HEADER HYDROLASE/NUCLEAR PROTEIN 24-JAN-03 1OB2
TITLE E. COLI ELONGATION FACTOR EF-TU COMPLEXED WITH THE
TITLE 2 ANTIBIOTIC KIRROMYCIN, A GTP ANALOG, AND PHE-TRNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EF-TU, P-43;
COMPND 5 EC: 3.6.1.48;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRANSFER-RNA, PHE;
COMPND 8 CHAIN: B;
COMPND 9 OTHER_DETAILS: AMINO-ACYLATED (PHE) AT THE 3' END
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 511693;
SOURCE 4 STRAIN: BL21;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 8 ORGANISM_TAXID: 4932;
SOURCE 9 OTHER_DETAILS: SIGMA-ALDRICH COMPOUND
KEYWDS HYDROLASE/NUCLEAR PROTEIN, HYDROLASE, GTPASE, TRANSLATION
KEYWDS 2 ELONGATION FACTOR, TRANSFER RNA
EXPDTA X-RAY DIFFRACTION
AUTHOR O.KRISTENSEN,P.NISSEN,J.NYBORG
REVDAT 5 14-NOV-12 1OB2 1 COMPND REMARK VERSN DBREF
REVDAT 5 2 SEQADV MODRES HETSYN FORMUL
REVDAT 4 24-FEB-09 1OB2 1 VERSN
REVDAT 3 14-JUN-06 1OB2 1 ATOM
REVDAT 2 31-AUG-04 1OB2 1 JRNL
REVDAT 1 27-MAY-04 1OB2 0
JRNL AUTH R.C.NIELSEN,O.KRISTENSEN,M.KJELDGAARD,S.THIRUP,
JRNL AUTH 2 P.NISSEN
JRNL TITL KIRROMYCIN DEFINES A SPECIFIC DOMAIN ARRANGEMENT
JRNL TITL 2 OF ELONGATION FACTOR EF-TU
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.35 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 6224852.51
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 18794
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) : 0.220
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 963
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
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) : 3.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2928
REMARK 3 BIN R VALUE (WORKING SET) : 0.249
REMARK 3 BIN FREE R VALUE : 0.285
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.2
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3035
REMARK 3 NUCLEIC ACID ATOMS : 1349
REMARK 3 HETEROGEN ATOMS : 426
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.0
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61
REMARK 3 B22 (A**2) : -0.30
REMARK 3 B33 (A**2) : -0.30
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.35
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) : 4.17 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.78 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.99 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.47 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.303178
REMARK 3 BSOL : 62.1852
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 : TRNAPHE-MULTI.PARAM
REMARK 3 PARAMETER FILE 3 : LIGANDS_HICUP.PAR
REMARK 3 PARAMETER FILE 4 : MG.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TRNAPHE-MULTI.TOP
REMARK 3 TOPOLOGY FILE 3 : LIGANDS_HICUP.TOP
REMARK 3 TOPOLOGY FILE 4 : MG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT WAS INITIATED WITH X-PLOR
REMARK 3 AND COMPLETED WITH CNS. ANTICODON LOOP OF TRNA IS DISORDERED
REMARK 3 AND ONLY THE CHAIN TRACE IN THIS REGION IS VISIBLE IN THE
REMARK 3 ELECTRON DENSITY MAPS.
REMARK 4
REMARK 4 1OB2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-03.
