HEADER TRANSFERASE 14-JAN-09 3FUX
TITLE T. THERMOPHILUS 16S RRNA A1518 AND A1519 METHYLTRANSFERASE (KSGA) IN
TITLE 2 COMPLEX WITH 5'-METHYLTHIOADENOSINE IN SPACE GROUP P212121
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIMETHYLADENOSINE TRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: S-ADENOSYLMETHIONINE-6-N', N'-ADENOSYL(RRNA)
COMPND 5 DIMETHYLTRANSFERASE, 16S RRNA DIMETHYLASE, HIGH LEVEL KASUGAMYCIN
COMPND 6 RESISTANCE PROTEIN KSGA, KASUGAMYCIN DIMETHYLTRANSFERASE;
COMPND 7 EC: 2.1.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: KSGA, TTHA0083;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS METHYLTRANSFERASE, DIMETHYLTRANSFERASE, DUAL-SPECIFIC
KEYWDS 2 METHYLTRANSFERASE, 16S RRNA METHYLTRANSFERASE, TRANSLATION,
KEYWDS 3 ANTIBIOTIC RESISTANCE, RNA-BINDING, RRNA PROCESSING, S-ADENOSYL-L-
KEYWDS 4 METHIONINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DEMIRCI,R.BELARDINELLI,E.SERI,S.T.GREGORY,C.GUALERZI,A.E.DAHLBERG,
AUTHOR 2 G.JOGL
REVDAT 5 21-FEB-24 3FUX 1 REMARK
REVDAT 4 01-NOV-17 3FUX 1 REMARK
REVDAT 3 13-JUL-11 3FUX 1 VERSN
REVDAT 2 28-APR-09 3FUX 1 JRNL
REVDAT 1 31-MAR-09 3FUX 0
JRNL AUTH H.DEMIRCI,R.BELARDINELLI,E.SERI,S.T.GREGORY,C.GUALERZI,
JRNL AUTH 2 A.E.DAHLBERG,G.JOGL
JRNL TITL STRUCTURAL REARRANGEMENTS IN THE ACTIVE SITE OF THE THERMUS
JRNL TITL 2 THERMOPHILUS 16S RRNA METHYLTRANSFERASE KSGA IN A BINARY
JRNL TITL 3 COMPLEX WITH 5'-METHYLTHIOADENOSINE.
JRNL REF J.MOL.BIOL. V. 388 271 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19285505
JRNL DOI 10.1016/J.JMB.2009.02.066
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 91277
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4529
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.2730
REMARK 3 BIN FREE R VALUE SET COUNT : 339
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6203
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 708
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : 0.17000
REMARK 3 B33 (A**2) : -0.62000
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): 0.121
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.991
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6456 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8789 ; 1.494 ; 2.011
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 798 ; 5.757 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 273 ;26.203 ;21.062
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1055 ;14.178 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;16.830 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1005 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4908 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3081 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4413 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 499 ; 0.129 ; 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): 57 ; 0.207 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 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): 4093 ; 0.792 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6430 ; 1.140 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2617 ; 2.136 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2359 ; 3.459 ; 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 : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 80
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9404 4.7686 -31.5101
REMARK 3 T TENSOR
REMARK 3 T11: -0.0457 T22: -0.0303
REMARK 3 T33: -0.1162 T12: -0.0663
REMARK 3 T13: -0.0124 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.9584 L22: 2.1778
REMARK 3 L33: 1.7272 L12: 1.3790
REMARK 3 L13: -0.0762 L23: -0.2223
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0652 S13: 0.1048
REMARK 3 S21: -0.1156 S22: -0.0304 S23: 0.0928
REMARK 3 S31: 0.1630 S32: -0.2650 S33: 0.0227
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 81 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7335 8.1976 -24.9302
REMARK 3 T TENSOR
REMARK 3 T11: -0.0608 T22: -0.0724
REMARK 3 T33: -0.0787 T12: -0.0567
REMARK 3 T13: 0.0080 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 1.2862 L22: 1.3770
REMARK 3 L33: 1.5718 L12: 0.6843
