HEADER COMPLEX (LIGASE/TRNA) 15-SEP-93 1GTR
TITLE STRUCTURAL BASIS OF ANTICODON LOOP RECOGNITION BY GLUTAMINYL-TRNA
TITLE 2 SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA (74-MER);
COMPND 3 CHAIN: B;
COMPND 4 EC: 6.1.1.18;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: GLUTAMINYL-TRNA SYNTHETASE;
COMPND 8 CHAIN: A;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 5 ORGANISM_TAXID: 562
KEYWDS COMPLEX (LIGASE-TRNA), COMPLEX (LIGASE-TRNA) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.ROULD,J.J.PERONA,T.A.STEITZ
REVDAT 3 16-NOV-11 1GTR 1 VERSN HETATM
REVDAT 2 24-FEB-09 1GTR 1 VERSN
REVDAT 1 07-FEB-95 1GTR 0
JRNL AUTH M.A.ROULD,J.J.PERONA,T.A.STEITZ
JRNL TITL STRUCTURAL BASIS OF ANTICODON LOOP RECOGNITION BY
JRNL TITL 2 GLUTAMINYL-TRNA SYNTHETASE.
JRNL REF NATURE V. 352 213 1991
JRNL REFN ISSN 0028-0836
JRNL PMID 1857417
JRNL DOI 10.1038/352213A0
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 4279
REMARK 3 NUCLEIC ACID ATOMS : 1573
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 231
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 3.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GTR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37820
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 57.90000
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 57.90000
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 121.40000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.15000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 121.40000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.15000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 57.90000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 121.40000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.15000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.90000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 121.40000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.15000
REMARK 290 SMTRY3 8 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: B, 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 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 HOH A 573 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 720 LIES ON A SPECIAL POSITION.
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 SER A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 5
REMARK 465 ARG A 6
REMARK 465 PRO A 7
REMARK 465 SER A 443
REMARK 465 LYS A 444
REMARK 465 ASP A 445
REMARK 465 PRO A 446
REMARK 465 ALA A 447
REMARK 465 ASP A 448
REMARK 465 GLY A 449
REMARK 465 ARG A 450
REMARK 465 LYS A 451
REMARK 465 VAL A 452
REMARK 465 LYS A 453
REMARK 465 TRP A 548
REMARK 465 ALA A 549
REMARK 465 LYS A 550
REMARK 465 VAL A 551
REMARK 465 GLY A 552
REMARK 465 GLU A 553
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 HIS A 24 NE2 HIS A 24 CD2 -0.071
REMARK 500 HIS A 28 NE2 HIS A 28 CD2 -0.071
REMARK 500 HIS A 40 NE2 HIS A 40 CD2 -0.070
REMARK 500 HIS A 43 NE2 HIS A 43 CD2 -0.069
REMARK 500 HIS A 107 NE2 HIS A 107 CD2 -0.068
REMARK 500 HIS A 198 NE2 HIS A 198 CD2 -0.076
REMARK 500 HIS A 215 NE2 HIS A 215 CD2 -0.071
REMARK 500 HIS A 226 NE2 HIS A 226 CD2 -0.071
REMARK 500 HIS A 252 NE2 HIS A 252 CD2 -0.078
REMARK 500 HIS A 281 NE2 HIS A 281 CD2 -0.071
REMARK 500 HIS A 368 NE2 HIS A 368 CD2 -0.072