REMARK 100 THE PDBE ID CODE IS EBI-12010.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : AGROVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18794
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.35
REMARK 200 RESOLUTION RANGE LOW (A) : 48.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 5.0
REMARK 200 R MERGE (I) : 0.154
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.1
REMARK 200 R MERGE FOR SHELL (I) : 0.429
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.0
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1TTT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM SULPHATE,
REMARK 280 10 MM MAGNESIUM CHLORIDE, 20 MM TRIS-MES, PH 6.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 98.20500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 98.20500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 98.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 98.20500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 98.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 98.20500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 98.20500
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 98.20500
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 98.20500
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 98.20500
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 98.20500
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 98.20500
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 98.20500
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 98.20500
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 98.20500
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 98.20500
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 98.20500
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 98.20500
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 147.30750
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 49.10250
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 147.30750
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 147.30750
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 147.30750
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 49.10250
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 147.30750
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 49.10250
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 147.30750
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 49.10250
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 147.30750
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 49.10250
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 49.10250
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 147.30750
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 49.10250
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 147.30750
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 147.30750
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 147.30750
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 49.10250
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 147.30750
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 147.30750
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 49.10250
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 49.10250
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 49.10250
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 147.30750
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 49.10250
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 147.30750
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 49.10250
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 147.30750
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 147.30750
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 147.30750
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
REMARK 350 TOTAL BURIED SURFACE AREA: 11980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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 G B 1 OP3 G B 1 P -0.084
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 GLU A 3 -129.69 -68.66
REMARK 500 LYS A 4 -45.74 -160.53
REMARK 500 PHE A 5 98.38 57.34
REMARK 500 THR A 8 135.08 175.64
REMARK 500 LYS A 9 155.67 65.24
REMARK 500 ASP A 21 3.93 34.07
REMARK 500 LYS A 24 -91.78 4.37
REMARK 500 ALA A 30 -74.38 -40.92
REMARK 500 VAL A 34 -72.26 -59.12
REMARK 500 ALA A 36 23.45 -71.65
REMARK 500 LYS A 37 -56.53 -155.20
REMARK 500 THR A 38 7.33 -63.02
REMARK 500 TYR A 39 7.63 -170.83
REMARK 500 ALA A 42 106.94 177.33
REMARK 500 ASP A 47 -33.26 -35.12
REMARK 500 ASP A 50 54.97 -93.78
REMARK 500 ILE A 60 0.14 -153.56
REMARK 500 THR A 61 109.05 61.55
REMARK 500 THR A 71 -167.93 -105.01
REMARK 500 VAL A 127 113.76 15.67
REMARK 500 ASP A 142 69.29 -174.18
REMARK 500 GLU A 143 -16.21 -32.93
REMARK 500 GLU A 155 -35.66 -38.02
REMARK 500 LEU A 156 -71.67 -65.94
REMARK 500 LEU A 157 -71.17 -33.78
REMARK 500 SER A 158 -1.27 -51.31
REMARK 500 ASP A 161 60.41 87.33
REMARK 500 ASP A 166 -9.08 -56.43
REMARK 500 ALA A 177 -74.66 -47.56
REMARK 500 LEU A 178 -36.43 -31.68
REMARK 500 ASP A 181 103.39 -40.41
REMARK 500 ALA A 192 -7.80 -54.29
REMARK 500 ILE A 199 -92.62 -7.10
REMARK 500 GLU A 201 124.89 23.62
REMARK 500 ALA A 205 -75.86 -53.38
REMARK 500 ILE A 206 -40.80 52.85
REMARK 500 ASP A 207 25.36 -75.22
REMARK 500 LEU A 211 128.35 -174.50
REMARK 500 ASP A 216 144.08 -172.93
REMARK 500 ARG A 223 -93.40 -89.87
REMARK 500 ILE A 247 -60.61 68.75
REMARK 500 THR A 256 18.46 -149.91
REMARK 500 PHE A 261 73.58 65.43
REMARK 500 ARG A 262 13.41 47.34
REMARK 500 LEU A 264 150.50 -35.85
REMARK 500 ALA A 270 137.42 -33.52
REMARK 500 LEU A 278 100.47 39.70
REMARK 500 GLU A 285 -3.52 -152.03
REMARK 500 ASP A 314 -1.09 -55.55
REMARK 500 ARG A 333 -112.55 58.52
REMARK 500
REMARK 500 THIS ENTRY HAS 51 RAMACHANDRAN OUTLIERS.
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 B 8 0.07 SIDE CHAIN
REMARK 500 G B 22 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 HIS A 22 24.9 L L OUTSIDE RANGE
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 MG A1398 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 25 OG1
REMARK 620 2 GNP A1397 O1G 107.7
REMARK 620 3 GNP A1397 O2B 77.3 79.1
REMARK 620 4 THR A 61 OG1 74.8 100.1 150.3
REMARK 620 5 GNP A1397 O3G 164.9 57.4 100.6 103.8
REMARK 620 6 GNP A1397 O2A 98.5 132.4 68.6 125.3 94.5
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KIR A1394
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SUC A1396
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A1397
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1398
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (
REMARK 900 EF-TU-MGGDP) COMPLEXED WITH GE2270A, A
REMARK 900 THIAZOLYL PEPTIDE ANTIBIOTIC
REMARK 900 RELATED ID: 1DG1 RELATED DB: PDB
REMARK 900 WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR
REMARK 900 TU).
