HEADER LIGASE/RNA 29-FEB-00 1EIY
TITLE THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS
TITLE 2 THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA(PHE);
COMPND 3 CHAIN: C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: PHENYLALANYL-TRNA SYNTHETASE;
COMPND 6 CHAIN: A;
COMPND 7 FRAGMENT: ALPHA CHAIN;
COMPND 8 SYNONYM: PHENYLALANINE--TRNA LIGASE ALPHA CHAIN, PHERS;
COMPND 9 EC: 6.1.1.20;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: PHENYLALANYL-TRNA SYNTHETASE;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: BETA CHAIN;
COMPND 14 SYNONYM: PHENYLALANINE--TRNA LIGASE BETA CHAIN, PHERS;
COMPND 15 EC: 6.1.1.20
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 7 ORGANISM_TAXID: 300852;
SOURCE 8 STRAIN: HB8;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 11 ORGANISM_TAXID: 300852;
SOURCE 12 STRAIN: HB8
KEYWDS AMINOACYL-TRNA SYNTHETASE, TRNA RECOGNITION, LIGASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.GOLDGUR,L.MOSYAK,L.RESHETNIKOVA,V.ANKILOVA,M.SAFRO
REVDAT 10 07-FEB-24 1EIY 1 SEQADV
REVDAT 9 04-OCT-17 1EIY 1 REMARK
REVDAT 8 13-JUL-11 1EIY 1 VERSN
REVDAT 7 24-FEB-09 1EIY 1 VERSN
REVDAT 6 01-APR-03 1EIY 1 JRNL
REVDAT 5 14-DEC-01 1EIY 1 REMARK
REVDAT 4 14-MAR-01 1EIY 1 JRNL DBREF REMARK
REVDAT 3 26-JUN-00 1EIY 1 SOURCE
REVDAT 2 17-APR-00 1EIY 1 HEADER
REVDAT 1 06-MAR-00 1EIY 0
JRNL AUTH Y.GOLDGUR,L.MOSYAK,L.RESHETNIKOVA,V.ANKILOVA,O.LAVRIK,
JRNL AUTH 2 S.KHODYREVA,M.SAFRO
JRNL TITL THE CRYSTAL STRUCTURE OF PHENYLALANYL-TRNA SYNTHETASE FROM
JRNL TITL 2 THERMUS THERMOPHILUS COMPLEXED WITH COGNATE TRNAPHE.
JRNL REF STRUCTURE V. 5 59 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9016717
JRNL DOI 10.1016/S0969-2126(97)00166-4
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 33340
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) : 0.221
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1667
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 : 8862
REMARK 3 NUCLEIC ACID ATOMS : 1623
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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) : 0.025
REMARK 3 BOND ANGLES (DEGREES) : 2.300
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 1EIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010620.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-92; 10-OCT-93
REMARK 200 TEMPERATURE (KELVIN) : 293; 293
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 4
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N; Y
REMARK 200 RADIATION SOURCE : ROTATING ANODE; LURE
REMARK 200 BEAMLINE : NULL; D41A
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418; 0.9900
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : XENTRONICS; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : X-GEN
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33340
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.15800
