HEADER STRUCTURAL PROTEIN/DNA 31-MAY-05 2CV5
TITLE CRYSTAL STRUCTURE OF HUMAN NUCLEOSOME CORE PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (146-MER);
COMPND 3 CHAIN: I, J;
COMPND 4 SYNONYM: PALINDROMIC 146-BP HUMAN A-SATELLITE DNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: HISTONE H3.1;
COMPND 8 CHAIN: A, E;
COMPND 9 SYNONYM: HISTONE H3;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: HISTONE H4;
COMPND 13 CHAIN: B, F;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: HISTONE H2A.A;
COMPND 17 CHAIN: C, G;
COMPND 18 SYNONYM: HISTONE H2A;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 5;
COMPND 21 MOLECULE: HISTONE H2B K;
COMPND 22 CHAIN: D, H;
COMPND 23 SYNONYM: HISTONE H2B, HIRA-INTERACTING PROTEIN 1;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 21 ORGANISM_COMMON: HUMAN;
SOURCE 22 ORGANISM_TAXID: 9606;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PET22B;
SOURCE 27 MOL_ID: 5;
SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 29 ORGANISM_COMMON: HUMAN;
SOURCE 30 ORGANISM_TAXID: 9606;
SOURCE 31 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 32 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 33 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 34 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HUMAN NUCLEOSOME STRUCTURE, X-RAY CRYSTALLOGRAPHY,
KEYWDS 2 SUPERCOILED DNA PATH, METAL BINDING SITE, STRUCTURAL
KEYWDS 3 PROTEIN/DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.TSUNAKA,N.KAJIMURA,S.TATE,K.MORIKAWA
REVDAT 2 24-FEB-09 2CV5 1 VERSN
REVDAT 1 28-JUN-05 2CV5 0
JRNL AUTH Y.TSUNAKA,N.KAJIMURA,S.TATE,K.MORIKAWA
JRNL TITL ALTERATION OF THE NUCLEOSOMAL DNA PATH IN THE
JRNL TITL 2 CRYSTAL STRUCTURE OF A HUMAN NUCLEOSOME CORE
JRNL TITL 3 PARTICLE
JRNL REF NUCLEIC ACIDS RES. V. 33 3424 2005
JRNL REFN ISSN 0305-1048
JRNL PMID 15951514
JRNL DOI 10.1093/NAR/GKI663
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : NULL
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)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 61552
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 6241
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 : 6048
REMARK 3 NUCLEIC ACID ATOMS : 5980
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 430
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 2CV5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-05.
REMARK 100 THE RCSB ID CODE IS RCSB024655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61700
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MANGANESE (II) ION, CHLORIDE ION,
REMARK 280 H2O
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 49.78200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.71250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.71250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.78200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.18500
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 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 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 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 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 MET D -3
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 ALA D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
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 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 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 MET H -3
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 ALA H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 ARG H 26
REMARK 465 LYS H 27
REMARK 465 LYS H 122
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 DG I 87 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DA J 213 O4' - C1' - N9 ANGL. DEV. = 1.8 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 ASP A 77 1.93 -67.98
REMARK 500 ASP A 81 58.95 29.57
REMARK 500 ASN C 110 104.82 -167.04
REMARK 500 ARG D 28 -54.67 -137.42
REMARK 500 SER D 29 71.76 68.77
REMARK 500 HIS D 46 85.41 -150.86
REMARK 500 ARG E 134 39.71 -152.94
REMARK 500 ARG F 19 -96.71 55.32
REMARK 500 PRO G 26 95.30 -69.23
REMARK 500 ASN G 110 121.43 -176.04
REMARK 500 PRO G 117 -162.15 -69.47
REMARK 500 SER H 29 -87.48 -64.32
REMARK 500 ARG H 30 -86.14 46.59
REMARK 500 HIS H 46 75.19 -153.12
REMARK 500 SER H 120 -97.68 -58.58
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 D1008 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL D 45 O
REMARK 620 2 HOH D1026 O 93.0
REMARK 620 3 ASP E 77 OD1 89.8 85.6