REMARK 900 RELATED ID: 1EFC RELATED DB: PDB
REMARK 900 INTACT ELONGATION FACTOR FROM E.COLI
REMARK 900 RELATED ID: 1EFM RELATED DB: PDB
REMARK 900 TRYPSIN-MODIFIED ELONGATION FACTOR TU (EF-TU
REMARK 900 -GDP)
REMARK 900 RELATED ID: 1EFU RELATED DB: PDB
REMARK 900 ELONGATION FACTOR COMPLEX EF-TU/EF-TS FROM
REMARK 900 ESCHERICHIA COLI
REMARK 900 RELATED ID: 1ETU RELATED DB: PDB
REMARK 900 ELONGATION FACTOR TU (DOMAIN I) - GUANOSINE
REMARK 900 DIPHOSPHATE COMPLEX
REMARK 900 RELATED ID: 1LS2 RELATED DB: PDB
REMARK 900 FITTING OF EF-TU AND TRNA IN THE LOW
REMARK 900 RESOLUTION CRYO-EM MAPOF AN EF-TU TERNARY
REMARK 900 COMPLEX (GDP AND KIRROMYCIN) BOUND TOE.
REMARK 900 COLI 70S RIBOSOME
REMARK 900 RELATED ID: 1QZD RELATED DB: PDB
REMARK 900 EF-TU.KIRROMYCIN COORDINATES FITTED INTO THE
REMARK 900 CRYO-EM MAP OFEF-TU TERNARY COMPLEX (GDP
REMARK 900 .KIRROMYCIN) BOUND 70S RIBOSOME
DBREF 1OB2 A 1 393 UNP P0CE48 EFTU2_ECOLI 2 394
DBREF 1OB2 B 1 77 PDB 1OB2 1OB2 1 77
SEQADV 1OB2 ALA A 1 UNP P0CE48 SER 2 CONFLICT
SEQRES 1 A 393 ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN
SEQRES 2 A 393 VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR
SEQRES 3 A 393 LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR
SEQRES 4 A 393 GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA
SEQRES 5 A 393 PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER
SEQRES 6 A 393 HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS
SEQRES 7 A 393 VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET
SEQRES 8 A 393 ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL
SEQRES 9 A 393 VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU
SEQRES 10 A 393 HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE
SEQRES 11 A 393 ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU
SEQRES 12 A 393 GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU
SEQRES 13 A 393 LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE
SEQRES 14 A 393 VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA
SEQRES 15 A 393 GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU
SEQRES 16 A 393 ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS
SEQRES 17 A 393 PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER
SEQRES 18 A 393 GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY
SEQRES 19 A 393 ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE
SEQRES 20 A 393 LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET
SEQRES 21 A 393 PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN
SEQRES 22 A 393 VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE
SEQRES 23 A 393 GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS
SEQRES 24 A 393 PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER
SEQRES 25 A 393 LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY
SEQRES 26 A 393 TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR
SEQRES 27 A 393 GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET
SEQRES 28 A 393 PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS
SEQRES 29 A 393 PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG
SEQRES 30 A 393 GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS
SEQRES 31 A 393 VAL LEU SER
SEQRES 1 B 77 G C G G A U U U A 2MG C U C
