HEADER COMPLEX (METHYLTRANSFERASE/TRNA) 29-JUL-98 2FMT
TITLE METHIONYL-TRNAFMET FORMYLTRANSFERASE COMPLEXED WITH FORMYL-METHIONYL-
TITLE 2 TRNAFMET
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORMYL-METHIONYL-TRNAFMET2;
COMPND 3 CHAIN: C, D;
COMPND 4 SYNONYM: INITIATOR TRNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: METHIONYL-TRNA FMET FORMYLTRANSFERASE;
COMPND 8 CHAIN: A, B;
COMPND 9 SYNONYM: 10-FORMYLTETRAHYDROFOLATE L-METHIONYL TRNAFMET
COMPND 10 FORMYLTRANSFERASE;
COMPND 11 EC: 2.1.2.9;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 562;
SOURCE 8 STRAIN: K37;
SOURCE 9 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 GENE: FMT;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: JM101TR;
SOURCE 14 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR: PUC18;
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PUCFATG
KEYWDS COMPLEX (METHYLTRANSFERASE-TRNA), FORMYLTRANSFERASE, INITIATION OF
KEYWDS 2 TRANSLATION, COMPLEX (METHYLTRANSFERASE-TRNA) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SCHMITT,Y.MECHULAM,S.BLANQUET
REVDAT 4 02-AUG-23 2FMT 1 REMARK LINK
REVDAT 3 19-FEB-20 2FMT 1 SOURCE REMARK LINK
REVDAT 2 24-FEB-09 2FMT 1 VERSN
REVDAT 1 29-JUL-99 2FMT 0
JRNL AUTH E.SCHMITT,M.PANVERT,S.BLANQUET,Y.MECHULAM
JRNL TITL CRYSTAL STRUCTURE OF METHIONYL-TRNAFMET TRANSFORMYLASE
JRNL TITL 2 COMPLEXED WITH THE INITIATOR FORMYL-METHIONYL-TRNAFMET.
JRNL REF EMBO J. V. 17 6819 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9843487
JRNL DOI 10.1093/EMBOJ/17.23.6819
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.3C
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 87.2
REMARK 3 NUMBER OF REFLECTIONS : 26136
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) : 0.247
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1528
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2171
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE : 0.4280
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 135
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4784
REMARK 3 NUCLEIC ACID ATOMS : 3290
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 83
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 78.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.23000
REMARK 3 B22 (A**2) : -7.43000
REMARK 3 B33 (A**2) : 26.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.440
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.72
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.270
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) : 2.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.700 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.600 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.900 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.23
REMARK 3 BSOL : 15.10
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.15 ; 50
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : 0.26 ; 50
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PARAM11.WAT
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.WAT
REMARK 3 TOPOLOGY FILE 3 : DNA-RNA-MULTI-ENDO.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE POSITIONS OF BASES 1, 16 - 18 AND 37 IN CHAINS C AND D
REMARK 3 ARE TENTATIVE.
REMARK 4
REMARK 4 2FMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000178099.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : DW32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29912
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: PDB ENTRY 1FMT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 100.85500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 100.85500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.03000
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
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICALLY ACTIVE COMPLEX CORRESPONDS TO EITHER
REMARK 300 CHAINS A AND C, OR CHAINS B AND D. THE COORDINATES FOR
REMARK 300 CHAINS A AND C ARE MORE ACCURATE.