REMARK 620 4 HOH E2048 O 174.5 88.3 95.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I1004 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH I1039 O
REMARK 620 2 DG I 68 O6 93.3
REMARK 620 3 HOH J1081 O 126.5 109.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J1001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH J1043 O
REMARK 620 2 HOH J1046 O 146.1
REMARK 620 3 DG J 185 N7 72.0 80.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J1002 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH J1071 O
REMARK 620 2 HOH J1041 O 71.9
REMARK 620 3 HOH J1044 O 90.3 159.8
REMARK 620 4 DG J 267 N7 98.6 91.7 81.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1003
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1004
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1005
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1006
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 1007
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN D 1008
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 1009
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 2001
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 2002
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 2003
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2004
DBREF 2CV5 A 0 135 UNP P68431 H31_HUMAN 0 135
DBREF 2CV5 B 0 102 UNP P62805 H4_HUMAN 0 102
DBREF 2CV5 C 0 129 UNP P28001 H2AA_HUMAN 0 129
DBREF 2CV5 D -3 122 UNP O60814 H2BK_HUMAN 0 125
DBREF 2CV5 E 0 135 UNP P68431 H31_HUMAN 0 135
DBREF 2CV5 F 0 102 UNP P62805 H4_HUMAN 0 102
DBREF 2CV5 G 0 129 UNP P28001 H2AA_HUMAN 0 129
DBREF 2CV5 H -3 122 UNP O60814 H2BK_HUMAN 0 125
DBREF 2CV5 I 1 146 PDB 2CV5 2CV5 1 146
DBREF 2CV5 J 147 292 PDB 2CV5 2CV5 147 292
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
SEQRES 1 A 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 A 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 A 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 A 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 A 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 A 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 A 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 A 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 A 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 A 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 A 136 ILE 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 HIS 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 130 MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA
SEQRES 2 C 130 LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 3 C 130 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 4 C 130 TYR SER GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 5 C 130 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 6 C 130 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 7 C 130 ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP
SEQRES 8 C 130 GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA
SEQRES 9 C 130 GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU
SEQRES 10 C 130 PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS
SEQRES 1 D 126 MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS
SEQRES 2 D 126 GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP
SEQRES 3 D 126 GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER
SEQRES 4 D 126 VAL TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP
SEQRES 5 D 126 THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER
SEQRES 6 D 126 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA
SEQRES 7 D 126 SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR
SEQRES 8 D 126 SER ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO
SEQRES 9 D 126 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS
SEQRES 10 D 126 ALA VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 136 MET ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY
SEQRES 2 E 136 GLY LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA
SEQRES 3 E 136 ARG LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO
SEQRES 4 E 136 HIS ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE
SEQRES 5 E 136 ARG ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS
SEQRES 6 E 136 LEU PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP
SEQRES 7 E 136 PHE LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET
SEQRES 8 E 136 ALA LEU GLN GLU ALA CYS GLU ALA TYR LEU VAL GLY LEU
SEQRES 9 E 136 PHE GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG
SEQRES 10 E 136 VAL THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG