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) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; 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 (%): 70.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, MAGNESIUM SULPHATE,
REMARK 280 PH 7.2, VAPOR DIFFUSION, HANGING DROP AT 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.73333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.86667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.86667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 93.73333
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 5
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 6 CG CD1 CD2
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 GLU A 109 CB GLU A 109 CG -0.124
REMARK 500 MET B 239 SD MET B 239 CE 0.341
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 C 20 C2' - C3' - O3' ANGL. DEV. = 12.3 DEGREES
REMARK 500 C C 62 N1 - C1' - C2' ANGL. DEV. = -8.1 DEGREES
REMARK 500 U C 68 N1 - C1' - C2' ANGL. DEV. = -7.0 DEGREES
REMARK 500 G C 71 N9 - C1' - C2' ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU A 39 CA - CB - CG ANGL. DEV. = 18.4 DEGREES
REMARK 500 PRO A 164 C - N - CA ANGL. DEV. = 14.9 DEGREES
REMARK 500 PRO A 164 C - N - CD ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 PRO A 247 C - N - CA ANGL. DEV. = 14.7 DEGREES
REMARK 500 PRO A 288 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU A 317 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 PRO A 330 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 LEU A 350 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG B 2 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 PRO B 57 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO B 97 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO B 162 C - N - CA ANGL. DEV. = 12.9 DEGREES
REMARK 500 PRO B 225 C - N - CA ANGL. DEV. = -10.1 DEGREES
REMARK 500 PRO B 310 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 340 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 LEU B 548 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 LEU B 603 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU B 609 CA - CB - CG ANGL. DEV. = 17.1 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 ALA A 41 65.22 -113.93
REMARK 500 GLU A 45 46.31 -104.87
REMARK 500 ARG A 48 -70.64 95.15
REMARK 500 GLN A 52 -70.75 -76.29
REMARK 500 LEU A 54 -108.88 -94.05
REMARK 500 ASN A 55 -53.34 -27.70
REMARK 500 LEU A 61 13.01 -68.57
REMARK 500 GLU A 62 -51.43 -135.40
REMARK 500 ARG A 83 -75.77 -73.27
REMARK 500 ARG A 85 61.02 -115.26
REMARK 500 LEU A 90 140.19 -178.73
REMARK 500 ALA A 93 135.42 -30.29
REMARK 500 SER A 97 -77.66 -71.58
REMARK 500 GLU A 130 -47.42 1.54
REMARK 500 ASN A 133 -144.14 -67.21
REMARK 500 ASP A 135 -80.04 157.32
REMARK 500 PRO A 144 3.16 -59.13
REMARK 500 PRO A 164 -72.31 -35.84
REMARK 500 LEU A 165 58.83 -97.40