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 APPLY THE FOLLOWING TO CHAINS: C, 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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 O3' A D 76 O FME D 586 2.15
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 C C 1 P C C 1 OP3 -0.084
REMARK 500 A C 76 O3' A C 76 C3' 0.073
REMARK 500 C D 1 P C D 1 OP3 -0.089
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 G C 2 O3' - P - OP1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 G D 2 O3' - P - OP2 ANGL. DEV. = 9.0 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 THR A 11 -61.27 -128.18
REMARK 500 ALA A 40 106.21 -161.76
REMARK 500 ARG A 42 96.83 69.34
REMARK 500 PRO A 48 -159.20 -68.97
REMARK 500 LYS A 58 0.73 -63.38
REMARK 500 GLN A 64 55.86 -118.57
REMARK 500 GLN A 81 75.86 34.31
REMARK 500 LEU A 114 165.39 -48.73
REMARK 500 THR A 134 -161.66 -160.14
REMARK 500 ASP A 142 -160.28 -111.25
REMARK 500 THR A 159 -170.94 -66.13
REMARK 500 THR A 163 -160.61 -105.84
REMARK 500 MET A 235 117.09 90.71
REMARK 500 THR A 255 103.49 -161.66
REMARK 500 ALA A 267 79.49 -164.20
REMARK 500 ASP A 278 109.86 -165.74
REMARK 500 ALA A 289 125.35 -33.65
REMARK 500 LYS A 291 -165.28 -119.08
REMARK 500 ASN A 301 10.45 -68.56
REMARK 500 SER A 302 -2.91 -160.08
REMARK 500 ARG A 303 40.32 -142.23
REMARK 500 SER B 3 109.39 -57.58
REMARK 500 THR B 11 -61.34 -127.30
REMARK 500 THR B 34 -160.76 -129.45
REMARK 500 ASP B 37 155.55 -43.73
REMARK 500 ALA B 40 115.66 -163.71
REMARK 500 ARG B 42 100.43 56.77
REMARK 500 GLN B 64 54.12 -116.31
REMARK 500 GLN B 81 78.58 31.35
REMARK 500 LEU B 114 166.30 -47.41
REMARK 500 ILE B 123 -70.38 -70.09
REMARK 500 THR B 134 -169.23 -160.62
REMARK 500 ASP B 142 -157.35 -113.25
REMARK 500 ASP B 146 45.42 39.03
REMARK 500 THR B 159 -169.50 -67.11
REMARK 500 THR B 163 -159.65 -108.44
REMARK 500 GLU B 198 -18.93 -45.34
REMARK 500 ARG B 213 135.50 -35.61
REMARK 500 ILE B 227 -19.04 -49.69
REMARK 500 MET B 235 107.69 90.50
REMARK 500 GLU B 241 45.31 71.79
REMARK 500 ASP B 254 76.41 -103.75
REMARK 500 THR B 255 69.88 -152.52
REMARK 500 ALA B 256 148.11 -22.89
REMARK 500 ALA B 267 75.94 -159.12
REMARK 500 THR B 276 -166.18 -118.15
REMARK 500 ASP B 278 144.42 -171.50
REMARK 500 ALA B 289 128.94 -39.18
REMARK 500 SER B 302 -8.31 -162.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 U D 24 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FME C 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FME D 586
DBREF 2FMT A 1 314 UNP P23882 FMT_ECOLI 1 314
DBREF 2FMT B 1 314 UNP P23882 FMT_ECOLI 1 314
DBREF 2FMT C 1 76 PDB 2FMT 2FMT 1 76
DBREF 2FMT D 1 76 PDB 2FMT 2FMT 1 76
SEQRES 1 C 77 C G C G G G G 4SU G G A G C
SEQRES 2 C 77 A G C C U G G H2U A G C U C
SEQRES 3 C 77 G U C G G G OMC U C A U A A
SEQRES 4 C 77 C C C G A A G A U C G U C
SEQRES 5 C 77 G G 5MU PSU C A A A U C C G G
SEQRES 6 C 77 C C C C C G C A A C C A
SEQRES 1 D 77 C G C G G G G 4SU G G A G C
