HEADER TRANSFERASE 11-MAR-03 1UAJ
TITLE CRYSTAL STRUCTURE OF TRNA(M1G37)METHYLTRANSFERASE: INSIGHT INTO TRNA
TITLE 2 RECOGNITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRNA(M1G37)METHYLTRANSFERASE;
COMPND 5 EC: 2.1.1.31;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS METHYLTRANSFERASE, SPOUT CLASS, TRMD, TRNA(M1G37)METHYLTRANSFERASE,
KEYWDS 2 TRNA MODIFICATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.AHN,H.-W.KIM,H.-J.YOON,B.I.LEE,S.W.SUH,J.K.YANG
REVDAT 4 27-DEC-23 1UAJ 1 SEQADV
REVDAT 3 13-JUL-11 1UAJ 1 VERSN
REVDAT 2 24-FEB-09 1UAJ 1 VERSN
REVDAT 1 17-JUN-03 1UAJ 0
JRNL AUTH H.J.AHN,H.-W.KIM,H.-J.YOON,B.I.LEE,S.W.SUH,J.K.YANG
JRNL TITL CRYSTAL STRUCTURE OF TRNA(M(1)G37)METHYLTRANSFERASE:
JRNL TITL 2 INSIGHTS INTO TRNA RECOGNITION
JRNL REF EMBO J. V. 22 2593 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12773376
JRNL DOI 10.1093/EMBOJ/CDG269
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2743170.300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 28115
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 SET) : 0.194
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2788
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4162
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 465
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1899
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.17000
REMARK 3 B22 (A**2) : 2.17000
REMARK 3 B33 (A**2) : -4.35000
REMARK 3 B12 (A**2) : 2.22000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.09
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.780
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.290 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.130 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 50.68
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UAJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000005618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9500
REMARK 200 MONOCHROMATOR : SI(111) + GE(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28115
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, SODIUM CACODYLATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 49.02350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 28.30373
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 58.93000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 49.02350
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 28.30373
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 58.93000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 49.02350
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 28.30373
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 58.93000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 49.02350
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 28.30373
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 58.93000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 49.02350
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 28.30373
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 58.93000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 49.02350
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 28.30373
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 58.93000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 56.60746
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 117.86000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 56.60746
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 117.86000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 56.60746
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 117.86000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 56.60746
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 117.86000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 56.60746
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 117.86000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 56.60746
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 117.86000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 6780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 49.02350
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 28.30373
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 58.93000
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A 161
REMARK 465 LYS A 162
REMARK 465 GLN A 163
REMARK 465 ALA A 164
REMARK 465 SER A 165
REMARK 465 ALA A 166
REMARK 465 GLU A 167
REMARK 465 GLU A 168
REMARK 465 ASP A 169
REMARK 465 SER A 170
REMARK 465 PHE A 171
REMARK 465 ALA A 172
REMARK 465 ASP A 173
REMARK 465 LEU A 247
REMARK 465 GLU A 248
REMARK 465 HIS A 249
REMARK 465 HIS A 250
REMARK 465 HIS A 251
REMARK 465 HIS A 252
REMARK 465 HIS A 253
REMARK 465 HIS A 254
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 TYR A 115 -144.74 57.30