REMARK 3 L13: 0.7957 L23: 0.4054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0400 S12: -0.0185 S13: 0.0235
REMARK 3 S21: 0.0305 S22: -0.0802 S23: -0.1216
REMARK 3 S31: 0.0917 S32: -0.0353 S33: 0.0401
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 201 A 268
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9596 14.6560 -6.8223
REMARK 3 T TENSOR
REMARK 3 T11: -0.0927 T22: -0.0352
REMARK 3 T33: -0.0078 T12: -0.0820
REMARK 3 T13: -0.0383 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 2.0296 L22: 0.9872
REMARK 3 L33: 2.9690 L12: -0.2322
REMARK 3 L13: -0.1758 L23: 0.8857
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: -0.0868 S13: 0.0383
REMARK 3 S21: 0.0216 S22: 0.0054 S23: -0.2146
REMARK 3 S31: -0.1269 S32: 0.3077 S33: -0.1049
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 80
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0733 33.6837 -30.5901
REMARK 3 T TENSOR
REMARK 3 T11: -0.0536 T22: -0.0282
REMARK 3 T33: -0.0768 T12: 0.0479
REMARK 3 T13: 0.0258 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 1.1063 L22: 1.8150
REMARK 3 L33: 4.0476 L12: -0.6129
REMARK 3 L13: -1.1738 L23: 0.2474
REMARK 3 S TENSOR
REMARK 3 S11: 0.1492 S12: 0.0300 S13: -0.0008
REMARK 3 S21: 0.1140 S22: -0.0963 S23: 0.1730
REMARK 3 S31: -0.3250 S32: -0.5571 S33: -0.0529
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 81 B 200
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0722 29.9737 -37.4822
REMARK 3 T TENSOR
REMARK 3 T11: -0.0456 T22: -0.0939
REMARK 3 T33: -0.1066 T12: 0.0365
REMARK 3 T13: -0.0035 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 1.7044 L22: 1.0145
REMARK 3 L33: 2.7406 L12: -0.4842
REMARK 3 L13: -1.1813 L23: 0.5069
REMARK 3 S TENSOR
REMARK 3 S11: 0.1645 S12: 0.0922 S13: 0.0211
REMARK 3 S21: -0.0517 S22: -0.1005 S23: -0.0148
REMARK 3 S31: -0.1130 S32: 0.0033 S33: -0.0640
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 201 B 268
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5368 23.8614 -56.0337
REMARK 3 T TENSOR
REMARK 3 T11: -0.0133 T22: 0.0395
REMARK 3 T33: -0.1148 T12: 0.2009
REMARK 3 T13: 0.0572 T23: 0.0449
REMARK 3 L TENSOR
REMARK 3 L11: 2.7156 L22: 1.6074
REMARK 3 L33: 4.3112 L12: -0.0756
REMARK 3 L13: -0.9624 L23: -0.1750
REMARK 3 S TENSOR
REMARK 3 S11: 0.1956 S12: 0.2100 S13: 0.0247
REMARK 3 S21: -0.3313 S22: -0.3097 S23: -0.2412
REMARK 3 S31: 0.2874 S32: 0.3950 S33: 0.1142
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 80
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2129 45.9023 0.5584
REMARK 3 T TENSOR
REMARK 3 T11: -0.0803 T22: -0.0650
REMARK 3 T33: -0.0748 T12: 0.0243
REMARK 3 T13: 0.0275 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 2.6910 L22: 2.4377
REMARK 3 L33: 0.9802 L12: -1.8915
REMARK 3 L13: -0.0540 L23: -0.0835
REMARK 3 S TENSOR
REMARK 3 S11: -0.1044 S12: -0.1767 S13: 0.0270
REMARK 3 S21: 0.0541 S22: 0.0776 S23: -0.1445
REMARK 3 S31: -0.0035 S32: 0.0933 S33: 0.0268
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 81 C 200
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3627 48.4811 -5.4711
REMARK 3 T TENSOR
REMARK 3 T11: -0.0593 T22: -0.0977
REMARK 3 T33: -0.0616 T12: 0.0203
REMARK 3 T13: 0.0259 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.9211 L22: 1.4087
REMARK 3 L33: 0.9792 L12: -0.7250
REMARK 3 L13: 0.4139 L23: -0.4615
REMARK 3 S TENSOR
REMARK 3 S11: -0.0551 S12: 0.0130 S13: -0.0977
REMARK 3 S21: -0.1106 S22: 0.0929 S23: 0.1614
REMARK 3 S31: 0.0426 S32: -0.0795 S33: -0.0378
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 201 C 268
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0394 52.4687 -22.0642
REMARK 3 T TENSOR
REMARK 3 T11: -0.1012 T22: -0.0467
REMARK 3 T33: -0.0673 T12: 0.0039
REMARK 3 T13: -0.0327 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 4.6916 L22: 1.6093
REMARK 3 L33: 4.9201 L12: -0.4203
REMARK 3 L13: 2.6933 L23: -1.7911
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.3280 S13: -0.2445
REMARK 3 S21: -0.2211 S22: -0.0001 S23: 0.2418
REMARK 3 S31: 0.1039 S32: 0.0557 S33: 0.0053
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3FUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051072.
