HEADER STRUCTURAL PROTEIN/DNA 07-APR-10 3MGS
TITLE BINDING OF CESIUM IONS TO THE NUCLEOSOME CORE PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.2;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A;
COMPND 11 CHAIN: C, G;
COMPND 12 FRAGMENT: UNP RESIDUES 2-120;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: HISTONE H2B 1.1;
COMPND 16 CHAIN: D, H;
COMPND 17 SYNONYM: H2B1.1;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 5;
COMPND 20 MOLECULE: DNA (147-MER);
COMPND 21 CHAIN: I;
COMPND 22 ENGINEERED: YES;
COMPND 23 MOL_ID: 6;
COMPND 24 MOLECULE: DNA (147-MER);
COMPND 25 CHAIN: J;
COMPND 26 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: HISTONE 3 OR H3;
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: PET3D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 13 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 14 ORGANISM_TAXID: 8355;
SOURCE 15 GENE: HISTONE 4 OR H4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 23 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 24 ORGANISM_TAXID: 8355;
SOURCE 25 GENE: HISTONE 2A OR H2A, LOC494591;
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: PET3A;
SOURCE 31 MOL_ID: 4;
SOURCE 32 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 33 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 34 ORGANISM_TAXID: 8355;
SOURCE 35 GENE: HISTONE 2B OR 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: PET3A;
SOURCE 41 MOL_ID: 5;
SOURCE 42 SYNTHETIC: YES;
SOURCE 43 OTHER_DETAILS: SYNTHETIC PALINDROMIC DNA EXPRESSED IN PUC18 PLASMID
SOURCE 44 USING E.COLI HB101 CELLS.;
SOURCE 45 MOL_ID: 6;
SOURCE 46 SYNTHETIC: YES;
SOURCE 47 OTHER_DETAILS: SYNTHETIC PALINDROMIC DNA EXPRESSED IN PUC18 PLASMID
SOURCE 48 USING E.COLI HB101 CELLS.
KEYWDS PROTEIN-DNA COMPLEX, STRUCTURAL PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MOHIDEEN,R.MUHAMMAD,C.A.DAVEY
REVDAT 3 01-NOV-23 3MGS 1 REMARK DBREF LINK
REVDAT 2 08-NOV-17 3MGS 1 REMARK
REVDAT 1 16-JUN-10 3MGS 0
JRNL AUTH K.MOHIDEEN,R.MUHAMMAD,C.A.DAVEY
JRNL TITL PERTURBATIONS IN NUCLEOSOME STRUCTURE FROM HEAVY METAL
JRNL TITL 2 ASSOCIATION.
JRNL REF NUCLEIC ACIDS RES. 2010
JRNL REFN ESSN 1362-4962
JRNL PMID 20494975
JRNL DOI 10.1093/NAR/GKQ420
REMARK 2
REMARK 2 RESOLUTION. 3.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC RIGID BODY
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 94.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 36839
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.100
REMARK 3 FREE R VALUE TEST SET COUNT : 774
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2606
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6156
REMARK 3 NUCLEIC ACID ATOMS : 6021
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 75.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.40000
REMARK 3 B22 (A**2) : -6.24000
REMARK 3 B33 (A**2) : 4.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.434
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.326
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.708
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12991 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18797 ; 1.460 ; 2.545
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 764 ; 5.037 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 274 ;32.962 ;21.131
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1209 ;16.600 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 89 ;20.451 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2134 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7656 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5153 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8187 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 373 ; 0.153 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 23 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.137 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3899 ; 0.654 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6170 ; 1.167 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12064 ; 1.058 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12627 ; 1.948 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3MGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058526.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.93
REMARK 200 MONOCHROMATOR : BARTELS MONOCHROMATOR
