRES 3 H 129 LYS LYS ASP GLY LYS LYS ARG LYS ARG SER ARG LYS GLU
SEQRES 4 H 129 SER TYR SER ILE TYR VAL TYR LYS VAL LEU LYS GLN VAL
SEQRES 5 H 129 HIS PRO ASP THR GLY ILE SER SER LYS ALA MET GLY ILE
SEQRES 6 H 129 MET ASN SER PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA
SEQRES 7 H 129 GLY GLU ALA SER ARG LEU ALA HIS TYR ASN LYS ARG SER
SEQRES 8 H 129 THR ILE THR SER ARG GLU ILE GLN THR ALA VAL ARG LEU
SEQRES 9 H 129 LEU LEU PRO GLY GLU LEU ALA LYS HIS ALA VAL SER GLU
SEQRES 10 H 129 GLY THR LYS ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 146 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 I 146 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 I 146 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 I 146 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 I 146 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 I 146 DC DA DG DC DT DG DA DA DT DT DC DA DG
SEQRES 7 I 146 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 I 146 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 I 146 DT DT DC DC DA DA DA DT DA DC DA DC DT
SEQRES 10 I 146 DT DT DT DG DG DT DA DG DA DA DT DC DT
SEQRES 11 I 146 DG DC DA DG DG DT DG DG DA DT DA DT DT
SEQRES 12 I 146 DG DA DT
SEQRES 1 J 146 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 J 146 DT DG DC DA DG DA DT DT DC DT DA DC DC
SEQRES 3 J 146 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 J 146 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 J 146 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 J 146 DC DA DG DC DT DG DA DA DT DT DC DA DG
SEQRES 7 J 146 DC DT DG DA DA DC DA DT DG DC DC DT DT
SEQRES 8 J 146 DT DT DG DA DT DG DG DA DG DC DA DG DT
SEQRES 9 J 146 DT DT DC DC DA DA DA DT DA DC DA DC DT
SEQRES 10 J 146 DT DT DT DG DG DT DA DG DA DA DT DC DT
SEQRES 11 J 146 DG DC DA DG DG DT DG DG DA DT DA DT DT
SEQRES 12 J 146 DG DA DT
HET CL A 201 1
HET CL C 201 1
HET MN D 201 1
HET CL E 201 1
HET CL G 201 1
HET MN I 201 1
HET MN I 202 1
HET MN I 203 1
HET MN J 301 1
HET MN J 302 1
HET MN J 303 1
HET MN J 304 1
HETNAM CL CHLORIDE ION
HETNAM MN MANGANESE (II) ION
FORMUL 11 CL 4(CL 1-)
FORMUL 13 MN 8(MN 2+)
FORMUL 23 HOH *183(H2 O)
HELIX 1 1 GLY A 44 SER A 57 1 14
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 THR C 16 GLY C 22 1 7
HELIX 10 10 PRO C 26 LYS C 36 1 11
HELIX 11 11 ALA C 45 ASN C 73 1 29
HELIX 12 12 ILE C 79 ASP C 90 1 12
HELIX 13 13 ASP C 90 LEU C 97 1 8
HELIX 14 14 GLN C 112 LEU C 116 5 5
HELIX 15 15 TYR D 37 HIS D 49 1 13
HELIX 16 16 SER D 55 ASN D 84 1 30
HELIX 17 17 THR D 90 LEU D 102 1 13
HELIX 18 18 PRO D 103 SER D 123 1 21
HELIX 19 19 GLY E 44 GLN E 55 1 12
HELIX 20 20 ARG E 63 LYS E 79 1 17
HELIX 21 21 GLN E 85 ALA E 114 1 30
HELIX 22 22 MET E 120 ARG E 131 1 12
HELIX 23 23 ASP F 24 ILE F 29 5 6
HELIX 24 24 THR F 30 GLY F 41 1 12
HELIX 25 25 LEU F 49 ALA F 76 1 28
HELIX 26 26 THR F 82 GLN F 93 1 12
HELIX 27 27 THR G 16 GLY G 22 1 7
HELIX 28 28 PRO G 26 GLY G 37 1 12
HELIX 29 29 ALA G 45 ASP G 72 1 28
HELIX 30 30 ILE G 79 ASN G 89 1 11
HELIX 31 31 ASP G 90 LEU G 97 1 8
HELIX 32 32 GLN G 112 LEU G 116 5 5
HELIX 33 33 TYR H 37 HIS H 49 1 13
HELIX 34 34 SER H 55 ASN H 84 1 30
HELIX 35 35 THR H 90 LEU H 102 1 13
HELIX 36 36 PRO H 103 ALA H 124 1 22
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 LEU B 97 TYR B 98 0
SHEET 2 C 2 THR G 101 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 88 ILE D 89 1 O ILE D 89 N ARG C 42
SHEET 1 E 2 ARG C 77 ILE C 78 0
SHEET 2 E 2 GLY D 53 ILE D 54 1 O GLY D 53 N ILE C 78
SHEET 1 F 2 VAL C 100 ILE C 102 0
SHEET 2 F 2 THR F 96 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 88 ILE H 89 1 O ILE H 89 N ARG G 42
SHEET 1 J 2 ARG G 77 ILE G 78 0
SHEET 2 J 2 GLY H 53 ILE H 54 1 O GLY H 53 N ILE G 78
LINK MN MN D 201 O HOH D 301 1555 1555 2.07
LINK O VAL D 48 MN MN D 201 1555 1555 2.31
LINK N7 DG J 217 MN MN J 303 1555 1555 2.32
LINK N7 DG J 280 MN MN J 304 1555 1555 2.58
LINK N7 DG I 121 MN MN I 202 1555 1555 2.67
LINK N7 DG J 267 MN MN J 302 1555 1555 2.80
CISPEP 1 LYS E 37 PRO E 38 0 -0.72
SITE 1 AC1 3 MET A 120 PRO A 121 LYS A 122
SITE 1 AC2 4 GLY C 46 ALA C 47 THR D 90 SER D 91
SITE 1 AC3 3 VAL D 48 HOH D 301 ASP E 77
SITE 1 AC4 1 LYS E 122
SITE 1 AC5 6 GLY G 44 ALA G 45 GLY G 46 ALA G 47
SITE 2 AC5 6 THR H 90 SER H 91
SITE 1 AC6 1 DG I 68
SITE 1 AC7 3 DG I 121 DG I 122 DC J 171
SITE 1 AC8 1 DA I 133
SITE 1 AC9 2 DG J 185 DG J 186
SITE 1 BC1 1 DG J 267
SITE 1 BC2 1 DG J 217
SITE 1 BC3 1 DG J 280
CRYST1 105.839 109.509 180.919 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 0.009448 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009132 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005527 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