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 : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : BENT SINGLE SI (111) CRYSTAL
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING AND DEFLECTION) WITH
REMARK 200 VERTICAL FOCUSING MIRROR
REMARK 200 OPTICS : BENT SINGLE SI (111) CRYSTAL
REMARK 200 MONOCHROMATOR (HORIZONTAL
REMARK 200 FOCUSING AND DEFLECTION) WITH
REMARK 200 VERTICAL FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 130 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91701
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLECULAR REPLACEMENT (PHASER)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% V/V POLYETHYLENE GLYCOL 300, 100
REMARK 280 MM TRIS-HCL (PH 8.5), 5% W/V POLYETHYLENE GLYCOL 8000, 10% V/V
REMARK 280 ANHYDROUS GLYCEROL, MICROBATCH TECHNIQUE UNDER OIL, TEMPERATURE
REMARK 280 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 28.02800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.21800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.95400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.21800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.02800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.95400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 LEU A 4
REMARK 465 GLY A 269
REMARK 465 ALA A 270
REMARK 465 VAL A 271
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
REMARK 465 LEU B 4
REMARK 465 GLY B 269
REMARK 465 ALA B 270
REMARK 465 VAL B 271
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 LYS C 3
REMARK 465 GLY C 269
REMARK 465 ALA C 270
REMARK 465 VAL C 271
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 GLN C 8 CD OE1 NE2
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 O HOH C 353 O HOH C 520 2.16
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 ARG A 242 CZ ARG A 242 NH1 0.141
REMARK 500 GLU B 15 CG GLU B 15 CD 0.094
REMARK 500 HIS B 17 CG HIS B 17 ND1 0.140
REMARK 500 GLU B 239 CD GLU B 239 OE1 0.099
REMARK 500 GLU B 239 CD GLU B 239 OE2 0.114
REMARK 500 ARG B 242 CZ ARG B 242 NH1 0.129
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 ARG A 138 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 138 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH2 ANGL. DEV. = -4.7 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 SER B 6 162.21 -49.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTA A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTA B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTA C 272