REMARK 200 OPTICS : VERTICALLY COLLIMATING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36839
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150
REMARK 200 RESOLUTION RANGE LOW (A) : 94.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC RIGID BODY
REMARK 200 STARTING MODEL: 1KX5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 85MM MNCL2, 60MM KCL, 40MM K
REMARK 280 -CACODYLATE , PH 6.0, VAPOR DIFFUSION, TEMPERATURE 291K
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 53.25500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.30450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.83400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.30450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.25500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.83400
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: 59200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 72610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -364.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 ALA B 15
REMARK 465 LYS B 16
REMARK 465 ARG B 17
REMARK 465 HIS B 18
REMARK 465 ARG B 19
REMARK 465 LYS B 20
REMARK 465 VAL B 21
REMARK 465 LEU B 22
REMARK 465 ARG B 23
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 THR C 10
REMARK 465 ARG C 11
REMARK 465 ALA C 12
REMARK 465 LYS C 13
REMARK 465 ALA C 14
REMARK 465 LYS C 119
REMARK 465 PRO D -2
REMARK 465 GLU D -1
REMARK 465 PRO D 0
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 THR D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 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 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 THR G 10
REMARK 465 ARG G 11
REMARK 465 ALA G 12
REMARK 465 LYS G 119
REMARK 465 PRO H -2
REMARK 465 GLU H -1
REMARK 465 PRO H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 THR H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CS CS J 74 MN MN J 3136 1.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DA I 4 O3' DA I 4 C3' -0.040
REMARK 500 DG I 25 O3' DG I 25 C3' -0.049
REMARK 500 DA J 29 O3' DA J 29 C3' -0.041
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DA I -73 O4' - C1' - N9 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DC I -71 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500 DA I -70 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DC I -64 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DA I -63 O4' - C1' - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DC I -62 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DC I -61 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DC I -52 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT I -51 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DA I -50 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG I -41 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT I -40 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA I -39 O4' - C1' - N9 ANGL. DEV. = 4.9 DEGREES
REMARK 500 DT I -38 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 DG I -34 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DA I -33 O4' - C1' - N9 ANGL. DEV. = -4.6 DEGREES
REMARK 500 DC I -30 O4' - C1' - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 DC I -25 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I -21 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DA I -19 O4' - C1' - N9 ANGL. DEV. = 5.5 DEGREES
REMARK 500 DA I -17 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DT I -10 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA I -7 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC I -5 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DT I -4 C4 - C5 - C7 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DG I -2 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DG I -2 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DC I 3 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I 6 O5' - C5' - C4' ANGL. DEV. = -5.5 DEGREES
REMARK 500 DG I 8 O4' - C1' - N9 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DA I 9 O4' - C1' - N9 ANGL. DEV. = -5.7 DEGREES
REMARK 500 DC I 11 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DC I 16 C3' - C2' - C1' ANGL. DEV. = -5.4 DEGREES