REMARK 500 THR A 208 115.23 -29.36
REMARK 500 PRO A 247 8.79 -47.61
REMARK 500 PRO A 272 -79.23 -29.20
REMARK 500 GLU A 279 -75.71 -86.39
REMARK 500 LEU A 280 -66.78 93.01
REMARK 500 PRO A 304 143.43 -38.09
REMARK 500 TYR A 307 48.46 -107.56
REMARK 500 GLU A 320 -31.01 -31.99
REMARK 500 PRO A 330 -70.19 -64.33
REMARK 500 GLU A 344 -7.23 -56.00
REMARK 500 ARG B 2 93.58 -170.33
REMARK 500 GLU B 16 123.16 28.61
REMARK 500 SER B 17 104.64 94.43
REMARK 500 PHE B 39 34.15 90.76
REMARK 500 PRO B 40 80.51 -68.61
REMARK 500 PRO B 57 131.33 -28.64
REMARK 500 LEU B 66 -166.19 -113.97
REMARK 500 ASP B 67 101.64 -160.62
REMARK 500 ALA B 68 48.57 -91.40
REMARK 500 ARG B 70 89.60 -171.47
REMARK 500 THR B 71 123.25 -29.09
REMARK 500 ASN B 80 -7.10 -55.43
REMARK 500 ALA B 81 95.81 -60.24
REMARK 500 LEU B 91 152.57 -32.22
REMARK 500 PRO B 97 -83.47 -56.97
REMARK 500 MET B 116 146.58 171.82
REMARK 500 GLU B 127 21.07 -70.69
REMARK 500 ALA B 139 -80.62 -27.02
REMARK 500 PRO B 142 108.45 -39.23
REMARK 500 TRP B 150 62.78 -114.61
REMARK 500 GLU B 152 171.00 -54.90
REMARK 500
REMARK 500 THIS ENTRY HAS 112 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 G C 19 0.06 SIDE CHAIN
REMARK 500 G C 30 0.07 SIDE CHAIN
REMARK 500 C C 48 0.10 SIDE CHAIN
REMARK 500 G C 57 0.05 SIDE CHAIN
REMARK 500 U C 60 0.09 SIDE CHAIN
REMARK 500 C C 62 0.07 SIDE CHAIN
REMARK 500 PHE B 617 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PYS RELATED DB: PDB
REMARK 900 PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS
DBREF 1EIY A 1 350 UNP P27001 SYFA_THETH 1 350
DBREF 1EIY B 1 785 UNP Q5SGX2 Q5SGX2_THET8 1 785
DBREF 1EIY C 1 76 UNP Q5SGX1 Q5SGX1_THET8 1 76
SEQADV 1EIY C C 49 UNP Q5SGX1 G 49 CONFLICT
SEQADV 1EIY G C 65 UNP Q5SGX1 C 65 CONFLICT
SEQRES 1 C 76 G C C G A G G U A G C U C
SEQRES 2 C 76 A G U U G G U A G A G C A
SEQRES 3 C 76 U G C G A C U G A A A A U
SEQRES 4 C 76 C G C A G U G U C C G C G
SEQRES 5 C 76 G U U C G A U U C C G C G
SEQRES 6 C 76 C C U C G G C A C C A
SEQRES 1 A 350 MET LEU GLU GLU ALA LEU ALA ALA ILE GLN ASN ALA ARG
SEQRES 2 A 350 ASP LEU GLU GLU LEU LYS ALA LEU LYS ALA ARG TYR LEU
SEQRES 3 A 350 GLY LYS LYS GLY LEU LEU THR GLN GLU MET LYS GLY LEU
SEQRES 4 A 350 SER ALA LEU PRO LEU GLU GLU ARG ARG LYS ARG GLY GLN
SEQRES 5 A 350 GLU LEU ASN ALA ILE LYS ALA ALA LEU GLU ALA ALA LEU
SEQRES 6 A 350 GLU ALA ARG GLU LYS ALA LEU GLU GLU ALA ALA LEU LYS
SEQRES 7 A 350 GLU ALA LEU GLU ARG GLU ARG VAL ASP VAL SER LEU PRO
SEQRES 8 A 350 GLY ALA SER LEU PHE SER GLY GLY LEU HIS PRO ILE THR
SEQRES 9 A 350 LEU MET GLU ARG GLU LEU VAL GLU ILE PHE ARG ALA LEU
SEQRES 10 A 350 GLY TYR GLN ALA VAL GLU GLY PRO GLU VAL GLU SER GLU
SEQRES 11 A 350 PHE PHE ASN PHE ASP ALA LEU ASN ILE PRO GLU HIS HIS
SEQRES 12 A 350 PRO ALA ARG ASP MET TRP ASP THR PHE TRP LEU THR GLY
SEQRES 13 A 350 GLU GLY PHE ARG LEU GLU GLY PRO LEU GLY GLU GLU VAL