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FUT RELATED DB: PDB
REMARK 900 APO-FORM OF T. THERMOPHILUS 16S RRNA A1518 AND A1519
REMARK 900 METHYLTRANSFERASE (KSGA) IN SPACE GROUP P21212
REMARK 900 RELATED ID: 3FUU RELATED DB: PDB
REMARK 900 T. THERMOPHILUS 16S RRNA A1518 AND A1519 METHYLTRANSFERASE (KSGA)
REMARK 900 IN COMPLEX WITH ADENOSINE IN SPACE GROUP P212121
REMARK 900 RELATED ID: 3FUV RELATED DB: PDB
REMARK 900 APO-FORM OF T. THERMOPHILUS 16S RRNA A1518 AND A1519
REMARK 900 METHYLTRANSFERASE (KSGA) IN SPACE GROUP P43212
REMARK 900 RELATED ID: 3FUW RELATED DB: PDB
REMARK 900 T. THERMOPHILUS 16S RRNA A1518 AND A1519 METHYLTRANSFERASE (KSGA)
REMARK 900 IN COMPLEX WITH 5'-METHYLTHIOADENOSINE IN SPACE GROUP P212121
DBREF 3FUX A 1 271 UNP Q5SM60 KSGA_THET8 1 271
DBREF 3FUX B 1 271 UNP Q5SM60 KSGA_THET8 1 271
DBREF 3FUX C 1 271 UNP Q5SM60 KSGA_THET8 1 271
SEQRES 1 A 271 MET SER LYS LEU ALA SER PRO GLN SER VAL ARG ALA LEU
SEQRES 2 A 271 LEU GLU ARG HIS GLY LEU PHE ALA ASP LYS ARG PHE GLY
SEQRES 3 A 271 GLN ASN PHE LEU VAL SER GLU ALA HIS LEU ARG ARG ILE
SEQRES 4 A 271 VAL GLU ALA ALA ARG PRO PHE THR GLY PRO VAL PHE GLU
SEQRES 5 A 271 VAL GLY PRO GLY LEU GLY ALA LEU THR ARG ALA LEU LEU
SEQRES 6 A 271 GLU ALA GLY ALA GLU VAL THR ALA ILE GLU LYS ASP LEU
SEQRES 7 A 271 ARG LEU ARG PRO VAL LEU GLU GLU THR LEU SER GLY LEU
SEQRES 8 A 271 PRO VAL ARG LEU VAL PHE GLN ASP ALA LEU LEU TYR PRO
SEQRES 9 A 271 TRP GLU GLU VAL PRO GLN GLY SER LEU LEU VAL ALA ASN
SEQRES 10 A 271 LEU PRO TYR HIS ILE ALA THR PRO LEU VAL THR ARG LEU
SEQRES 11 A 271 LEU LYS THR GLY ARG PHE ALA ARG LEU VAL PHE LEU VAL
SEQRES 12 A 271 GLN LYS GLU VAL ALA GLU ARG MET THR ALA ARG PRO LYS
SEQRES 13 A 271 THR PRO ALA TYR GLY VAL LEU THR LEU ARG VAL ALA HIS
SEQRES 14 A 271 HIS ALA VAL ALA GLU ARG LEU PHE ASP LEU PRO PRO GLY
SEQRES 15 A 271 ALA PHE PHE PRO PRO PRO LYS VAL TRP SER SER LEU VAL
SEQRES 16 A 271 ARG LEU THR PRO THR GLY ALA LEU ASP ASP PRO GLY LEU
SEQRES 17 A 271 PHE ARG LEU VAL GLU ALA ALA PHE GLY LYS ARG ARG LYS
SEQRES 18 A 271 THR LEU LEU ASN ALA LEU ALA ALA ALA GLY TYR PRO LYS
SEQRES 19 A 271 ALA ARG VAL GLU GLU ALA LEU ARG ALA LEU GLY LEU PRO
SEQRES 20 A 271 PRO ARG VAL ARG ALA GLU GLU LEU ASP LEU GLU ALA PHE
SEQRES 21 A 271 ARG ARG LEU ARG GLU GLY LEU GLU GLY ALA VAL