SEQRES 11 E 136 ILE 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 HIS 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 130 MET SER GLY ARG GLY LYS GLN GLY GLY LYS ALA ARG ALA
SEQRES 2 G 130 LYS ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE
SEQRES 3 G 130 PRO VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN
SEQRES 4 G 130 TYR SER GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU
SEQRES 5 G 130 ALA ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU
SEQRES 6 G 130 LEU ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG
SEQRES 7 G 130 ILE ILE PRO ARG HIS LEU GLN LEU ALA ILE ARG ASN ASP
SEQRES 8 G 130 GLU GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA
SEQRES 9 G 130 GLN GLY GLY VAL LEU PRO ASN ILE GLN ALA VAL LEU LEU
SEQRES 10 G 130 PRO LYS LYS THR GLU SER HIS HIS LYS ALA LYS GLY LYS
SEQRES 1 H 126 MET PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS
SEQRES 2 H 126 GLY SER LYS LYS ALA VAL THR LYS ALA GLN LYS LYS ASP
SEQRES 3 H 126 GLY LYS LYS ARG LYS ARG SER ARG LYS GLU SER TYR SER
SEQRES 4 H 126 VAL TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP
SEQRES 5 H 126 THR GLY ILE SER SER LYS ALA MET GLY ILE MET ASN SER
SEQRES 6 H 126 PHE VAL ASN ASP ILE PHE GLU ARG ILE ALA GLY GLU ALA
SEQRES 7 H 126 SER ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR
SEQRES 8 H 126 SER ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO
SEQRES 9 H 126 GLY GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS
SEQRES 10 H 126 ALA VAL THR LYS TYR THR SER ALA LYS
HET MN J1001 1
HET MN J1002 1
HET MN J1003 1
HET MN I1004 1
HET MN I1005 1
HET MN J1006 1
HET MN I1007 1
HET MN D1008 1
HET MN J1009 1
HET CL C2001 1
HET CL G2002 1
HET CL E2003 1
HET CL A2004 1
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
FORMUL 11 MN 9(MN 2+)
FORMUL 20 CL 4(CL 1-)
FORMUL 24 HOH *430(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 ASN C 89 1 11
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 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 LYS E 56 1 13
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 GLN F 93 1 12
HELIX 27 27 THR G 16 ALA G 21 1 6
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 ASP G 90 1 12
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 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 ALA H 121 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 THR B 96 TYR B 98 0
SHEET 2 C 2 VAL G 100 ILE G 102 1 O THR G 101 N TYR B 98
SHEET 1 D 2 ARG C 42 VAL C 43 0
SHEET 2 D 2 THR D 85 ILE D 86 1 O ILE D 86 N ARG C 42
SHEET 1 E 2 ARG C 77 ILE C 78 0
SHEET 2 E 2 GLY D 50 ILE D 51 1 O GLY D 50 N ILE C 78
SHEET 1 F 2 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 85 ILE H 86 1 O ILE H 86 N ARG G 42
SHEET 1 J 2 ARG G 77 ILE G 78 0
SHEET 2 J 2 GLY H 50 ILE H 51 1 O GLY H 50 N ILE G 78
LINK MN MN D1008 O VAL D 45 1555 1555 2.39
LINK MN MN D1008 O HOH D1026 1555 1555 2.27
LINK MN MN I1004 O HOH I1039 1555 1555 2.62
LINK MN MN I1004 O6 DG I 68 1555 1555 2.38
LINK MN MN I1005 N7 DG I 121 1555 1555 2.53
LINK MN MN I1007 O HOH I1042 1555 1555 2.67
LINK MN MN J1001 O HOH J1043 1555 1555 2.56
LINK MN MN J1001 O HOH J1046 1555 1555 2.45
LINK MN MN J1001 N7 DG J 185 1555 1555 2.46
LINK MN MN J1002 O HOH J1071 1555 1555 2.39
LINK MN MN J1002 O HOH J1041 1555 1555 2.35
LINK MN MN J1002 O HOH J1044 1555 1555 2.22
LINK MN MN J1002 N7 DG J 267 1555 1555 2.25
LINK MN MN J1003 N7 DG J 217 1555 1555 2.60
LINK MN MN J1006 N7 DG J 280 1555 1555 2.74
LINK MN MN J1009 O HOH J1088 1555 1555 2.16
LINK MN MN D1008 OD1 ASP E 77 1555 3555 2.09
LINK MN MN D1008 O HOH E2048 1555 3555 2.29
LINK MN MN I1004 O HOH J1081 1555 4555 2.41
CISPEP 1 LYS E 37 PRO E 38 0 -0.41
SITE 1 AC1 4 DG J 185 DG J 186 HOH J1043 HOH J1046
SITE 1 AC2 4 DG J 267 HOH J1041 HOH J1044 HOH J1071
SITE 1 AC3 2 DG J 217 HOH J1042
SITE 1 AC4 3 DG I 68 HOH I1039 HOH J1081
SITE 1 AC5 1 DG I 121
SITE 1 AC6 1 DG J 280
SITE 1 AC7 2 DG I 134 HOH I1042
SITE 1 AC8 4 VAL D 45 HOH D1026 ASP E 77 HOH E2048
SITE 1 AC9 3 HOH I1095 HOH J1087 HOH J1088
SITE 1 BC1 4 GLY C 46 ALA C 47 THR D 87 SER D 88
SITE 1 BC2 6 GLY G 44 ALA G 45 GLY G 46 ALA G 47
SITE 2 BC2 6 THR H 87 SER H 88
SITE 1 BC3 2 PRO E 121 LYS E 122
SITE 1 BC4 2 PRO A 121 LYS A 122
CRYST1 99.564 108.370 169.425 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 0.010044 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009228 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005902 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