SEQRES 2 D 77 A G C C U G G H2U A G C U C
SEQRES 3 D 77 G U C G G G OMC U C A U A A
SEQRES 4 D 77 C C C G A A G A U C G U C
SEQRES 5 D 77 G G 5MU PSU C A A A U C C G G
SEQRES 6 D 77 C C C C C G C A A C C A
SEQRES 1 A 314 SER GLU SER LEU ARG ILE ILE PHE ALA GLY THR PRO ASP
SEQRES 2 A 314 PHE ALA ALA ARG HIS LEU ASP ALA LEU LEU SER SER GLY
SEQRES 3 A 314 HIS ASN VAL VAL GLY VAL PHE THR GLN PRO ASP ARG PRO
SEQRES 4 A 314 ALA GLY ARG GLY LYS LYS LEU MET PRO SER PRO VAL LYS
SEQRES 5 A 314 VAL LEU ALA GLU GLU LYS GLY LEU PRO VAL PHE GLN PRO
SEQRES 6 A 314 VAL SER LEU ARG PRO GLN GLU ASN GLN GLN LEU VAL ALA
SEQRES 7 A 314 GLU LEU GLN ALA ASP VAL MET VAL VAL VAL ALA TYR GLY
SEQRES 8 A 314 LEU ILE LEU PRO LYS ALA VAL LEU GLU MET PRO ARG LEU
SEQRES 9 A 314 GLY CYS ILE ASN VAL HIS GLY SER LEU LEU PRO ARG TRP
SEQRES 10 A 314 ARG GLY ALA ALA PRO ILE GLN ARG SER LEU TRP ALA GLY
SEQRES 11 A 314 ASP ALA GLU THR GLY VAL THR ILE MET GLN MET ASP VAL
SEQRES 12 A 314 GLY LEU ASP THR GLY ASP MET LEU TYR LYS LEU SER CYS
SEQRES 13 A 314 PRO ILE THR ALA GLU ASP THR SER GLY THR LEU TYR ASP
SEQRES 14 A 314 LYS LEU ALA GLU LEU GLY PRO GLN GLY LEU ILE THR THR
SEQRES 15 A 314 LEU LYS GLN LEU ALA ASP GLY THR ALA LYS PRO GLU VAL
SEQRES 16 A 314 GLN ASP GLU THR LEU VAL THR TYR ALA GLU LYS LEU SER
SEQRES 17 A 314 LYS GLU GLU ALA ARG ILE ASP TRP SER LEU SER ALA ALA
SEQRES 18 A 314 GLN LEU GLU ARG CYS ILE ARG ALA PHE ASN PRO TRP PRO
SEQRES 19 A 314 MET SER TRP LEU GLU ILE GLU GLY GLN PRO VAL LYS VAL
SEQRES 20 A 314 TRP LYS ALA SER VAL ILE ASP THR ALA THR ASN ALA ALA
SEQRES 21 A 314 PRO GLY THR ILE LEU GLU ALA ASN LYS GLN GLY ILE GLN
SEQRES 22 A 314 VAL ALA THR GLY ASP GLY ILE LEU ASN LEU LEU SER LEU
SEQRES 23 A 314 GLN PRO ALA GLY LYS LYS ALA MET SER ALA GLN ASP LEU
SEQRES 24 A 314 LEU ASN SER ARG ARG GLU TRP PHE VAL PRO GLY ASN ARG
SEQRES 25 A 314 LEU VAL
SEQRES 1 B 314 SER GLU SER LEU ARG ILE ILE PHE ALA GLY THR PRO ASP
SEQRES 2 B 314 PHE ALA ALA ARG HIS LEU ASP ALA LEU LEU SER SER GLY
SEQRES 3 B 314 HIS ASN VAL VAL GLY VAL PHE THR GLN PRO ASP ARG PRO
SEQRES 4 B 314 ALA GLY ARG GLY LYS LYS LEU MET PRO SER PRO VAL LYS
SEQRES 5 B 314 VAL LEU ALA GLU GLU LYS GLY LEU PRO VAL PHE GLN PRO
SEQRES 6 B 314 VAL SER LEU ARG PRO GLN GLU ASN GLN GLN LEU VAL ALA
SEQRES 7 B 314 GLU LEU GLN ALA ASP VAL MET VAL VAL VAL ALA TYR GLY
SEQRES 8 B 314 LEU ILE LEU PRO LYS ALA VAL LEU GLU MET PRO ARG LEU
SEQRES 9 B 314 GLY CYS ILE ASN VAL HIS GLY SER LEU LEU PRO ARG TRP
SEQRES 10 B 314 ARG GLY ALA ALA PRO ILE GLN ARG SER LEU TRP ALA GLY
SEQRES 11 B 314 ASP ALA GLU THR GLY VAL THR ILE MET GLN MET ASP VAL
SEQRES 12 B 314 GLY LEU ASP THR GLY ASP MET LEU TYR LYS LEU SER CYS
SEQRES 13 B 314 PRO ILE THR ALA GLU ASP THR SER GLY THR LEU TYR ASP
SEQRES 14 B 314 LYS LEU ALA GLU LEU GLY PRO GLN GLY LEU ILE THR THR
SEQRES 15 B 314 LEU LYS GLN LEU ALA ASP GLY THR ALA LYS PRO GLU VAL
