HEADER GENE REGULATION/RNA 04-DEC-98 1B23
TITLE E. COLI CYSTEINYL-TRNA AND T. AQUATICUS ELONGATION FACTOR EF-TU:GTP
TITLE 2 TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINYL TRNA;
COMPND 3 CHAIN: R;
COMPND 4 SYNONYM: CYS-TRNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: AMINOACYL LINK BETWEEN A76 AND CYS77;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ELONGATION FACTOR TU;
COMPND 9 CHAIN: P;
COMPND 10 SYNONYM: EF-TU;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS AQUATICUS;
SOURCE 6 ORGANISM_TAXID: 271;
SOURCE 7 STRAIN: YT-1;
SOURCE 8 GENE: TUFA;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSLATION ELONGATION FACTOR, TRANSFER RNA, PROTEIN SYNTHESIS, GENE
KEYWDS 2 REGULATION-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.NISSEN,M.KJELDGAARD,S.THIRUP,J.NYBORG
REVDAT 7 09-AUG-23 1B23 1 REMARK LINK
REVDAT 6 03-JUL-19 1B23 1 COMPND REMARK FORMUL LINK
REVDAT 5 16-NOV-11 1B23 1 VERSN HETATM
REVDAT 4 24-FEB-09 1B23 1 VERSN
REVDAT 3 01-APR-03 1B23 1 JRNL
REVDAT 2 22-DEC-99 1B23 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 07-DEC-98 1B23 0
JRNL AUTH P.NISSEN,S.THIRUP,M.KJELDGAARD,J.NYBORG
JRNL TITL THE CRYSTAL STRUCTURE OF CYS-TRNACYS-EF-TU-GDPNP REVEALS
JRNL TITL 2 GENERAL AND SPECIFIC FEATURES IN THE TERNARY COMPLEX AND IN
JRNL TITL 3 TRNA.
JRNL REF STRUCTURE FOLD.DES. V. 7 143 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10368282
JRNL DOI 10.1016/S0969-2126(99)80021-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.NISSEN,M.KJELDGAARD,S.THIRUP,G.POLEKHINA,L.RESHETNIKOVA,
REMARK 1 AUTH 2 B.F.C.CLARK,J.NYBORG
REMARK 1 TITL CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF PHE-TRNAPHE,
REMARK 1 TITL 2 EF-TU, AND A GTP ANALOG
REMARK 1 REF SCIENCE V. 270 1464 1995
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 18043
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) : 0.206
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1424
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1314
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE : 0.3980
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 107
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 : 3144
REMARK 3 NUCLEIC ACID ATOMS : 1584
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 261
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -31.50000
REMARK 3 B22 (A**2) : -4.00000
REMARK 3 B33 (A**2) : 14.90000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.46
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) : 0.45
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.56
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.880
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 5.410
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 1.500 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.500 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.500 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.300 ; 5.000
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : TRNA-MULTI-ENDO.PARAM
REMARK 3 PARAMETER FILE 3 : GTP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TRNA-MULTI-ENDO.TOP
REMARK 3 TOPOLOGY FILE 3 : GTP.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 ANISOTROPIC SCALING WAS CRUCIAL FOR REFINEMENT. ANISOTROPIC
REMARK 3 SCALEFACTORS DERIVED FROM 4.0 - 2.6 A AMPLITUDES
REMARK 3
REMARK 3 THE ISOPENTENYL GROUP OF MIA R 37 AND THE N-TERMINAL ALA P
REMARK 3 1 RESIDUE WERE STEREOCHEMICALLY MODELED
REMARK 4
REMARK 4 1B23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000000207.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.098
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.39600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: ANISOTROPIC DIFFRACTION
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M (NH4)2SO4, 30 MM TRIS, 5 MM MES,
REMARK 280 10 MM MGCL2, 10 MM DTT, 1 MM GDPNP PH 6.7, 4 DEG. C, HANGING
REMARK 280 DROP, VAPOR DIFFUSION - HANGING DROP, TEMPERATURE 277K, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 66.49000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 77.44000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.49000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.44000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.49000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.44000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.49000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.44000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 77.44000
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 77.44000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 77.44000
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 77.44000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 66.49000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 66.49000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 66.49000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 63.37500
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 66.49000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, P
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG R 179 LIES ON A SPECIAL POSITION.