REMARK 500 DT I 20 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG I 21 O4' - C1' - N9 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DA I 22 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 DT I 23 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DG I 25 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 DC I 35 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA I 37 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA I 40 O4' - C1' - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DA I 42 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DC I 43 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DT I 44 O4' - C1' - N1 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DT I 44 C3' - O3' - P ANGL. DEV. = 7.5 DEGREES
REMARK 500 DG I 52 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT I 53 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DA I 54 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG I 62 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG I 64 O4' - C1' - N9 ANGL. DEV. = 4.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 129 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN B 25 -89.58 81.22
REMARK 500 ILE B 29 96.49 -68.94
REMARK 500 ASN C 110 107.43 -173.07
REMARK 500 ARG D 26 35.84 39.71
REMARK 500 ARG D 27 97.91 18.39
REMARK 500 ARG E 134 -76.05 -104.47
REMARK 500 HIS F 18 -107.68 -85.44
REMARK 500 ARG F 19 87.94 44.35
REMARK 500 ALA G 14 -82.07 -64.13
REMARK 500 LYS G 74 37.73 71.77
REMARK 500 ASN G 110 112.85 -162.65
REMARK 500 PRO G 117 138.10 -34.95
REMARK 500 ARG H 26 -90.31 -70.00
REMARK 500 ARG H 27 15.29 -67.59
REMARK 500 THR H 29 96.56 -13.56
REMARK 500 HIS H 46 71.48 -152.92
REMARK 500 LYS H 117 -37.57 -37.07
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 CS D 123 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG D 96 O
REMARK 620 2 LEU D 97 O 66.5
REMARK 620 3 LEU D 99 O 71.6 94.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS H 123 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG H 96 O
REMARK 620 2 LEU H 99 O 71.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 74 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT I -66 O2
REMARK 620 2 DC I -65 O4' 65.2
REMARK 620 3 DT J 67 O2 82.3 127.7
REMARK 620 4 DA J 68 O4' 137.2 154.7 60.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 80 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT I -60 O2
REMARK 620 2 DG I -59 O4' 111.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN I3143 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG I -35 N7
REMARK 620 2 DG I -34 O6 81.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 76 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT I -26 O2
REMARK 620 2 DC I -25 O4' 83.6
REMARK 620 3 DC I -25 O2 84.3 67.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 79 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC I 11 O2
REMARK 620 2 DT J -10 O2 91.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 78 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC I 16 O2
REMARK 620 2 DC I 16 O4' 63.1
REMARK 620 3 DG J -15 N2 85.5 121.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS I 77 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT I 67 O2
REMARK 620 2 DA I 68 O4' 59.8
REMARK 620 3 DT J -66 O2 110.1 140.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS J 75 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT J -60 O2
REMARK 620 2 DG J -59 O4' 91.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN J3139 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG J -35 N7
REMARK 620 2 DG J -34 O6 89.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CS J 74 CS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DT J -12 O2
REMARK 620 2 DT J -12 O4' 71.5
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 CS I 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 75
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS H 123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 77
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 79
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS C 120
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS J 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS I 80
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS D 123
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CS J 75
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3131
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 3132