REMARK 500 ASN A 245 -73.94 -66.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UAK RELATED DB: PDB
REMARK 900 TRNA(M1G37)METHYLTRANSFERASE WITH S-ADENOSYLMETHIONINE
REMARK 900 RELATED ID: 1UAL RELATED DB: PDB
REMARK 900 TRNA(M1G37)METHYLTRANSFERASE WITH S-ADENOSYL-L-HOMOCYSTEINE
REMARK 900 RELATED ID: 1UAM RELATED DB: PDB
REMARK 900 TRNA(M1G37)METHYLTRANSFERASE WITH S-ADENOSYL-L-HOMOCYSTEINE AND
REMARK 900 PHOSPHATE ION
DBREF 1UAJ A 1 246 UNP P43912 TRMD_HAEIN 1 246
SEQADV 1UAJ MET A -19 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ GLY A -18 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ SER A -17 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ SER A -16 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -15 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -14 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -13 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -12 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -11 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A -10 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ SER A -9 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ SER A -8 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ GLY A -7 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ LEU A -6 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ VAL A -5 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ PRO A -4 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ ARG A -3 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ GLY A -2 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ SER A -1 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 0 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ LEU A 247 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ GLU A 248 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 249 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 250 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 251 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 252 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 253 UNP P43912 EXPRESSION TAG
SEQADV 1UAJ HIS A 254 UNP P43912 EXPRESSION TAG
SEQRES 1 A 274 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 274 LEU VAL PRO ARG GLY SER HIS MET TRP ILE GLY VAL ILE
SEQRES 3 A 274 SER LEU PHE PRO GLU MET PHE LYS ALA ILE THR GLU PHE
SEQRES 4 A 274 GLY VAL THR GLY ARG ALA VAL LYS HIS ASN LEU LEU LYS
SEQRES 5 A 274 VAL GLU CYS TRP ASN PRO ARG ASP PHE THR PHE ASP LYS
SEQRES 6 A 274 HIS LYS THR VAL ASP ASP ARG PRO TYR GLY GLY GLY PRO
SEQRES 7 A 274 GLY MET LEU MET MET VAL GLN PRO LEU ARG ASP ALA ILE
SEQRES 8 A 274 HIS THR ALA LYS ALA ALA ALA GLY GLU GLY ALA LYS VAL
SEQRES 9 A 274 ILE TYR LEU SER PRO GLN GLY ARG LYS LEU ASP GLN GLY
SEQRES 10 A 274 GLY VAL THR GLU LEU ALA GLN ASN GLN LYS LEU ILE LEU
SEQRES 11 A 274 VAL CYS GLY ARG TYR GLU GLY ILE ASP GLU ARG LEU ILE
SEQRES 12 A 274 GLN THR GLU ILE ASP GLU GLU TRP SER ILE GLY ASP TYR
SEQRES 13 A 274 VAL LEU THR GLY GLY GLU LEU PRO ALA MET THR LEU ILE
SEQRES 14 A 274 ASP ALA VAL ALA ARG PHE ILE PRO GLY VAL LEU GLY LYS
SEQRES 15 A 274 GLN ALA SER ALA GLU GLU ASP SER PHE ALA ASP GLY LEU
SEQRES 16 A 274 LEU ASP CYS PRO HIS TYR THR ARG PRO GLU VAL LEU GLU
SEQRES 17 A 274 GLY LEU THR VAL PRO PRO VAL LEU MET SER GLY HIS HIS
SEQRES 18 A 274 GLU GLU ILE ARG LYS TRP ARG LEU LYS GLN SER LEU GLN
SEQRES 19 A 274 ARG THR TRP LEU ARG ARG PRO GLU LEU LEU GLU GLY LEU
SEQRES 20 A 274 ALA LEU THR ASP GLU GLN ARG LYS LEU LEU LYS GLU ALA
SEQRES 21 A 274 GLN ALA GLU HIS ASN SER LEU GLU HIS HIS HIS HIS HIS
SEQRES 22 A 274 HIS
FORMUL 2 HOH *262(H2 O)
HELIX 1 1 PHE A 9 MET A 12 5 4
HELIX 2 2 PHE A 13 GLU A 18 1 6
HELIX 3 3 PHE A 19 HIS A 28 1 10
HELIX 4 4 ASN A 37 THR A 42 5 6
HELIX 5 5 MET A 63 GLY A 79 1 17
HELIX 6 6 ASP A 95 ALA A 103 1 9
HELIX 7 7 ASP A 119 GLU A 126 1 8
HELIX 8 8 GLY A 141 ARG A 154 1 14
HELIX 9 9 PRO A 193 SER A 198 1 6
HELIX 10 10 HIS A 200 ARG A 220 1 21
HELIX 11 11 PRO A 221 LEU A 224 5 4
HELIX 12 12 THR A 230 SER A 246 1 17
SHEET 1 A 6 LEU A 31 TRP A 36 0
SHEET 2 A 6 MET A 1 ILE A 6 1 N ILE A 3 O LYS A 32
SHEET 3 A 6 LYS A 107 VAL A 111 1 O LEU A 110 N GLY A 4
SHEET 4 A 6 LYS A 83 LEU A 87 1 N ILE A 85 O ILE A 109
SHEET 5 A 6 GLU A 129 SER A 132 1 O TRP A 131 N TYR A 86
SHEET 6 A 6 ARG A 92 LYS A 93 1 N ARG A 92 O SER A 132
SHEET 1 B 2 ASP A 50 ASP A 51 0
SHEET 2 B 2 LEU A 61 MET A 62 -1 O LEU A 61 N ASP A 51
SHEET 1 C 2 VAL A 186 LEU A 187 0
SHEET 2 C 2 LEU A 190 THR A 191 -1 O LEU A 190 N LEU A 187
CISPEP 1 ARG A 183 PRO A 184 0 0.21
CRYST1 98.047 98.047 176.790 90.00 90.00 120.00 H 3 2 18
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 0.010199 0.005889 0.000000 0.00000
SCALE2 0.000000 0.011777 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