SEQRES 14 A 350 GLU GLY ARG LEU LEU LEU ARG THR HIS THR SER PRO MET
SEQRES 15 A 350 GLN VAL ARG TYR MET VAL ALA HIS THR PRO PRO PHE ARG
SEQRES 16 A 350 ILE VAL VAL PRO GLY ARG VAL PHE ARG PHE GLU GLN THR
SEQRES 17 A 350 ASP ALA THR HIS GLU ALA VAL PHE HIS GLN LEU GLU GLY
SEQRES 18 A 350 LEU VAL VAL GLY GLU GLY ILE ALA MET ALA HIS LEU LYS
SEQRES 19 A 350 GLY ALA ILE TYR GLU LEU ALA GLN ALA LEU PHE GLY PRO
SEQRES 20 A 350 ASP SER LYS VAL ARG PHE GLN PRO VAL TYR PHE PRO PHE
SEQRES 21 A 350 VAL GLU PRO GLY ALA GLN PHE ALA VAL TRP TRP PRO GLU
SEQRES 22 A 350 GLY GLY LYS TRP LEU GLU LEU GLY GLY ALA GLY MET VAL
SEQRES 23 A 350 HIS PRO LYS VAL PHE GLN ALA VAL ASP ALA TYR ARG GLU
SEQRES 24 A 350 ARG LEU GLY LEU PRO PRO ALA TYR ARG GLY VAL THR GLY
SEQRES 25 A 350 PHE ALA PHE GLY LEU GLY VAL GLU ARG LEU ALA MET LEU
SEQRES 26 A 350 ARG TYR GLY ILE PRO ASP ILE ARG TYR PHE PHE GLY GLY
SEQRES 27 A 350 ARG LEU LYS PHE LEU GLU GLN PHE LYS GLY VAL LEU
SEQRES 1 B 785 MET ARG VAL PRO PHE SER TRP LEU LYS ALA TYR VAL PRO
SEQRES 2 B 785 GLU LEU GLU SER PRO GLU VAL LEU GLU GLU ARG LEU ALA
SEQRES 3 B 785 GLY LEU GLY PHE GLU THR ASP ARG ILE GLU ARG VAL PHE
SEQRES 4 B 785 PRO ILE PRO ARG GLY VAL VAL PHE ALA ARG VAL LEU GLU
SEQRES 5 B 785 ALA HIS PRO ILE PRO GLY THR ARG LEU LYS ARG LEU VAL
SEQRES 6 B 785 LEU ASP ALA GLY ARG THR VAL GLU VAL VAL SER GLY ALA
SEQRES 7 B 785 GLU ASN ALA ARG LYS GLY ILE GLY VAL ALA LEU ALA LEU
SEQRES 8 B 785 PRO GLY THR GLU LEU PRO GLY LEU GLY GLN LYS VAL GLY
SEQRES 9 B 785 GLU ARG VAL ILE GLN GLY VAL ARG SER PHE GLY MET ALA
SEQRES 10 B 785 LEU SER PRO ARG GLU LEU GLY VAL GLY GLU TYR GLY GLY
SEQRES 11 B 785 GLY LEU LEU GLU PHE PRO GLU ASP ALA LEU PRO PRO GLY
SEQRES 12 B 785 THR PRO LEU SER GLU ALA TRP PRO GLU GLU VAL VAL LEU
SEQRES 13 B 785 ASP LEU GLU VAL THR PRO ASN ARG PRO ASP ALA LEU GLY
SEQRES 14 B 785 LEU LEU GLY LEU ALA ARG ASP LEU HIS ALA LEU GLY TYR
SEQRES 15 B 785 ALA LEU VAL GLU PRO GLU ALA ALA LEU LYS ALA GLU ALA
SEQRES 16 B 785 LEU PRO LEU PRO PHE ALA LEU LYS VAL GLU ASP PRO GLU
SEQRES 17 B 785 GLY ALA PRO HIS PHE THR LEU GLY TYR ALA PHE GLY LEU
SEQRES 18 B 785 ARG VAL ALA PRO SER PRO LEU TRP MET GLN ARG ALA LEU
SEQRES 19 B 785 PHE ALA ALA GLY MET ARG PRO ILE ASN ASN VAL VAL ASP
SEQRES 20 B 785 VAL THR ASN TYR VAL MET LEU GLU ARG ALA GLN PRO MET
SEQRES 21 B 785 HIS ALA PHE ASP LEU ARG PHE VAL GLY GLU GLY ILE ALA
SEQRES 22 B 785 VAL ARG ARG ALA ARG GLU GLY GLU ARG LEU LYS THR LEU
SEQRES 23 B 785 ASP GLY VAL GLU ARG THR LEU HIS PRO GLU ASP LEU VAL
SEQRES 24 B 785 ILE ALA GLY TRP ARG GLY GLU GLU SER PHE PRO LEU GLY
SEQRES 25 B 785 LEU ALA GLY VAL MET GLY GLY ALA GLU SER GLU VAL ARG
SEQRES 26 B 785 GLU ASP THR GLU ALA ILE ALA LEU GLU VAL ALA CYS PHE
SEQRES 27 B 785 ASP PRO VAL SER ILE ARG LYS THR ALA ARG ARG HIS GLY
SEQRES 28 B 785 LEU ARG THR GLU ALA SER HIS ARG PHE GLU ARG GLY VAL
SEQRES 29 B 785 ASP PRO LEU GLY GLN VAL PRO ALA GLN ARG ARG ALA LEU