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MIA R 37 C12 C13 C14 C15 C16
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 N4 C R 72 O4 U R 73 1.57
REMARK 500 N4 C R 75 OG1 THR P 232 1.70
REMARK 500 N4 C R 72 C4 U R 73 1.77
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 G R 1 P G R 1 OP3 -0.085
REMARK 500 U R 7 C1' U R 7 N1 -0.238
REMARK 500 A R 22 N9 A R 22 C4 -0.065
REMARK 500 C R 72 C1' C R 72 N1 0.200
REMARK 500 C R 75 O5' C R 75 C5' 0.256
REMARK 500 C R 75 C1' C R 75 N1 0.360
REMARK 500 ALA P 1 C LYS P 2 N -0.173
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 U R 7 N1 - C1' - C2' ANGL. DEV. = 23.4 DEGREES
REMARK 500 U R 7 C6 - N1 - C1' ANGL. DEV. = -22.9 DEGREES
REMARK 500 U R 7 C2 - N1 - C1' ANGL. DEV. = 22.3 DEGREES
REMARK 500 A R 22 C8 - N9 - C4 ANGL. DEV. = 2.7 DEGREES
REMARK 500 C R 72 N1 - C1' - C2' ANGL. DEV. = -7.3 DEGREES
REMARK 500 C R 75 O5' - C5' - C4' ANGL. DEV. = -43.9 DEGREES
REMARK 500 C R 75 P - O5' - C5' ANGL. DEV. = -31.6 DEGREES
REMARK 500 C R 75 C4' - C3' - O3' ANGL. DEV. = 38.1 DEGREES
REMARK 500 C R 75 C2' - C3' - O3' ANGL. DEV. = -22.6 DEGREES
REMARK 500 C R 75 O4' - C1' - N1 ANGL. DEV. = 19.7 DEGREES
REMARK 500 C R 75 C2 - N1 - C1' ANGL. DEV. = 7.1 DEGREES
REMARK 500 C R 75 C3' - O3' - P ANGL. DEV. = 11.7 DEGREES
REMARK 500 LYS P 2 C - N - CA ANGL. DEV. = 38.9 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 LYS P 2 -60.00 140.11
REMARK 500 ILE P 50 -70.99 -83.03
REMARK 500 THR P 72 -162.35 -100.06
REMARK 500 ASP P 216 45.80 -85.86
REMARK 500 LEU P 222 119.43 -165.12
REMARK 500 ALA P 259 141.93 177.35
REMARK 500 HIS P 273 70.06 55.87
REMARK 500 ARG P 274 10.92 56.37
REMARK 500 GLN P 302 -168.56 -75.44
REMARK 500 THR P 314 -41.37 -131.24
REMARK 500 PHE P 316 150.09 177.67
REMARK 500 ARG P 339 78.11 -117.40
REMARK 500 ARG P 345 -117.68 54.24
REMARK 500 ALA P 379 109.84 -54.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA P 1 LYS P 2 96.61
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 C R 72 0.06 SIDE CHAIN
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 R 77 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A R 76 O5'
REMARK 620 2 A R 76 OP2 52.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG P 407 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR P 25 OG1
REMARK 620 2 THR P 62 OG1 80.9
REMARK 620 3 GNP P 406 O2B 80.4 145.4
REMARK 620 4 GNP P 406 N3B 120.1 116.2 52.5
REMARK 620 5 GNP P 406 O3G 162.3 88.0 101.9 53.4
REMARK 620 6 HOH P 410 O 88.2 109.4 98.8 128.7 108.6