SEQRES 1 B 271 MET SER LYS LEU ALA SER PRO GLN SER VAL ARG ALA LEU
SEQRES 2 B 271 LEU GLU ARG HIS GLY LEU PHE ALA ASP LYS ARG PHE GLY
SEQRES 3 B 271 GLN ASN PHE LEU VAL SER GLU ALA HIS LEU ARG ARG ILE
SEQRES 4 B 271 VAL GLU ALA ALA ARG PRO PHE THR GLY PRO VAL PHE GLU
SEQRES 5 B 271 VAL GLY PRO GLY LEU GLY ALA LEU THR ARG ALA LEU LEU
SEQRES 6 B 271 GLU ALA GLY ALA GLU VAL THR ALA ILE GLU LYS ASP LEU
SEQRES 7 B 271 ARG LEU ARG PRO VAL LEU GLU GLU THR LEU SER GLY LEU
SEQRES 8 B 271 PRO VAL ARG LEU VAL PHE GLN ASP ALA LEU LEU TYR PRO
SEQRES 9 B 271 TRP GLU GLU VAL PRO GLN GLY SER LEU LEU VAL ALA ASN
SEQRES 10 B 271 LEU PRO TYR HIS ILE ALA THR PRO LEU VAL THR ARG LEU
SEQRES 11 B 271 LEU LYS THR GLY ARG PHE ALA ARG LEU VAL PHE LEU VAL
SEQRES 12 B 271 GLN LYS GLU VAL ALA GLU ARG MET THR ALA ARG PRO LYS
SEQRES 13 B 271 THR PRO ALA TYR GLY VAL LEU THR LEU ARG VAL ALA HIS
SEQRES 14 B 271 HIS ALA VAL ALA GLU ARG LEU PHE ASP LEU PRO PRO GLY
SEQRES 15 B 271 ALA PHE PHE PRO PRO PRO LYS VAL TRP SER SER LEU VAL
SEQRES 16 B 271 ARG LEU THR PRO THR GLY ALA LEU ASP ASP PRO GLY LEU
SEQRES 17 B 271 PHE ARG LEU VAL GLU ALA ALA PHE GLY LYS ARG ARG LYS
SEQRES 18 B 271 THR LEU LEU ASN ALA LEU ALA ALA ALA GLY TYR PRO LYS
SEQRES 19 B 271 ALA ARG VAL GLU GLU ALA LEU ARG ALA LEU GLY LEU PRO
SEQRES 20 B 271 PRO ARG VAL ARG ALA GLU GLU LEU ASP LEU GLU ALA PHE
SEQRES 21 B 271 ARG ARG LEU ARG GLU GLY LEU GLU GLY ALA VAL
SEQRES 1 C 271 MET SER LYS LEU ALA SER PRO GLN SER VAL ARG ALA LEU
SEQRES 2 C 271 LEU GLU ARG HIS GLY LEU PHE ALA ASP LYS ARG PHE GLY
SEQRES 3 C 271 GLN ASN PHE LEU VAL SER GLU ALA HIS LEU ARG ARG ILE
SEQRES 4 C 271 VAL GLU ALA ALA ARG PRO PHE THR GLY PRO VAL PHE GLU
SEQRES 5 C 271 VAL GLY PRO GLY LEU GLY ALA LEU THR ARG ALA LEU LEU
SEQRES 6 C 271 GLU ALA GLY ALA GLU VAL THR ALA ILE GLU LYS ASP LEU
SEQRES 7 C 271 ARG LEU ARG PRO VAL LEU GLU GLU THR LEU SER GLY LEU
SEQRES 8 C 271 PRO VAL ARG LEU VAL PHE GLN ASP ALA LEU LEU TYR PRO
SEQRES 9 C 271 TRP GLU GLU VAL PRO GLN GLY SER LEU LEU VAL ALA ASN
SEQRES 10 C 271 LEU PRO TYR HIS ILE ALA THR PRO LEU VAL THR ARG LEU
SEQRES 11 C 271 LEU LYS THR GLY ARG PHE ALA ARG LEU VAL PHE LEU VAL
SEQRES 12 C 271 GLN LYS GLU VAL ALA GLU ARG MET THR ALA ARG PRO LYS
SEQRES 13 C 271 THR PRO ALA TYR GLY VAL LEU THR LEU ARG VAL ALA HIS
SEQRES 14 C 271 HIS ALA VAL ALA GLU ARG LEU PHE ASP LEU PRO PRO GLY
SEQRES 15 C 271 ALA PHE PHE PRO PRO PRO LYS VAL TRP SER SER LEU VAL
