HEADER STRUCTURAL PROTEIN/DNA 16-MAY-07 2PYO
TITLE DROSOPHILA NUCLEOSOME CORE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (147-MER);
COMPND 3 CHAIN: I;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (147-MER);
COMPND 7 CHAIN: J;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H3;
COMPND 11 CHAIN: A, E;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H4;
COMPND 15 CHAIN: B, F;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: HISTONE H2A;
COMPND 19 CHAIN: C, G;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: HISTONE H2B;
COMPND 23 CHAIN: D, H;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 15 ORGANISM_COMMON: FRUIT FLY;
SOURCE 16 ORGANISM_TAXID: 7227;
SOURCE 17 GENE: HIS3;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 22 ORGANISM_COMMON: FRUIT FLY;
SOURCE 23 ORGANISM_TAXID: 7227;
SOURCE 24 GENE: HIS4, H4;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 MOL_ID: 5;
SOURCE 28 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 29 ORGANISM_COMMON: FRUIT FLY;
SOURCE 30 ORGANISM_TAXID: 7227;
SOURCE 31 GENE: HIS2A, H2A;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 34 MOL_ID: 6;
SOURCE 35 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 36 ORGANISM_COMMON: FRUIT FLY;
SOURCE 37 ORGANISM_TAXID: 7227;
SOURCE 38 GENE: HIS2B;
SOURCE 39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 40 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NUCLEOSOME CORE, HISTONE FOLD, STRUCTURAL PROTEIN/DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.CLAPIER,C.PETOSA,C.W.MUELLER
REVDAT 3 24-FEB-09 2PYO 1 VERSN
REVDAT 2 04-MAR-08 2PYO 1 JRNL
REVDAT 1 06-NOV-07 2PYO 0
JRNL AUTH C.R.CLAPIER,S.CHAKRAVARTHY,C.PETOSA,
JRNL AUTH 2 C.FERNANDEZ-TORNERO,K.LUGER,C.W.MULLER
JRNL TITL STRUCTURE OF THE DROSOPHILA NUCLEOSOME CORE
JRNL TITL 2 PARTICLE HIGHLIGHTS EVOLUTIONARY CONSTRAINTS ON
JRNL TITL 3 THE H2A-H2B HISTONE DIMER.
JRNL REF PROTEINS V. 71 1 2007
JRNL REFN ISSN 0887-3585
JRNL PMID 17957772
JRNL DOI 10.1002/PROT.21720
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.43 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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) : 2.43
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 500.00
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) (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 75234
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) : 0.229
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 3798
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 : 6112
REMARK 3 NUCLEIC ACID ATOMS : 6021
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.49700
REMARK 3 B22 (A**2) : -5.89000
REMARK 3 B33 (A**2) : 11.38700
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 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) : 0.009
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 : 50.66
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-07.
REMARK 100 THE RCSB ID CODE IS RCSB042931.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75234
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION WAS CARRIED OUT BY
REMARK 280 EQUILIBRATING A DROPLET CONTAINING 3 MG/ML NUCLEOSOME CORE
REMARK 280 PARTICLE, 80-85 MM MNCL2, 50-80 MM KCL AND 20 MM POTASSIUM
REMARK 280 CACODYLATE (PH 6.0) AGAINST A RESERVOIR SOLUTION CONTAINING OF
REMARK 280 40-42.5 MM MNCL2, 25-40 MM KCL AND 20 MM POTASSIUM CACODYLATE
REMARK 280 (PH 6.0). , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 53.01500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.71000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 91.02000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.71000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.01500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 91.02000
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 300 REMARK: THERE IS ONE NUCLEOSOME IN THE ASYMMETRIC UNIT,
REMARK 300 CONSISTING OF TWO COPIES EACH OF HISTONES H2A, H2B, H3 AND H4
REMARK 300 PLUS DOUBLE-STRANDED DNA.