SEQRES 16 B 314 GLN ASP GLU THR LEU VAL THR TYR ALA GLU LYS LEU SER
SEQRES 17 B 314 LYS GLU GLU ALA ARG ILE ASP TRP SER LEU SER ALA ALA
SEQRES 18 B 314 GLN LEU GLU ARG CYS ILE ARG ALA PHE ASN PRO TRP PRO
SEQRES 19 B 314 MET SER TRP LEU GLU ILE GLU GLY GLN PRO VAL LYS VAL
SEQRES 20 B 314 TRP LYS ALA SER VAL ILE ASP THR ALA THR ASN ALA ALA
SEQRES 21 B 314 PRO GLY THR ILE LEU GLU ALA ASN LYS GLN GLY ILE GLN
SEQRES 22 B 314 VAL ALA THR GLY ASP GLY ILE LEU ASN LEU LEU SER LEU
SEQRES 23 B 314 GLN PRO ALA GLY LYS LYS ALA MET SER ALA GLN ASP LEU
SEQRES 24 B 314 LEU ASN SER ARG ARG GLU TRP PHE VAL PRO GLY ASN ARG
SEQRES 25 B 314 LEU VAL
MODRES 2FMT 4SU C 8 U 4-THIOURIDINE-5'-MONOPHOSPHATE
MODRES 2FMT H2U C 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 2FMT OMC C 32 C O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
MODRES 2FMT 5MU C 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 2FMT PSU C 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 2FMT 4SU D 8 U 4-THIOURIDINE-5'-MONOPHOSPHATE
MODRES 2FMT H2U D 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 2FMT OMC D 32 C O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
MODRES 2FMT 5MU D 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 2FMT PSU D 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET 4SU C 8 20
HET H2U C 20 20
HET OMC C 32 21
HET 5MU C 54 21
HET PSU C 55 20
HET 4SU D 8 20
HET H2U D 20 20
HET OMC D 32 21
HET 5MU D 54 21
HET PSU D 55 20
HET MG C 584 1
HET FME C 585 10
HET MG D 585 1
HET FME D 586 10
HETNAM 4SU 4-THIOURIDINE-5'-MONOPHOSPHATE
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM FME N-FORMYLMETHIONINE
FORMUL 1 4SU 2(C9 H13 N2 O8 P S)
FORMUL 1 H2U 2(C9 H15 N2 O9 P)
FORMUL 1 OMC 2(C10 H16 N3 O8 P)
FORMUL 1 5MU 2(C10 H15 N2 O9 P)
FORMUL 1 PSU 2(C9 H13 N2 O9 P)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 FME 2(C6 H11 N O3 S)
FORMUL 9 HOH *83(H2 O)
HELIX 1 1 ASP A 13 SER A 24 1 12
HELIX 2 2 PRO A 50 LYS A 58 1 9
HELIX 3 3 GLN A 71 LEU A 80 1 10
HELIX 4 4 LYS A 96 MET A 101 1 6
HELIX 5 5 PRO A 122 TRP A 128 1 7
HELIX 6 6 SER A 164 ASP A 188 1 25
HELIX 7 7 GLU A 198 LEU A 200 5 3
HELIX 8 8 LYS A 209 ALA A 212 1 4
HELIX 9 9 ALA A 220 ALA A 229 1 10
HELIX 10 10 ALA A 296 PHE A 307 1 12
HELIX 11 11 ASP B 13 SER B 24 1 12
HELIX 12 12 PRO B 50 LYS B 58 1 9
HELIX 13 13 GLN B 71 LEU B 80 1 10
HELIX 14 14 LYS B 96 MET B 101 1 6
HELIX 15 15 PRO B 122 TRP B 128 1 7
HELIX 16 16 SER B 164 ASP B 188 1 25
HELIX 17 17 GLU B 198 LEU B 200 5 3
HELIX 18 18 LYS B 209 ALA B 212 1 4
HELIX 19 19 ALA B 220 ALA B 229 1 10
HELIX 20 20 ALA B 296 LEU B 300 1 5
HELIX 21 21 ARG B 304 PHE B 307 5 4
SHEET 1 A 6 MET A 150 PRO A 157 0
SHEET 2 A 6 GLU A 133 GLN A 140 -1 N ILE A 138 O LEU A 151
SHEET 3 A 6 CYS A 106 HIS A 110 -1 N HIS A 110 O THR A 137
SHEET 4 A 6 VAL A 84 VAL A 88 1 N MET A 85 O ILE A 107
SHEET 5 A 6 ARG A 5 GLY A 10 1 N ILE A 7 O VAL A 84
SHEET 6 A 6 ASN A 28 PHE A 33 1 N ASN A 28 O ILE A 6