SEQRES 16 C 271 ARG LEU THR PRO THR GLY ALA LEU ASP ASP PRO GLY LEU
SEQRES 17 C 271 PHE ARG LEU VAL GLU ALA ALA PHE GLY LYS ARG ARG LYS
SEQRES 18 C 271 THR LEU LEU ASN ALA LEU ALA ALA ALA GLY TYR PRO LYS
SEQRES 19 C 271 ALA ARG VAL GLU GLU ALA LEU ARG ALA LEU GLY LEU PRO
SEQRES 20 C 271 PRO ARG VAL ARG ALA GLU GLU LEU ASP LEU GLU ALA PHE
SEQRES 21 C 271 ARG ARG LEU ARG GLU GLY LEU GLU GLY ALA VAL
HET MTA A 272 20
HET MTA B 272 20
HET MTA C 272 20
HETNAM MTA 5'-DEOXY-5'-METHYLTHIOADENOSINE
FORMUL 4 MTA 3(C11 H15 N5 O3 S)
FORMUL 7 HOH *708(H2 O)
HELIX 1 1 SER A 6 HIS A 17 1 12
HELIX 2 2 ASP A 22 GLY A 26 5 5
HELIX 3 3 SER A 32 ARG A 44 1 13
HELIX 4 4 GLY A 58 ALA A 67 1 10
HELIX 5 5 ASP A 77 ARG A 79 5 3
HELIX 6 6 LEU A 80 LEU A 88 1 9
HELIX 7 7 ASP A 99 TYR A 103 5 5
HELIX 8 8 PRO A 104 VAL A 108 5 5
HELIX 9 9 ILE A 122 GLY A 134 1 13
HELIX 10 10 LYS A 145 THR A 152 1 8
HELIX 11 11 GLY A 161 HIS A 170 1 10
HELIX 12 12 PRO A 180 GLY A 182 5 3
HELIX 13 13 ASP A 205 LYS A 218 1 14
HELIX 14 14 THR A 222 ALA A 230 1 9
HELIX 15 15 PRO A 233 LEU A 244 1 12
HELIX 16 16 ARG A 251 LEU A 255 5 5
HELIX 17 17 ASP A 256 GLU A 268 1 13
HELIX 18 18 SER B 6 HIS B 17 1 12
HELIX 19 19 ASP B 22 GLY B 26 5 5
HELIX 20 20 SER B 32 ARG B 44 1 13
HELIX 21 21 GLY B 58 ALA B 67 1 10
HELIX 22 22 ASP B 77 ARG B 79 5 3
HELIX 23 23 LEU B 80 LEU B 88 1 9
HELIX 24 24 ASP B 99 TYR B 103 5 5
HELIX 25 25 PRO B 104 VAL B 108 5 5
HELIX 26 26 ILE B 122 GLY B 134 1 13
HELIX 27 27 LYS B 145 ALA B 153 1 9
HELIX 28 28 GLY B 161 HIS B 170 1 10
HELIX 29 29 PRO B 180 GLY B 182 5 3
HELIX 30 30 ASP B 205 PHE B 216 1 12
HELIX 31 31 THR B 222 ALA B 230 1 9
HELIX 32 32 PRO B 233 LEU B 244 1 12
HELIX 33 33 ARG B 251 LEU B 255 5 5
HELIX 34 34 ASP B 256 GLU B 268 1 13
HELIX 35 35 SER C 6 HIS C 17 1 12
HELIX 36 36 ASP C 22 GLY C 26 5 5
HELIX 37 37 SER C 32 ARG C 44 1 13
HELIX 38 38 GLY C 58 ALA C 67 1 10
HELIX 39 39 ASP C 77 ARG C 79 5 3
HELIX 40 40 LEU C 80 LEU C 88 1 9
HELIX 41 41 ASP C 99 TYR C 103 5 5
HELIX 42 42 PRO C 104 VAL C 108 5 5
HELIX 43 43 PRO C 119 HIS C 121 5 3
HELIX 44 44 ILE C 122 GLY C 134 1 13
HELIX 45 45 LYS C 145 THR C 152 1 8
HELIX 46 46 GLY C 161 HIS C 170 1 10
HELIX 47 47 PRO C 180 GLY C 182 5 3
HELIX 48 48 ASP C 205 PHE C 216 1 12
HELIX 49 49 THR C 222 ALA C 230 1 9
HELIX 50 50 PRO C 233 LEU C 244 1 12
HELIX 51 51 ARG C 251 LEU C 255 5 5
HELIX 52 52 ASP C 256 GLU C 268 1 13
SHEET 1 A 2 PHE A 29 LEU A 30 0