REMARK 500 HIS A 457 NE2 HIS A 457 CD2 -0.072
REMARK 500 HIS A 463 NE2 HIS A 463 CD2 -0.067
REMARK 500 HIS A 530 NE2 HIS A 530 CD2 -0.070
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 B 5 O3' - P - OP2 ANGL. DEV. = 14.3 DEGREES
REMARK 500 G B 5 O3' - P - OP1 ANGL. DEV. = -14.3 DEGREES
REMARK 500 U B 8 O4' - C1' - N1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 U B 8 O3' - P - OP2 ANGL. DEV. = 28.3 DEGREES
REMARK 500 U B 8 O3' - P - OP1 ANGL. DEV. = -25.6 DEGREES
REMARK 500 C B 9 O3' - P - OP2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 C B 9 O3' - P - OP1 ANGL. DEV. = -17.0 DEGREES
REMARK 500 C B 12 C4' - C3' - C2' ANGL. DEV. = -7.2 DEGREES
REMARK 500 C B 12 O3' - P - OP2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 C B 12 O3' - P - OP1 ANGL. DEV. = -20.1 DEGREES
REMARK 500 A B 13 O3' - P - O5' ANGL. DEV. = 13.2 DEGREES
REMARK 500 A B 14 C1' - O4' - C4' ANGL. DEV. = -4.8 DEGREES
REMARK 500 A B 14 O3' - P - O5' ANGL. DEV. = 18.9 DEGREES
REMARK 500 A B 14 O3' - P - OP1 ANGL. DEV. = -15.6 DEGREES
REMARK 500 G B 15 O4' - C1' - N9 ANGL. DEV. = 6.8 DEGREES
REMARK 500 C B 16 N1 - C2 - O2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 G B 15 C3' - O3' - P ANGL. DEV. = 11.0 DEGREES
REMARK 500 C B 16 O3' - P - O5' ANGL. DEV. = -25.9 DEGREES
REMARK 500 C B 16 O3' - P - OP2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 C B 16 O3' - P - OP1 ANGL. DEV. = 33.6 DEGREES
REMARK 500 C B 16 C3' - O3' - P ANGL. DEV. = 8.2 DEGREES
REMARK 500 G B 18 O3' - P - OP2 ANGL. DEV. = 24.1 DEGREES
REMARK 500 G B 18 O3' - P - OP1 ANGL. DEV. = -27.0 DEGREES
REMARK 500 U B 20 C3' - O3' - P ANGL. DEV. = 12.1 DEGREES
REMARK 500 A B 21 O3' - P - O5' ANGL. DEV. = -21.3 DEGREES
REMARK 500 A B 21 O3' - P - OP2 ANGL. DEV. = 37.2 DEGREES
REMARK 500 A B 21 O3' - P - OP1 ANGL. DEV. = -22.0 DEGREES
REMARK 500 A B 22 O3' - P - O5' ANGL. DEV. = 21.7 DEGREES
REMARK 500 A B 22 O3' - P - OP1 ANGL. DEV. = -30.2 DEGREES
REMARK 500 G B 23 O3' - P - OP2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 C B 25 O3' - P - OP1 ANGL. DEV. = -14.7 DEGREES
REMARK 500 C B 28 O3' - P - OP2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 C B 28 O3' - P - OP1 ANGL. DEV. = -19.5 DEGREES
REMARK 500 G B 29 C5' - C4' - C3' ANGL. DEV. = -8.6 DEGREES
REMARK 500 G B 29 O3' - P - OP1 ANGL. DEV. = -18.1 DEGREES
REMARK 500 G B 30 C1' - O4' - C4' ANGL. DEV. = -5.3 DEGREES
REMARK 500 G B 30 O4' - C1' - N9 ANGL. DEV. = 6.2 DEGREES
REMARK 500 G B 30 O3' - P - O5' ANGL. DEV. = 18.2 DEGREES
REMARK 500 G B 30 O3' - P - OP2 ANGL. DEV. = 11.9 DEGREES
REMARK 500 G B 30 O3' - P - OP1 ANGL. DEV. = -30.1 DEGREES
REMARK 500 U B 32 C5' - C4' - O4' ANGL. DEV. = 6.5 DEGREES
REMARK 500 U B 32 N1 - C1' - C2' ANGL. DEV. = -7.4 DEGREES
REMARK 500 U B 32 O4' - C1' - N1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 U B 32 O3' - P - O5' ANGL. DEV. = -36.6 DEGREES
REMARK 500 U B 32 O3' - P - OP2 ANGL. DEV. = 45.2 DEGREES
REMARK 500 U B 32 O3' - P - OP1 ANGL. DEV. = -23.6 DEGREES
REMARK 500 U B 33 O3' - P - O5' ANGL. DEV. = 16.6 DEGREES
REMARK 500 U B 33 O3' - P - OP2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 U B 33 O3' - P - OP1 ANGL. DEV. = -29.3 DEGREES
REMARK 500 C B 34 O3' - P - O5' ANGL. DEV. = 16.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 140 ANGLE DEVIATIONS.