SEQRES 2 B 77 A G H2U H2U G G G A G A G C M2G
SEQRES 3 B 77 C C A G A OMC U OMG A A YG A PSU
SEQRES 4 B 77 5MC U G G A G 7MG U C 5MC U G U
SEQRES 5 B 77 G U PSU C G MAD U C C A C A G
SEQRES 6 B 77 A A U U C G C A C C A PHA
MODRES 1OB2 2MG B 10 G 2N-METHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 1OB2 H2U B 16 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 H2U B 17 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 M2G B 26 G N2-DIMETHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 1OB2 OMC B 32 C O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 OMG B 34 G O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 1OB2 YG B 37 G WYBUTOSINE
MODRES 1OB2 PSU B 39 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 5MC B 40 C 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 7MG B 46 G 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE
MODRES 1OB2 5MC B 49 C 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 PSU B 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1OB2 MAD B 58 A 6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE
MODRES 1OB2 PHA B 77 PHE PHENYLALANINAL
HET KIR A1394 57
HET 2MG B 10 24
HET H2U B 16 20
HET H2U B 17 20
HET M2G B 26 25
HET OMC B 32 21
HET OMG B 34 24
HET YG B 37 39
HET PSU B 39 20
HET 5MC B 40 21
HET 7MG B 46 24
HET 5MC B 49 21
HET PSU B 55 20
HET MAD B 58 23
HET PHA B 77 11
HET SUC A1396 23
HET GNP A1397 32
HET MG A1398 1
HETNAM KIR KIRROMYCIN
HETNAM 2MG 2N-METHYLGUANOSINE-5'-MONOPHOSPHATE
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM M2G N2-DIMETHYLGUANOSINE-5'-MONOPHOSPHATE
HETNAM OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
HETNAM OMG O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE
HETNAM YG WYBUTOSINE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM 5MC 5-METHYLCYTIDINE-5'-MONOPHOSPHATE
HETNAM 7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE
HETNAM PHA PHENYLALANINAL
HETNAM SUC SUCROSE
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM MAD 6-HYDRO-1-METHYLADENOSINE-5'-MONOPHOSPHATE
HETSYN YG Y-BASE; 1H-IMIDAZO(1,2-ALPHA)PURINE-7-BUTANOIC ACID,4,
HETSYN 2 YG 9-DIHYDRO-ALPHA-((METHOXYCARBONYL)AMINO)-4,6-DIMETHYL-
HETSYN 3 YG 9-OXO-METHYL ESTER
HETSYN KIR MOCIMYCIN; DELVOMYCIN; MYC-8003
FORMUL 3 KIR C43 H60 N2 O12
FORMUL 4 2MG C11 H16 N5 O8 P
FORMUL 5 H2U 2(C9 H15 N2 O9 P)
FORMUL 6 M2G C12 H18 N5 O8 P
FORMUL 7 OMC C10 H16 N3 O8 P
FORMUL 8 OMG C11 H16 N5 O8 P
FORMUL 9 YG C21 H29 N6 O12 P
FORMUL 10 PSU 2(C9 H13 N2 O9 P)
FORMUL 11 5MC 2(C10 H16 N3 O8 P)
FORMUL 12 7MG C11 H18 N5 O8 P
FORMUL 13 PHA C9 H11 N O
FORMUL 14 SUC C12 H22 O11
FORMUL 15 GNP C10 H17 N6 O13 P3
FORMUL 16 MG MG 2+
FORMUL 17 MAD C11 H16 N5 O7 P
HELIX 1 1 GLY A 23 TYR A 39 1 17
HELIX 2 2 ALA A 45 ASP A 50 1 6
HELIX 3 3 ALA A 52 GLY A 59 1 8
HELIX 4 4 HIS A 84 ASP A 86 5 3
HELIX 5 5 TYR A 87 GLN A 97 1 11
HELIX 6 6 MET A 112 VAL A 125 1 14
HELIX 7 7 LYS A 136 VAL A 140 5 5
HELIX 8 8 ASP A 142 ASP A 161 1 20
HELIX 9 9 SER A 173 GLY A 180 1 8
HELIX 10 10 ASP A 181 GLY A 193 1 13
HELIX 11 11 GLY A 193 TYR A 198 1 6
HELIX 12 12 LYS A 282 ILE A 286 5 5
HELIX 13 13 SER A 312 GLY A 316 5 5
SHEET 1 AA 6 SER A 65 ASP A 70 0
SHEET 2 AA 6 HIS A 75 ASP A 80 -1 O TYR A 76 N TYR A 69