SHEET 1 B 4 TRP A 237 GLU A 239 0
SHEET 2 B 4 PRO A 244 LYS A 249 -1 N VAL A 245 O LEU A 238
SHEET 3 B 4 SER A 285 PRO A 288 -1 N GLN A 287 O LYS A 246
SHEET 4 B 4 ALA A 293 SER A 295 -1 N MET A 294 O LEU A 286
SHEET 1 C 3 ALA A 250 ILE A 253 0
SHEET 2 C 3 ILE A 280 LEU A 283 -1 N ASN A 282 O SER A 251
SHEET 3 C 3 ILE A 272 ALA A 275 -1 N VAL A 274 O LEU A 281
SHEET 1 D 6 MET B 150 PRO B 157 0
SHEET 2 D 6 GLU B 133 GLN B 140 -1 N ILE B 138 O LEU B 151
SHEET 3 D 6 CYS B 106 HIS B 110 -1 N HIS B 110 O THR B 137
SHEET 4 D 6 VAL B 84 VAL B 88 1 N MET B 85 O ILE B 107
SHEET 5 D 6 ARG B 5 GLY B 10 1 N ILE B 7 O VAL B 84
SHEET 6 D 6 ASN B 28 PHE B 33 1 N ASN B 28 O ILE B 6
SHEET 1 E 4 TRP B 237 GLU B 239 0
SHEET 2 E 4 PRO B 244 LYS B 249 -1 N VAL B 245 O LEU B 238
SHEET 3 E 4 SER B 285 PRO B 288 -1 N GLN B 287 O LYS B 246
SHEET 4 E 4 ALA B 293 SER B 295 -1 N MET B 294 O LEU B 286
SHEET 1 F 3 ALA B 250 ILE B 253 0
SHEET 2 F 3 ILE B 280 LEU B 283 -1 N ASN B 282 O SER B 251
SHEET 3 F 3 ILE B 272 ALA B 275 -1 N VAL B 274 O LEU B 281
LINK O3' G C 7 P 4SU C 8 1555 1555 1.62
LINK O3' 4SU C 8 P G C 9 1555 1555 1.60
LINK O3' G C 19 P H2U C 20 1555 1555 1.61
LINK O3' H2U C 20 P A C 21 1555 1555 1.60
LINK O3' G C 31 P OMC C 32 1555 1555 1.62
LINK O3' OMC C 32 P U C 33 1555 1555 1.63
LINK O3' G C 53 P 5MU C 54 1555 1555 1.62
LINK O3' 5MU C 54 P PSU C 55 1555 1555 1.60
LINK O3' PSU C 55 P C C 56 1555 1555 1.61
LINK O3' A C 76 C FME C 585 1555 1555 1.40
LINK O3' G D 7 P 4SU D 8 1555 1555 1.62
LINK O3' 4SU D 8 P G D 9 1555 1555 1.61
LINK O3' G D 19 P H2U D 20 1555 1555 1.61
LINK O3' H2U D 20 P A D 21 1555 1555 1.62
LINK O3' G D 31 P OMC D 32 1555 1555 1.61
LINK O3' OMC D 32 P U D 33 1555 1555 1.62
LINK O3' G D 53 P 5MU D 54 1555 1555 1.62
LINK O3' 5MU D 54 P PSU D 55 1555 1555 1.60
LINK O3' PSU D 55 P C D 56 1555 1555 1.61
LINK O3' A D 76 C FME D 586 1555 1555 1.36
LINK OP2 G C 9 MG MG C 584 1555 1555 2.72
LINK OP1 G D 9 MG MG D 585 1555 1555 3.05
CISPEP 1 LEU A 114 PRO A 115 0 0.48
CISPEP 2 ASN A 231 PRO A 232 0 -0.78
CISPEP 3 TRP A 233 PRO A 234 0 -0.39
CISPEP 4 LEU B 114 PRO B 115 0 0.01
CISPEP 5 ASN B 231 PRO B 232 0 0.58
CISPEP 6 TRP B 233 PRO B 234 0 -0.43
SITE 1 AC3 2 4SU C 8 G C 9
SITE 1 AC4 6 ALA A 89 TYR A 90 ASN A 108 GLY A 119
SITE 2 AC4 6 ALA A 120 A C 76
SITE 1 AC5 2 4SU D 8 G D 9
SITE 1 AC6 7 ALA B 89 TYR B 90 ASN B 108 GLY B 111
SITE 2 AC6 7 GLY B 119 ALA B 120 A D 76
CRYST1 201.710 68.060 86.350 90.00 90.00 90.00 P 21 21 2 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 0.004958 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011581 0.00000
MTRIX1 1 0.979390 -0.201950 -0.002340 6.31224 1
MTRIX2 1 0.201930 0.979370 -0.008130 -48.79334 1
MTRIX3 1 0.003940 0.007490 0.999960 0.78390 1
MTRIX1 2 0.994740 -0.102400 -0.003480 3.90927 1
MTRIX2 2 0.102270 0.994380 -0.027190 -42.12500 1
MTRIX3 2 0.006250 0.026690 0.999620 0.04122 1
(ATOM LINES ARE NOT SHOWN.)
END