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3133
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3134
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3135
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3136
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3137
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3138
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3139
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3140
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3141
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3142
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 3143
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN J 3144
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 3145
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 3146
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 3147
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 3148
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KX5 RELATED DB: PDB
REMARK 900 RELATED ID: 3MGP RELATED DB: PDB
REMARK 900 RELATED ID: 3MGQ RELATED DB: PDB
REMARK 900 RELATED ID: 3MGR RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICTS REPRESENT UNINTENTIONAL MUTATION OR VARIATION IN
REMARK 999 GENOMIC SOURCES
DBREF 3MGS A 1 135 UNP P84233 H32_XENLA 2 136
DBREF 3MGS B 1 102 UNP P62799 H4_XENLA 2 103
DBREF 3MGS C 1 119 UNP Q6AZJ8 Q6AZJ8_XENLA 2 120
DBREF 3MGS D -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 3MGS E 1 135 UNP P84233 H32_XENLA 2 136
DBREF 3MGS F 1 102 UNP P62799 H4_XENLA 2 103
DBREF 3MGS G 1 119 UNP Q6AZJ8 Q6AZJ8_XENLA 2 120
DBREF 3MGS H -2 122 UNP P02281 H2B11_XENLA 2 126
DBREF 3MGS I -73 73 PDB 3MGS 3MGS -73 73
DBREF 3MGS J -73 73 PDB 3MGS 3MGS -73 73
SEQADV 3MGS ALA A 102 UNP P84233 GLY 103 SEE REMARK 999
SEQADV 3MGS THR D 29 UNP P02281 SER 33 SEE REMARK 999
SEQADV 3MGS ALA E 102 UNP P84233 GLY 103 SEE REMARK 999
SEQADV 3MGS THR H 29 UNP P02281 SER 33 SEE REMARK 999
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 119 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 C 119 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 C 119 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 C 119 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 C 119 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 C 119 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 C 119 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 C 119 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 C 119 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 C 119 LYS LYS
SEQRES 1 D 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 D 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 D 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 D 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 D 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 D 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 D 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 D 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 D 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 D 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 119 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 G 119 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 G 119 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 G 119 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 G 119 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 G 119 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 G 119 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 G 119 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 G 119 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 G 119 LYS LYS
SEQRES 1 H 125 PRO GLU PRO ALA LYS SER ALA PRO ALA PRO LYS LYS GLY
SEQRES 2 H 125 SER LYS LYS ALA VAL THR LYS THR GLN LYS LYS ASP GLY
SEQRES 3 H 125 LYS LYS ARG ARG LYS THR ARG LYS GLU SER TYR ALA ILE
SEQRES 4 H 125 TYR VAL TYR LYS VAL LEU LYS GLN VAL HIS PRO ASP THR
SEQRES 5 H 125 GLY ILE SER SER LYS ALA MET SER ILE MET ASN SER PHE
SEQRES 6 H 125 VAL ASN ASP VAL PHE GLU ARG ILE ALA GLY GLU ALA SER
SEQRES 7 H 125 ARG LEU ALA HIS TYR ASN LYS ARG SER THR ILE THR SER
SEQRES 8 H 125 ARG GLU ILE GLN THR ALA VAL ARG LEU LEU LEU PRO GLY
SEQRES 9 H 125 GLU LEU ALA LYS HIS ALA VAL SER GLU GLY THR LYS ALA
SEQRES 10 H 125 VAL THR LYS TYR THR SER ALA LYS
SEQRES 1 I 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