SHEET 3 AA 6 HIS A 11 ILE A 17 1 O VAL A 12 N ALA A 77
SHEET 4 AA 6 ALA A 101 ALA A 106 1 O ILE A 102 N ILE A 17
SHEET 5 AA 6 ILE A 130 ASN A 135 1 O ILE A 131 N LEU A 103
SHEET 6 AA 6 ILE A 169 ARG A 171 1 O VAL A 170 N LEU A 134
SHEET 1 AB 4 LEU A 211 PRO A 213 0
SHEET 2 AB 4 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 AB 4 GLU A 241 VAL A 245 -1 O GLU A 243 N ALA A 293
SHEET 4 AB 4 GLN A 251 THR A 254 -1 O GLN A 251 N ILE A 244
SHEET 1 AC 3 ASP A 216 SER A 219 0
SHEET 2 AC 3 THR A 225 ARG A 230 -1 O VAL A 226 N PHE A 218
SHEET 3 AC 3 ASN A 273 VAL A 276 -1 O VAL A 274 N GLY A 229
SHEET 1 AD 7 PRO A 300 TYR A 309 0
SHEET 2 AD 7 ASN A 355 ALA A 367 -1 O ILE A 356 N VAL A 308
SHEET 3 AD 7 THR A 335 THR A 340 -1 O THR A 338 N ILE A 363
SHEET 4 AD 7 GLN A 329 PHE A 332 -1 O PHE A 330 N VAL A 337
SHEET 5 AD 7 ARG A 373 GLU A 378 -1 O ALA A 375 N TYR A 331
SHEET 6 AD 7 ARG A 381 VAL A 391 -1 O ARG A 381 N GLU A 378
SHEET 7 AD 7 PRO A 300 TYR A 309 -1 O GLU A 305 N LYS A 390
LINK MG MG A1398 OG1 THR A 25 1555 1555 2.03
LINK MG MG A1398 O1G GNP A1397 1555 1555 1.86
LINK MG MG A1398 O2B GNP A1397 1555 1555 2.34
LINK MG MG A1398 O2A GNP A1397 1555 1555 2.84
LINK MG MG A1398 O3G GNP A1397 1555 1555 2.83
LINK MG MG A1398 OG1 THR A 61 1555 1555 2.53
LINK O3' A B 9 P 2MG B 10 1555 1555 1.60
LINK O3' 2MG B 10 P C B 11 1555 1555 1.61
LINK O3' G B 15 P H2U B 16 1555 1555 1.61
LINK O3' H2U B 16 P H2U B 17 1555 1555 1.61
LINK O3' H2U B 17 P G B 18 1555 1555 1.61
LINK O3' C B 25 P M2G B 26 1555 1555 1.61
LINK O3' M2G B 26 P C B 27 1555 1555 1.61
LINK O3' A B 31 P OMC B 32 1555 1555 1.61
LINK O3' OMC B 32 P U B 33 1555 1555 1.61
LINK O3' U B 33 P OMG B 34 1555 1555 1.61
LINK O3' OMG B 34 P A B 35 1555 1555 1.61
LINK O3' A B 36 P YG B 37 1555 1555 1.61
LINK O3' YG B 37 P A B 38 1555 1555 1.61
LINK O3' A B 38 P PSU B 39 1555 1555 1.61
LINK O3' PSU B 39 P 5MC B 40 1555 1555 1.61
LINK O3' 5MC B 40 P U B 41 1555 1555 1.61
LINK O3' G B 45 P 7MG B 46 1555 1555 1.61
LINK O3' 7MG B 46 P U B 47 1555 1555 1.61
LINK O3' C B 48 P 5MC B 49 1555 1555 1.60
LINK O3' 5MC B 49 P U B 50 1555 1555 1.61
LINK O3' U B 54 P PSU B 55 1555 1555 1.60
LINK O3' PSU B 55 P C B 56 1555 1555 1.61
LINK O3' G B 57 P MAD B 58 1555 1555 1.60
LINK O3' MAD B 58 P U B 59 1555 1555 1.60
LINK O3' A B 76 C PHA B 77 1555 1555 1.31
CISPEP 1 ILE A 199 PRO A 200 0 0.25
SITE 1 AC1 14 LEU A 120 ARG A 123 GLN A 124 VAL A 125
SITE 2 AC1 14 TYR A 160 ASP A 161 LYS A 313 ASP A 314
SITE 3 AC1 14 GLU A 315 ARG A 333 ARG A 373 PHE A 374
SITE 4 AC1 14 ALA A 375 ALA A 385
SITE 1 AC2 11 GLU A 3 PHE A 5 GLU A 6 THR A 8
SITE 2 AC2 11 LYS A 9 TYR A 39 GLY A 40 GLU A 68
SITE 3 AC2 11 ASP A 70 HIS A 75 LYS A 263
SITE 1 AC3 20 VAL A 20 ASP A 21 HIS A 22 GLY A 23
SITE 2 AC3 20 LYS A 24 THR A 25 THR A 26 PHE A 46
SITE 3 AC3 20 ILE A 60 THR A 61 GLY A 83 HIS A 84
SITE 4 AC3 20 ASN A 135 LYS A 136 ASP A 138 MET A 139
SITE 5 AC3 20 SER A 173 ALA A 174 LEU A 175 MG A1398
SITE 1 AC4 3 THR A 25 THR A 61 GNP A1397
CRYST1 196.410 196.410 196.410 90.00 90.00 90.00 P 41 3 2 24
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 0.005091 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005091 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