REMARK 620 7 HOH P 419 O 74.6 69.3 77.8 62.4 88.6 162.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 P 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 77
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS R 976
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP P 406
DBREF 1B23 P 1 405 UNP Q01698 EFTU_THEAQ 1 405
DBREF 1B23 R 1 76 PDB 1B23 1B23 1 76
SEQRES 1 R 74 G G C G C G U 4SU A A C A A
SEQRES 2 R 74 A G C G G H2U H2U A U G U A G
SEQRES 3 R 74 C G G A PSU U G C A MIA A PSU C
SEQRES 4 R 74 C G U C U A G U C C G G 5MU
SEQRES 5 R 74 PSU C G A C U C C G G A A C
SEQRES 6 R 74 G C G C C U C C A
SEQRES 1 P 405 ALA LYS GLY GLU PHE ILE ARG THR LYS PRO HIS VAL ASN
SEQRES 2 P 405 VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR
SEQRES 3 P 405 LEU THR ALA ALA LEU THR TYR VAL ALA ALA ALA GLU ASN
SEQRES 4 P 405 PRO ASN VAL GLU VAL LYS ASP TYR GLY ASP ILE ASP LYS
SEQRES 5 P 405 ALA PRO GLU GLU ARG ALA ARG GLY ILE THR ILE ASN THR
SEQRES 6 P 405 ALA HIS VAL GLU TYR GLU THR ALA LYS ARG HIS TYR SER
SEQRES 7 P 405 HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR ILE LYS ASN
SEQRES 8 P 405 MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU
SEQRES 9 P 405 VAL VAL SER ALA ALA ASP GLY PRO MET PRO GLN THR ARG
SEQRES 10 P 405 GLU HIS ILE LEU LEU ALA ARG GLN VAL GLY VAL PRO TYR
SEQRES 11 P 405 ILE VAL VAL PHE MET ASN LYS VAL ASP MET VAL ASP ASP
SEQRES 12 P 405 PRO GLU LEU LEU ASP LEU VAL GLU MET GLU VAL ARG ASP
SEQRES 13 P 405 LEU LEU ASN GLN TYR GLU PHE PRO GLY ASP GLU VAL PRO
SEQRES 14 P 405 VAL ILE ARG GLY SER ALA LEU LEU ALA LEU GLU GLU MET
SEQRES 15 P 405 HIS LYS ASN PRO LYS THR LYS ARG GLY GLU ASN GLU TRP
SEQRES 16 P 405 VAL ASP LYS ILE TRP GLU LEU LEU ASP ALA ILE ASP GLU
SEQRES 17 P 405 TYR ILE PRO THR PRO VAL ARG ASP VAL ASP LYS PRO PHE
SEQRES 18 P 405 LEU MET PRO VAL GLU ASP VAL PHE THR ILE THR GLY ARG
SEQRES 19 P 405 GLY THR VAL ALA THR GLY ARG ILE GLU ARG GLY LYS VAL
SEQRES 20 P 405 LYS VAL GLY ASP GLU VAL GLU ILE VAL GLY LEU ALA PRO
SEQRES 21 P 405 GLU THR ARG LYS THR VAL VAL THR GLY VAL GLU MET HIS
SEQRES 22 P 405 ARG LYS THR LEU GLN GLU GLY ILE ALA GLY ASP ASN VAL
SEQRES 23 P 405 GLY LEU LEU LEU ARG GLY VAL SER ARG GLU GLU VAL GLU
SEQRES 24 P 405 ARG GLY GLN VAL LEU ALA LYS PRO GLY SER ILE THR PRO
SEQRES 25 P 405 HIS THR LYS PHE GLU ALA SER VAL TYR ILE LEU LYS LYS
SEQRES 26 P 405 GLU GLU GLY GLY ARG HIS THR GLY PHE PHE THR GLY TYR
SEQRES 27 P 405 ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY