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 APPLY THE FOLLOWING TO CHAINS: I, J, A, B, 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 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 THR 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 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 GLY C 6
REMARK 465 GLY C 7
REMARK 465 LYS C 8
REMARK 465 VAL C 9
REMARK 465 LYS C 10
REMARK 465 GLY C 11
REMARK 465 LYS C 12
REMARK 465 PRO D 1
REMARK 465 PRO D 2
REMARK 465 LYS D 3
REMARK 465 THR D 4
REMARK 465 SER D 5
REMARK 465 GLY D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 LYS D 10
REMARK 465 LYS D 11
REMARK 465 ALA D 12
REMARK 465 GLY D 13
REMARK 465 LYS D 14
REMARK 465 ALA D 15
REMARK 465 GLN D 16
REMARK 465 LYS D 17
REMARK 465 ASN D 18
REMARK 465 ILE D 19
REMARK 465 THR D 20
REMARK 465 LYS D 21
REMARK 465 THR D 22
REMARK 465 ASP D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 LYS D 26
REMARK 465 LYS D 27
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 THR 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 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 GLY G 6
REMARK 465 GLY G 7
REMARK 465 LYS G 8
REMARK 465 VAL G 9
REMARK 465 LYS G 10
REMARK 465 GLU G 120
REMARK 465 PRO H 1
REMARK 465 PRO H 2
REMARK 465 LYS H 3
REMARK 465 THR H 4
REMARK 465 SER H 5
REMARK 465 GLY H 6
REMARK 465 LYS H 7
REMARK 465 ALA H 8
REMARK 465 ALA H 9
REMARK 465 LYS H 10
REMARK 465 LYS H 11
REMARK 465 ALA H 12
REMARK 465 GLY H 13
REMARK 465 LYS H 14
REMARK 465 ALA H 15
REMARK 465 GLN H 16
REMARK 465 LYS H 17
REMARK 465 ASN H 18
REMARK 465 ILE H 19
REMARK 465 THR H 20
REMARK 465 LYS H 21
REMARK 465 THR H 22
REMARK 465 ASP H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 LYS H 26
REMARK 465 LYS H 27
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG B 23 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS C 117 CB CG CD CE NZ
REMARK 470 LYS C 118 CB CG CD CE NZ
REMARK 470 THR C 119 CB OG1 CG2
REMARK 470 GLU C 120 CB CG CD OE1 OE2
REMARK 470 LYS G 118 CB CG CD CE NZ
REMARK 470 THR G 119 CB OG1 CG2
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 DT I 67 C3' - C2' - C1' ANGL. DEV. = -4.8 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 ARG B 95 50.48 -113.26
REMARK 500 THR B 96 131.63 -35.65
REMARK 500 LYS C 14 109.92 -177.81
REMARK 500 PRO C 25 98.98 -64.04
REMARK 500 LYS C 117 179.09 149.42
REMARK 500 THR C 119 -106.91 60.89
REMARK 500 LYS D 29 113.64 66.78
REMARK 500 PRO E 38 154.54 -46.27
REMARK 500 LYS E 115 32.47 70.31
REMARK 500 HIS F 18 59.10 31.17
REMARK 500 ARG F 95 51.55 -109.42
REMARK 500 SER G 15 151.19 -49.07
REMARK 500 PRO G 25 88.26 -65.66
REMARK 500 ASN G 109 119.04 -166.25
REMARK 500 PRO G 116 140.42 -39.99
REMARK 500 LYS G 117 79.93 66.10
REMARK 500 LYS G 118 -110.03 77.78
REMARK 500 LYS H 29 101.24 -165.06
REMARK 500 SER H 120 38.50 -68.98
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 DG I -6 0.07 SIDE_CHAIN
REMARK 500 DG J -6 0.07 SIDE_CHAIN
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 E1002 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 77 OD1
REMARK 620 2 HOH E1029 O 81.4
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 MN I 1007
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1008
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1010
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1011
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1012
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1013
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1001
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1003
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1004