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 PRO A 32 74.28 -114.47
REMARK 500 THR A 135 -167.43 -127.08
REMARK 500 ILE A 176 -98.64 -111.42
REMARK 500 ASN A 397 -176.14 -68.80
REMARK 500 ALA A 414 -132.18 -133.16
REMARK 500 GLU A 420 -50.11 -130.65
REMARK 500 ASP A 425 -53.32 -122.73
REMARK 500 ALA A 426 -40.74 173.13
REMARK 500 THR A 441 46.74 -165.86
REMARK 500 GLU A 521 -55.56 -121.80
REMARK 500 ARG A 529 -38.98 -170.46
REMARK 500 THR A 532 -157.46 -118.72
REMARK 500 LYS A 535 107.18 -168.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 999
DBREF 1GTR A 1 553 UNP P00962 SYQ_ECOLI 1 553
DBREF 1GTR B 2 76 PDB 1GTR 1GTR 2 76
SEQRES 1 B 74 G G G G U A U C G C C A A
SEQRES 2 B 74 G C G G U A A G G C A C C
SEQRES 3 B 74 G G A U U C U G A U U C C
SEQRES 4 B 74 G G C A U U C C G A G G U
SEQRES 5 B 74 U C G A A U C C U C G U A
SEQRES 6 B 74 C C C C A G C C A
SEQRES 1 A 553 SER GLU ALA GLU ALA ARG PRO THR ASN PHE ILE ARG GLN
SEQRES 2 A 553 ILE ILE ASP GLU ASP LEU ALA SER GLY LYS HIS THR THR
SEQRES 3 A 553 VAL HIS THR ARG PHE PRO PRO GLU PRO ASN GLY TYR LEU
SEQRES 4 A 553 HIS ILE GLY HIS ALA LYS SER ILE CYS LEU ASN PHE GLY
SEQRES 5 A 553 ILE ALA GLN ASP TYR LYS GLY GLN CYS ASN LEU ARG PHE
SEQRES 6 A 553 ASP ASP THR ASN PRO VAL LYS GLU ASP ILE GLU TYR VAL
SEQRES 7 A 553 GLU SER ILE LYS ASN ASP VAL GLU TRP LEU GLY PHE HIS
SEQRES 8 A 553 TRP SER GLY ASN VAL ARG TYR SER SER ASP TYR PHE ASP
SEQRES 9 A 553 GLN LEU HIS ALA TYR ALA ILE GLU LEU ILE ASN LYS GLY
SEQRES 10 A 553 LEU ALA TYR VAL ASP GLU LEU THR PRO GLU GLN ILE ARG
SEQRES 11 A 553 GLU TYR ARG GLY THR LEU THR GLN PRO GLY LYS ASN SER
SEQRES 12 A 553 PRO TYR ARG ASP ARG SER VAL GLU GLU ASN LEU ALA LEU
SEQRES 13 A 553 PHE GLU LYS MET ARG ALA GLY GLY PHE GLU GLU GLY LYS
SEQRES 14 A 553 ALA CYS LEU ARG ALA LYS ILE ASP MET ALA SER PRO PHE
SEQRES 15 A 553 ILE VAL MET ARG ASP PRO VAL LEU TYR ARG ILE LYS PHE
SEQRES 16 A 553 ALA GLU HIS HIS GLN THR GLY ASN LYS TRP CYS ILE TYR
SEQRES 17 A 553 PRO MET TYR ASP PHE THR HIS CYS ILE SER ASP ALA LEU
SEQRES 18 A 553 GLU GLY ILE THR HIS SER LEU CYS THR LEU GLU PHE GLN
SEQRES 19 A 553 ASP ASN ARG ARG LEU TYR ASP TRP VAL LEU ASP ASN ILE
SEQRES 20 A 553 THR ILE PRO VAL HIS PRO ARG GLN TYR GLU PHE SER ARG
SEQRES 21 A 553 LEU ASN LEU GLU TYR THR VAL MET SER LYS ARG LYS LEU
SEQRES 22 A 553 ASN LEU LEU VAL THR ASP LYS HIS VAL GLU GLY TRP ASP
SEQRES 23 A 553 ASP PRO ARG MET PRO THR ILE SER GLY LEU ARG ARG ARG
SEQRES 24 A 553 GLY TYR THR ALA ALA SER ILE ARG GLU PHE CYS LYS ARG
SEQRES 25 A 553 ILE GLY VAL THR LYS GLN ASP ASN THR ILE GLU MET ALA
SEQRES 26 A 553 SER LEU GLU SER CYS ILE ARG GLU ASP LEU ASN GLU ASN
SEQRES 27 A 553 ALA PRO ARG ALA MET ALA VAL ILE ASP PRO VAL LYS LEU
SEQRES 28 A 553 VAL ILE GLU ASN TYR GLN GLY GLU GLY GLU MET VAL THR
SEQRES 29 A 553 MET PRO ASN HIS PRO ASN LYS PRO GLU MET GLY SER ARG
SEQRES 30 A 553 GLN VAL PRO PHE SER GLY GLU ILE TRP ILE ASP ARG ALA
SEQRES 31 A 553 ASP PHE ARG GLU GLU ALA ASN LYS GLN TYR LYS ARG LEU
SEQRES 32 A 553 VAL LEU GLY LYS GLU VAL ARG LEU ARG ASN ALA TYR VAL
SEQRES 33 A 553 ILE LYS ALA GLU ARG VAL GLU LYS ASP ALA GLU GLY ASN