SEQRES 28 P 405 VAL VAL ARG LEU PRO GLN GLY VAL GLU MET VAL MET PRO
SEQRES 29 P 405 GLY ASP ASN VAL THR PHE THR VAL GLU LEU ILE LYS PRO
SEQRES 30 P 405 VAL ALA LEU GLU GLU GLY LEU ARG PHE ALA ILE ARG GLU
SEQRES 31 P 405 GLY GLY ARG THR VAL GLY ALA GLY VAL VAL THR LYS ILE
SEQRES 32 P 405 LEU GLU
MODRES 1B23 4SU R 8 U 4-THIOURIDINE-5'-MONOPHOSPHATE
MODRES 1B23 H2U R 20 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1B23 H2U R 21 U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
MODRES 1B23 PSU R 32 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1B23 MIA R 37 A
MODRES 1B23 PSU R 39 U PSEUDOURIDINE-5'-MONOPHOSPHATE
MODRES 1B23 5MU R 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 1B23 PSU R 55 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET 4SU R 8 20
HET H2U R 20 20
HET H2U R 21 20
HET PSU R 32 20
HET MIA R 37 29
HET PSU R 39 20
HET 5MU R 54 21
HET PSU R 55 20
HET MG R 77 1
HET MG R 179 1
HET CYS R 976 6
HET MG P 407 1
HET SO4 P 408 5
HET SO4 P 409 5
HET GNP P 406 32
HETNAM 4SU 4-THIOURIDINE-5'-MONOPHOSPHATE
HETNAM H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM MIA 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM CYS CYSTEINE
HETNAM SO4 SULFATE ION
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
FORMUL 1 4SU C9 H13 N2 O8 P S
FORMUL 1 H2U 2(C9 H15 N2 O9 P)
FORMUL 1 PSU 3(C9 H13 N2 O9 P)
FORMUL 1 MIA C16 H24 N5 O7 P S
FORMUL 1 5MU C10 H15 N2 O9 P
FORMUL 3 MG 3(MG 2+)
FORMUL 5 CYS C3 H7 N O2 S
FORMUL 7 SO4 2(O4 S 2-)
FORMUL 9 GNP C10 H17 N6 O13 P3
FORMUL 10 HOH *261(H2 O)
HELIX 1 1 LYS P 24 GLU P 38 1 15
HELIX 2 2 TYR P 47 ILE P 50 1 4
HELIX 3 3 PRO P 54 ARG P 59 1 6
HELIX 4 4 ALA P 86 GLN P 98 5 13
HELIX 5 5 PRO P 114 VAL P 126 1 13
HELIX 6 6 VAL P 138 MET P 140 5 3
HELIX 7 7 PRO P 144 TYR P 161 1 18
HELIX 8 8 ALA P 175 LYS P 184 1 10
HELIX 9 9 GLU P 194 TYR P 209 1 16
HELIX 10 10 LYS P 325 GLU P 327 5 3
SHEET 1 A 6 VAL P 170 ARG P 172 0
SHEET 2 A 6 TYR P 130 ASN P 136 1 N VAL P 133 O ILE P 171
SHEET 3 A 6 GLY P 101 SER P 107 1 N ALA P 102 O TYR P 130
SHEET 4 A 6 PRO P 10 ILE P 17 1 N GLY P 15 O GLY P 101
SHEET 5 A 6 ARG P 75 ASP P 81 1 N HIS P 76 O PRO P 10
SHEET 6 A 6 ALA P 66 GLU P 71 -1 N TYR P 70 O TYR P 77
SHEET 1 B 4 LEU P 222 PRO P 224 0
SHEET 2 B 4 VAL P 303 LYS P 306 -1 N LEU P 304 O MET P 223
SHEET 3 B 4 GLU P 252 VAL P 256 -1 N VAL P 256 O VAL P 303
SHEET 4 B 4 LYS P 264 VAL P 266 -1 N THR P 265 O VAL P 253
SHEET 1 C 4 ASP P 227 ILE P 231 0