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1005
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1009
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1014
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1017
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1016
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 1002
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 1018
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1015
DBREF 2PYO I -73 73 PDB 2PYO 2PYO 1 147
DBREF 2PYO J -73 73 PDB 2PYO 2PYO 1 147
DBREF 2PYO A 1 135 UNP P02299 H3_DROME 2 136
DBREF 2PYO B 1 102 UNP P84040 H4_DROME 2 103
DBREF 2PYO C 1 120 UNP P84051 H2A_DROME 2 121
DBREF 2PYO D 1 122 UNP P02283 H2B_DROME 2 123
DBREF 2PYO E 1 135 UNP P02299 H3_DROME 2 136
DBREF 2PYO F 1 102 UNP P84040 H4_DROME 2 103
DBREF 2PYO G 1 120 UNP P84051 H2A_DROME 2 121
DBREF 2PYO H 1 122 UNP P02283 H2B_DROME 2 123
SEQRES 1 I 147 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 I 147 DT DG DC DA DG DA DT DA DC DT DA DC DC
SEQRES 3 I 147 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 I 147 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 I 147 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 I 147 DC DA DG DC DT DG DG DA DA DT DC DC DA
SEQRES 7 I 147 DG DC DT DG DA DA DC DA DT DG DC DC DT
SEQRES 8 I 147 DT DT DT DG DA DT DG DG DA DG DC DA DG
SEQRES 9 I 147 DT DT DT DC DC DA DA DA DT DA DC DA DC
SEQRES 10 I 147 DT DT DT DT DG DG DT DA DG DT DA DT DC
SEQRES 11 I 147 DT DG DC DA DG DG DT DG DG DA DT DA DT
SEQRES 12 I 147 DT DG DA DT
SEQRES 1 J 147 DA DT DC DA DA DT DA DT DC DC DA DC DC
SEQRES 2 J 147 DT DG DC DA DG DA DT DA DC DT DA DC DC
SEQRES 3 J 147 DA DA DA DA DG DT DG DT DA DT DT DT DG
SEQRES 4 J 147 DG DA DA DA DC DT DG DC DT DC DC DA DT
SEQRES 5 J 147 DC DA DA DA DA DG DG DC DA DT DG DT DT
SEQRES 6 J 147 DC DA DG DC DT DG DG DA DT DT DC DC DA
SEQRES 7 J 147 DG DC DT DG DA DA DC DA DT DG DC DC DT
SEQRES 8 J 147 DT DT DT DG DA DT DG DG DA DG DC DA DG
SEQRES 9 J 147 DT DT DT DC DC DA DA DA DT DA DC DA DC
SEQRES 10 J 147 DT DT DT DT DG DG DT DA DG DT DA DT DC
SEQRES 11 J 147 DT DG DC DA DG DG DT DG DG DA DT DA DT
SEQRES 12 J 147 DT DG DA DT
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 GLY 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 THR 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 120 SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA
SEQRES 2 C 120 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 3 C 120 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 4 C 120 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 5 C 120 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 6 C 120 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 7 C 120 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 8 C 120 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 9 C 120 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 10 C 120 LYS THR GLU
SEQRES 1 D 122 PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY
SEQRES 2 D 122 LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS
SEQRES 3 D 122 LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE 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 ILE PHE GLU ARG ILE ALA ALA 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 SER 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 GLY 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 THR 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 120 SER GLY ARG GLY LYS GLY GLY LYS VAL LYS GLY LYS ALA
SEQRES 2 G 120 LYS SER ARG SER ASN ARG ALA GLY LEU GLN PHE PRO VAL