SHEET 2 A 2 PHE A 184 PHE A 185 -1 O PHE A 185 N PHE A 29
SHEET 1 B 7 VAL A 93 PHE A 97 0
SHEET 2 B 7 VAL A 71 GLU A 75 1 N ALA A 73 O ARG A 94
SHEET 3 B 7 VAL A 50 VAL A 53 1 N GLU A 52 O THR A 72
SHEET 4 B 7 SER A 112 ASN A 117 1 O LEU A 113 N PHE A 51
SHEET 5 B 7 PHE A 136 GLN A 144 1 O VAL A 140 N LEU A 114
SHEET 6 B 7 SER A 192 PRO A 199 -1 O LEU A 197 N LEU A 139
SHEET 7 B 7 ALA A 171 LEU A 179 -1 N LEU A 176 O LEU A 194
SHEET 1 C 2 PHE B 29 LEU B 30 0
SHEET 2 C 2 PHE B 184 PHE B 185 -1 O PHE B 185 N PHE B 29
SHEET 1 D 7 ARG B 94 VAL B 96 0
SHEET 2 D 7 VAL B 71 ILE B 74 1 N ALA B 73 O ARG B 94
SHEET 3 D 7 VAL B 50 VAL B 53 1 N GLU B 52 O ILE B 74
SHEET 4 D 7 SER B 112 ASN B 117 1 O LEU B 113 N PHE B 51
SHEET 5 D 7 PHE B 136 GLN B 144 1 O VAL B 140 N LEU B 114
SHEET 6 D 7 SER B 192 PRO B 199 -1 O LEU B 197 N LEU B 139
SHEET 7 D 7 ALA B 171 LEU B 179 -1 N LEU B 176 O LEU B 194
SHEET 1 E 2 PHE C 29 LEU C 30 0
SHEET 2 E 2 PHE C 184 PHE C 185 -1 O PHE C 185 N PHE C 29
SHEET 1 F 7 VAL C 93 VAL C 96 0
SHEET 2 F 7 VAL C 71 ILE C 74 1 N ALA C 73 O VAL C 96
SHEET 3 F 7 VAL C 50 VAL C 53 1 N GLU C 52 O ILE C 74
SHEET 4 F 7 SER C 112 ASN C 117 1 O LEU C 113 N PHE C 51
SHEET 5 F 7 PHE C 136 GLN C 144 1 O VAL C 140 N LEU C 114
SHEET 6 F 7 SER C 192 PRO C 199 -1 O LEU C 197 N LEU C 139
SHEET 7 F 7 ALA C 171 LEU C 179 -1 N LEU C 179 O SER C 192
CISPEP 1 ARG A 44 PRO A 45 0 -1.77
CISPEP 2 PHE A 185 PRO A 186 0 -7.40
CISPEP 3 ARG B 44 PRO B 45 0 -2.79
CISPEP 4 PHE B 185 PRO B 186 0 -10.08
CISPEP 5 ARG C 44 PRO C 45 0 -3.22
CISPEP 6 PHE C 185 PRO C 186 0 -6.85
SITE 1 AC1 15 PHE A 25 GLY A 26 GLN A 27 ASN A 28
SITE 2 AC1 15 GLY A 54 GLY A 56 ILE A 74 GLU A 75
SITE 3 AC1 15 LYS A 76 ASP A 99 ALA A 100 ASN A 117
SITE 4 AC1 15 LEU A 118 PRO A 119 HIS A 121
SITE 1 AC2 14 PHE B 25 GLY B 26 GLN B 27 ASN B 28
SITE 2 AC2 14 GLY B 54 GLY B 56 ILE B 74 GLU B 75
SITE 3 AC2 14 LYS B 76 ASP B 99 ALA B 100 ASN B 117
SITE 4 AC2 14 PRO B 119 HIS B 121
SITE 1 AC3 15 PHE C 25 GLY C 26 GLN C 27 ASN C 28
SITE 2 AC3 15 GLY C 54 GLY C 56 ILE C 74 GLU C 75
SITE 3 AC3 15 LYS C 76 ASP C 99 ALA C 100 ASN C 117
SITE 4 AC3 15 PRO C 119 HIS C 121 HOH C 403
CRYST1 56.056 79.908 186.436 90.00 90.00 90.00 P 21 21 21 12
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 0.017839 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012514 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