SHEET 2 C 4 GLY P 235 ARG P 241 -1 N THR P 239 O ASP P 227
SHEET 3 C 4 ASN P 285 LEU P 290 -1 N LEU P 290 O THR P 236
SHEET 4 C 4 VAL P 267 VAL P 270 -1 N GLY P 269 O LEU P 289
SHEET 1 D 2 LYS P 246 LYS P 248 0
SHEET 2 D 2 GLU P 279 ILE P 281 -1 N GLY P 280 O VAL P 247
SHEET 1 E 7 GLY P 351 ARG P 354 0
SHEET 2 E 7 ASN P 367 LEU P 374 -1 N GLU P 373 O VAL P 352
SHEET 3 E 7 LYS P 315 ILE P 322 -1 N VAL P 320 O VAL P 368
SHEET 4 E 7 ARG P 393 LYS P 402 -1 N LYS P 402 O GLU P 317
SHEET 5 E 7 ARG P 385 GLU P 390 -1 N GLU P 390 O ARG P 393
SHEET 6 E 7 GLN P 341 PHE P 344 -1 N TYR P 343 O ALA P 387
SHEET 7 E 7 THR P 347 THR P 350 -1 N VAL P 349 O PHE P 342
LINK O3' U R 7 P 4SU R 8 1555 1555 1.61
LINK O3' 4SU R 8 P A R 9 1555 1555 1.61
LINK O3' G R 19 P H2U R 20 1555 1555 1.60
LINK O3' H2U R 20 P H2U R 21 1555 1555 1.61
LINK O3' H2U R 21 P A R 22 1555 1555 1.60
LINK O3' A R 31 P PSU R 32 1555 1555 1.60
LINK O3' PSU R 32 P U R 33 1555 1555 1.61
LINK O3' A R 36 P MIA R 37 1555 1555 1.61
LINK O3' MIA R 37 P A R 38 1555 1555 1.61
LINK O3' A R 38 P PSU R 39 1555 1555 1.62
LINK O3' PSU R 39 P C R 40 1555 1555 1.61
LINK O3' G R 53 P 5MU R 54 1555 1555 1.60
LINK O3' 5MU R 54 P PSU R 55 1555 1555 1.61
LINK O3' PSU R 55 P C R 56 1555 1555 1.61
LINK O3' A R 76 C CYS R 976 1555 1555 1.31
LINK O5' A R 76 MG MG R 77 1555 1555 3.08
LINK OP2 A R 76 MG MG R 77 1555 1555 1.63
LINK OG1 THR P 25 MG MG P 407 1555 1555 2.13
LINK OG1 THR P 62 MG MG P 407 1555 1555 2.25
LINK O2B GNP P 406 MG MG P 407 1555 1555 1.96
LINK N3B GNP P 406 MG MG P 407 1555 1555 3.15
LINK O3G GNP P 406 MG MG P 407 1555 1555 2.08
LINK MG MG P 407 O HOH P 410 1555 1555 1.94
LINK MG MG P 407 O HOH P 419 1555 1555 2.60
SITE 1 AC1 5 THR P 25 THR P 62 GNP P 406 HOH P 410
SITE 2 AC1 5 HOH P 419
SITE 1 AC2 6 ARG P 339 VAL P 352 ARG P 354 HOH P 442
SITE 2 AC2 6 HOH P 463 HOH P 548
SITE 1 AC3 4 MET P 113 PRO P 114 ARG P 117 HOH P 423
SITE 1 AC4 2 C R 75 A R 76
SITE 1 AC5 1 G R 70
SITE 1 AC6 6 HIS P 67 HIS P 273 ARG P 274 ASN P 285
SITE 2 AC6 6 VAL P 286 A R 76
SITE 1 AC7 22 VAL P 20 ASP P 21 HIS P 22 GLY P 23
SITE 2 AC7 22 LYS P 24 THR P 25 THR P 26 TYR P 47
SITE 3 AC7 22 ILE P 61 THR P 62 GLY P 84 ASN P 136
SITE 4 AC7 22 LYS P 137 ASP P 139 MET P 140 SER P 174
SITE 5 AC7 22 ALA P 175 LEU P 176 MG P 407 HOH P 410
SITE 6 AC7 22 HOH P 419 HOH P 524
CRYST1 126.750 132.980 154.880 90.00 90.00 90.00 F 2 2 2 16
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 0.007889 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