HET CL A3147 1
HET CS C 120 1
HET CL C3146 1
HET CS D 123 1
HET MN E3132 1
HET CL E3148 1
HET CL G3145 1
HET CS H 123 1
HET CS I 74 1
HET CS I 75 1
HET CS I 76 1
HET CS I 77 1
HET CS I 78 1
HET CS I 79 1
HET CS I 80 1
HET MN I3137 1
HET MN I3138 1
HET MN I3140 1
HET MN I3141 1
HET MN I3142 1
HET MN I3143 1
HET CS J 74 1
HET CS J 75 1
HET MN J3131 1
HET MN J3133 1
HET MN J3134 1
HET MN J3135 1
HET MN J3136 1
HET MN J3139 1
HET MN J3144 1
HETNAM CL CHLORIDE ION
HETNAM CS CESIUM ION
HETNAM MN MANGANESE (II) ION
FORMUL 11 CL 4(CL 1-)
FORMUL 12 CS 12(CS 1+)
FORMUL 15 MN 14(MN 2+)
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 ASP B 24 ILE B 29 5 6
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 ALA C 21 1 6
HELIX 10 10 PRO C 26 GLY C 37 1 12
HELIX 11 11 GLY C 46 ASN C 73 1 28
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 ALA D 121 1 22
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 GLN F 93 1 12
HELIX 27 27 THR G 16 GLY G 22 1 7
HELIX 28 28 PRO G 26 LYS G 36 1 11
HELIX 29 29 ALA G 45 ASN G 73 1 29
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 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 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 O GLY C 37 CS CS C 120 1555 1555 3.44
LINK O ARG D 96 CS CS D 123 1555 1555 3.31
LINK O LEU D 97 CS CS D 123 1555 1555 3.48
LINK O LEU D 99 CS CS D 123 1555 1555 3.14
LINK OD1 ASP E 77 MN MN E3132 1555 1555 2.28
LINK O ARG H 96 CS CS H 123 1555 1555 3.18
LINK O LEU H 99 CS CS H 123 1555 1555 3.25
LINK O2 DT I -66 CS CS I 74 1555 1555 2.80
LINK O4' DC I -65 CS CS I 74 1555 1555 3.17
LINK O2 DT I -60 CS CS I 80 1555 1555 2.86
LINK O4' DG I -59 CS CS I 80 1555 1555 2.92
LINK N7 DG I -35 MN MN I3143 1555 1555 2.27
LINK O6 DG I -34 MN MN I3143 1555 1555 2.78
LINK O2 DT I -26 CS CS I 76 1555 1555 2.80
LINK O4' DC I -25 CS CS I 76 1555 1555 2.81
LINK O2 DC I -25 CS CS I 76 1555 1555 2.86
LINK N7 DG I -3 MN MN I3142 1555 1555 2.33
LINK O2 DC I 11 CS CS I 79 1555 1555 2.83
LINK O4' DC I 15 CS CS I 75 1555 1555 3.20
LINK O2 DC I 16 CS CS I 78 1555 1555 2.94
LINK O4' DC I 16 CS CS I 78 1555 1555 3.45
LINK N7 DG I 27 MN MN I3140 1555 1555 2.60
LINK N7 DG I 48 MN MN I3137 1555 1555 2.35
LINK N7 DG I 61 MN MN I3138 1555 1555 2.43
LINK O2 DT I 67 CS CS I 77 1555 1555 2.66
LINK O4' DA I 68 CS CS I 77 1555 1555 3.39
LINK CS CS I 74 O2 DT J 67 1555 1555 3.09
LINK CS CS I 74 O4' DA J 68 1555 1555 2.92
LINK CS CS I 77 O2 DT J -66 1555 1555 2.41
LINK CS CS I 78 N2 DG J -15 1555 1555 2.70
LINK CS CS I 79 O2 DT J -10 1555 1555 2.50
LINK O2 DT J -60 CS CS J 75 1555 1555 3.09
LINK O4' DG J -59 CS CS J 75 1555 1555 3.10
LINK N7 DG J -35 MN MN J3139 1555 1555 2.46
LINK O6 DG J -34 MN MN J3139 1555 1555 2.67
LINK O2 DT J -12 CS CS J 74 1555 1555 2.56
LINK O4' DT J -12 CS CS J 74 1555 1555 3.31
LINK N7 DG J -3 MN MN J3134 1555 1555 2.30
LINK O6 DG J 5 MN MN J3144 1555 1555 2.60
LINK N7 DG J 27 MN MN J3133 1555 1555 2.53
LINK N7 DG J 48 MN MN J3135 1555 1555 2.18
LINK N7 DG J 61 MN MN J3131 1555 1555 2.53
SITE 1 AC1 4 DT I -66 DC I -65 DT J 67 DA J 68
SITE 1 AC2 5 DG I 14 DC I 15 DA J -13 CS J 74
SITE 2 AC2 5 MN J3136
SITE 1 AC3 3 ARG H 96 LEU H 97 LEU H 99
SITE 1 AC4 3 DC I -25 DT I -26 DA J 26
SITE 1 AC5 4 DT I 67 DA I 68 DC J -65 DT J -66
SITE 1 AC6 3 DC I 15 DC I 16 DG J -15
SITE 1 AC7 2 DC I 11 DT J -10
SITE 1 AC8 2 GLY C 37 TYR C 39
SITE 1 AC9 5 DT I 13 CS I 75 DA J -13 DT J -12
SITE 2 AC9 5 MN J3136
SITE 1 BC1 2 DG I -59 DT I -60
SITE 1 BC2 3 ARG D 96 LEU D 97 LEU D 99
SITE 1 BC3 2 DG J -59 DT J -60
SITE 1 BC4 1 DG J 61
SITE 1 BC5 2 VAL D 45 ASP E 77
SITE 1 BC6 2 DT I 67 DG J 27
SITE 1 BC7 1 DG J -3
SITE 1 BC8 1 DG J 48
SITE 1 BC9 2 CS I 75 CS J 74
SITE 1 CC1 1 DG I 48
SITE 1 CC2 1 DG I 61
SITE 1 CC3 2 DG J -35 DG J -34
SITE 1 CC4 1 DG I 27
SITE 1 CC5 1 DG I 5
SITE 1 CC6 2 DG I -3 DG I -2
SITE 1 CC7 2 DG I -35 DG I -34
SITE 1 CC8 2 DA J 4 DG J 5
SITE 1 CC9 5 GLY G 44 ALA G 45 GLY G 46 ALA G 47
SITE 2 CC9 5 SER H 88
SITE 1 DC1 4 GLY C 44 GLY C 46 THR D 87 SER D 88
SITE 1 DC2 3 MET A 120 PRO A 121 LYS A 122
SITE 1 DC3 2 PRO E 121 LYS E 122
CRYST1 106.510 109.668 182.609 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 0.009389 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009118 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005476 0.00000
(ATOM LINES ARE NOT SHOWN.)
END