SEQRES 34 A 553 ILE THR THR ILE PHE CYS THR TYR ASP ALA ASP THR LEU
SEQRES 35 A 553 SER LYS ASP PRO ALA ASP GLY ARG LYS VAL LYS GLY VAL
SEQRES 36 A 553 ILE HIS TRP VAL SER ALA ALA HIS ALA LEU PRO VAL GLU
SEQRES 37 A 553 ILE ARG LEU TYR ASP ARG LEU PHE SER VAL PRO ASN PRO
SEQRES 38 A 553 GLY ALA ALA ASP ASP PHE LEU SER VAL ILE ASN PRO GLU
SEQRES 39 A 553 SER LEU VAL ILE LYS GLN GLY PHE ALA GLU PRO SER LEU
SEQRES 40 A 553 LYS ASP ALA VAL ALA GLY LYS ALA PHE GLN PHE GLU ARG
SEQRES 41 A 553 GLU GLY TYR PHE CYS LEU ASP SER ARG HIS SER THR ALA
SEQRES 42 A 553 GLU LYS PRO VAL PHE ASN ARG THR VAL GLY LEU ARG ASP
SEQRES 43 A 553 THR TRP ALA LYS VAL GLY GLU
HET ATP A 999 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 HOH *231(H2 O)
HELIX 1 1 PHE A 10 SER A 21 1 12
HELIX 2 2 ILE A 41 ASP A 56 1 16
HELIX 3 3 PRO A 70 LYS A 72 5 3
HELIX 4 4 ILE A 75 TRP A 87 1 13
HELIX 5 5 SER A 99 ASN A 115 5 17
HELIX 6 6 PRO A 126 ARG A 133 1 8
HELIX 7 7 VAL A 150 ALA A 162 1 13
HELIX 8 8 ILE A 183 MET A 185 5 3
HELIX 9 9 TYR A 211 GLU A 222 1 12
HELIX 10 10 LEU A 231 PHE A 233 5 3
HELIX 11 11 ASN A 236 ASN A 246 5 11
HELIX 12 12 LYS A 270 THR A 278 1 9
HELIX 13 13 ILE A 293 ARG A 299 1 7
HELIX 14 14 ALA A 303 ILE A 313 1 11
HELIX 15 15 MET A 324 ASN A 338 1 15
HELIX 16 16 PRO A 372 MET A 374 5 3
HELIX 17 17 ARG A 389 ASP A 391 5 3
HELIX 18 18 PRO A 481 ALA A 483 5 3
HELIX 19 19 LEU A 488 VAL A 490 5 3
HELIX 20 20 PRO A 505 ASP A 509 5 5
SHEET 1 A 2 HIS A 28 PHE A 31 0
SHEET 2 A 2 GLN A 60 LEU A 63 1 N GLN A 60 O THR A 29
SHEET 1 B 4 ALA A 119 ASP A 122 0
SHEET 2 B 4 CYS A 171 ALA A 174 -1 N ARG A 173 O TYR A 120
SHEET 3 B 4 VAL A 189 ILE A 193 -1 N TYR A 191 O LEU A 172
SHEET 4 B 4 ILE A 207 PRO A 209 -1 N TYR A 208 O ARG A 192
SHEET 1 C 2 HIS A 226 THR A 230 0
SHEET 2 C 2 ARG A 254 PHE A 258 1 N ARG A 254 O SER A 227
SHEET 1 D 6 PRO A 340 ALA A 342 0
SHEET 2 D 6 ALA A 515 PHE A 518 1 N GLN A 517 O PRO A 340
SHEET 3 D 6 GLY A 522 LEU A 526 -1 N PHE A 524 O PHE A 516
SHEET 4 D 6 PRO A 536 GLY A 543 -1 N VAL A 542 O TYR A 523
SHEET 5 D 6 LEU A 465 TYR A 472 1 N GLU A 468 O PRO A 536
SHEET 6 D 6 LEU A 496 ALA A 503 -1 N ALA A 503 O LEU A 465
SHEET 1 E 4 GLU A 384 ASP A 388 0
SHEET 2 E 4 PRO A 348 ILE A 353 -1 N LEU A 351 O ILE A 385
SHEET 3 E 4 THR A 432 CYS A 435 1 N ILE A 433 O LYS A 350
SHEET 4 E 4 ALA A 419 GLU A 423 -1 N GLU A 423 O THR A 432
SHEET 1 F 2 GLU A 361 PRO A 366 0
SHEET 2 F 2 SER A 376 PHE A 381 -1 N PHE A 381 O GLU A 361
SHEET 1 G 2 GLU A 408 ARG A 410 0
SHEET 2 G 2 VAL A 416 LYS A 418 -1 N ILE A 417 O VAL A 409
SITE 1 AC1 16 PHE A 31 PRO A 33 GLU A 34 ASN A 36
SITE 2 AC1 16 GLY A 42 HIS A 43 THR A 230 ARG A 260
SITE 3 AC1 16 LEU A 261 LYS A 270 HOH A 602 HOH A 619
SITE 4 AC1 16 HOH A 628 HOH A 784 A B 76 HOH B 792
CRYST1 242.800 94.300 115.800 90.00 90.00 90.00 C 2 2 21 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 0.004119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010604 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008636 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