SEQRES 3 G 120 GLY ARG ILE HIS ARG LEU LEU ARG LYS GLY ASN TYR ALA
SEQRES 4 G 120 GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA ALA
SEQRES 5 G 120 VAL MET GLU TYR LEU ALA ALA GLU VAL LEU GLU LEU ALA
SEQRES 6 G 120 GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE ILE
SEQRES 7 G 120 PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP GLU GLU
SEQRES 8 G 120 LEU ASN LYS LEU LEU SER GLY VAL THR ILE ALA GLN GLY
SEQRES 9 G 120 GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU PRO LYS
SEQRES 10 G 120 LYS THR GLU
SEQRES 1 H 122 PRO PRO LYS THR SER GLY LYS ALA ALA LYS LYS ALA GLY
SEQRES 2 H 122 LYS ALA GLN LYS ASN ILE THR LYS THR ASP LYS LYS LYS
SEQRES 3 H 122 LYS ARG LYS ARG LYS GLU SER TYR ALA ILE TYR ILE 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 ILE PHE GLU ARG ILE ALA ALA 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 SER LYS
HET MN I1006 1
HET MN I1007 1
HET MN I1008 1
HET MN I1010 1
HET MN I1011 1
HET MN I1012 1
HET MN I1013 1
HET MN J1001 1
HET MN J1003 1
HET MN J1004 1
HET MN J1005 1
HET MN J1009 1
HET MN J1014 1
HET CL A1017 1
HET CL D1016 1
HET MN E1002 1
HET CL E1018 1
HET CL H1015 1
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
FORMUL 11 MN 14(MN 2+)
FORMUL 24 CL 4(CL 1-)
FORMUL 29 HOH *88(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 SER C 15 GLY C 21 1 7
HELIX 10 10 PRO C 25 GLY C 36 1 12
HELIX 11 11 ALA C 44 ASN C 72 1 29
HELIX 12 12 ILE C 78 ASP C 89 1 12
HELIX 13 13 ASP C 89 LEU C 96 1 8
HELIX 14 14 GLN C 111 LEU C 115 5 5
HELIX 15 15 TYR D 34 HIS D 46 1 13
HELIX 16 16 SER D 52 ASN D 81 1 30
HELIX 17 17 THR D 87 LEU D 99 1 13
HELIX 18 18 PRO D 100 SER D 120 1 21
HELIX 19 19 GLY E 44 SER E 57 1 14
HELIX 20 20 ARG E 63 ASP E 77 1 15
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 ARG F 92 1 11
HELIX 27 27 SER G 15 GLY G 21 1 7
HELIX 28 28 PRO G 25 LYS G 35 1 11
HELIX 29 29 ALA G 44 ASP G 71 1 28
HELIX 30 30 ILE G 78 ASP G 89 1 12
HELIX 31 31 ASP G 89 LEU G 96 1 8
HELIX 32 32 GLN G 111 LEU G 115 5 5
HELIX 33 33 TYR H 34 HIS H 46 1 13
HELIX 34 34 SER H 52 ASN H 81 1 30
HELIX 35 35 THR H 87 LEU H 99 1 13
HELIX 36 36 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 LEU B 97 TYR B 98 0
SHEET 2 C 2 THR G 100 ILE G 101 1 O THR G 100 N TYR B 98
SHEET 1 D 2 ARG C 41 VAL C 42 0
SHEET 2 D 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 41
SHEET 1 E 2 ARG C 76 ILE C 77 0
SHEET 2 E 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 77
SHEET 1 F 2 THR C 100 ILE C 101 0
SHEET 2 F 2 LEU F 97 TYR F 98 1 O TYR F 98 N THR C 100
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 41 VAL G 42 0
SHEET 2 I 2 THR H 85 ILE H 86 1 O ILE H 86 N ARG G 41
SHEET 1 J 2 ARG G 76 ILE G 77 0
SHEET 2 J 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 77
LINK O6 DG I -34 MN MN I1013 1555 1555 2.26
LINK O6 DG J -34 MN MN J1009 1555 1555 2.36
LINK OD1 ASP E 77 MN MN E1002 1555 1555 2.10
LINK MN MN E1002 O HOH E1029 1555 1555 2.33
SITE 1 AC1 1 DG I 48
SITE 1 AC2 1 DG I 61
SITE 1 AC3 1 DG I 27
SITE 1 AC4 2 DG I 5 DG J -6
SITE 1 AC5 2 DG I -3 DG I -2
SITE 1 AC6 2 DG I -35 DG I -34
SITE 1 AC7 1 DG J 61
SITE 1 AC8 2 DT I 67 DG J 27
SITE 1 AC9 1 DG J -3
SITE 1 BC1 1 DG J 48
SITE 1 BC2 2 DG J -35 DG J -34
SITE 1 BC3 2 DG I -6 DG J 5
SITE 1 BC4 2 PRO A 121 LYS A 122
SITE 1 BC5 3 GLY C 45 THR D 87 SER D 88
SITE 1 BC6 3 VAL D 45 ASP E 77 HOH E1029
SITE 1 BC7 3 MET E 120 PRO E 121 LYS E 122
SITE 1 BC8 4 GLY G 45 ALA G 46 THR H 87 SER H 88
CRYST1 106.030 182.040 109.420 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 0.009431 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009139 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