SEQRES 30 B 785 SER LEU LEU GLN ALA LEU ALA GLY ALA ARG VAL ALA GLU
SEQRES 31 B 785 ALA LEU LEU GLU ALA GLY SER PRO LYS PRO PRO GLU ALA
SEQRES 32 B 785 ILE PRO PHE ARG PRO GLU TYR ALA ASN ARG LEU LEU GLY
SEQRES 33 B 785 THR SER TYR PRO GLU ALA GLU GLN ILE ALA ILE LEU LYS
SEQRES 34 B 785 ARG LEU GLY CYS ARG VAL GLU GLY GLU GLY PRO THR TYR
SEQRES 35 B 785 ARG VAL THR PRO PRO SER HIS ARG LEU ASP LEU ARG LEU
SEQRES 36 B 785 GLU GLU ASP LEU VAL GLU GLU VAL ALA ARG ILE GLN GLY
SEQRES 37 B 785 TYR GLU THR ILE PRO LEU ALA LEU PRO ALA PHE PHE PRO
SEQRES 38 B 785 ALA PRO ASP ASN ARG GLY VAL GLU ALA PRO TYR ARG LYS
SEQRES 39 B 785 GLU GLN ARG LEU ARG GLU VAL LEU SER GLY LEU GLY PHE
SEQRES 40 B 785 GLN GLU VAL TYR THR TYR SER PHE MET ASP PRO GLU ASP
SEQRES 41 B 785 ALA ARG ARG PHE ARG LEU ASP PRO PRO ARG LEU LEU LEU
SEQRES 42 B 785 LEU ASN PRO LEU ALA PRO GLU LYS ALA ALA LEU ARG THR
SEQRES 43 B 785 HIS LEU PHE PRO GLY LEU VAL ARG VAL LEU LYS GLU ASN
SEQRES 44 B 785 LEU ASP LEU ASP ARG PRO GLU ARG ALA LEU LEU PHE GLU
SEQRES 45 B 785 VAL GLY ARG VAL PHE ARG GLU ARG GLU GLU THR HIS LEU
SEQRES 46 B 785 ALA GLY LEU LEU PHE GLY GLU GLY VAL GLY LEU PRO TRP
SEQRES 47 B 785 ALA LYS GLU ARG LEU SER GLY TYR PHE LEU LEU LYS GLY
SEQRES 48 B 785 TYR LEU GLU ALA LEU PHE ALA ARG LEU GLY LEU ALA PHE
SEQRES 49 B 785 ARG VAL GLU ALA GLN ALA PHE PRO PHE LEU HIS PRO GLY
SEQRES 50 B 785 VAL SER GLY ARG VAL LEU VAL GLU GLY GLU GLU VAL GLY
SEQRES 51 B 785 PHE LEU GLY ALA LEU HIS PRO GLU ILE ALA GLN GLU LEU
SEQRES 52 B 785 GLU LEU PRO PRO VAL HIS LEU PHE GLU LEU ARG LEU PRO
SEQRES 53 B 785 LEU PRO ASP LYS PRO LEU ALA PHE GLN ASP PRO SER ARG
SEQRES 54 B 785 HIS PRO ALA ALA PHE ARG ASP LEU ALA VAL VAL VAL PRO
SEQRES 55 B 785 ALA PRO THR PRO TYR GLY GLU VAL GLU ALA LEU VAL ARG
SEQRES 56 B 785 GLU ALA ALA GLY PRO TYR LEU GLU SER LEU ALA LEU PHE
SEQRES 57 B 785 ASP LEU TYR GLN GLY PRO PRO LEU PRO GLU GLY HIS LYS
SEQRES 58 B 785 SER LEU ALA PHE HIS LEU ARG PHE ARG HIS PRO LYS ARG
SEQRES 59 B 785 THR LEU ARG ASP GLU GLU VAL GLU GLU ALA VAL SER ARG
SEQRES 60 B 785 VAL ALA GLU ALA LEU ARG ALA ARG GLY PHE GLY LEU ARG
SEQRES 61 B 785 GLY LEU ASP THR PRO
HELIX 1 1 ALA A 8 GLU A 16 1 9
HELIX 2 2 GLU A 16 GLY A 38 1 23
HELIX 3 3 ARG A 48 GLU A 53 1 6
HELIX 4 4 LEU A 54 ALA A 59 1 6
HELIX 5 5 ALA A 59 ALA A 71 1 13
HELIX 6 6 LEU A 72 GLU A 84 1 13
HELIX 7 7 HIS A 101 ALA A 116 1 16
HELIX 8 8 ALA A 145 TRP A 149 5 5
HELIX 9 9 SER A 180 HIS A 190 1 11
HELIX 10 10 ALA A 229 GLY A 246 1 18
HELIX 11 11 PRO A 272 GLY A 275 5 4
HELIX 12 12 HIS A 287 LEU A 301 1 15
HELIX 13 13 VAL A 319 ARG A 326 1 8
HELIX 14 14 ILE A 332 GLY A 337 1 6
HELIX 15 15 ARG A 339 GLU A 344 1 6
HELIX 16 16 GLN A 345 LYS A 347 5 3
HELIX 17 17 PHE B 5 VAL B 12 1 8
HELIX 18 18 SER B 17 GLY B 29 1 13
HELIX 19 19 SER B 119 GLY B 124 1 6
HELIX 20 20 GLY B 169 HIS B 178 1 10
HELIX 21 21 PRO B 227 ALA B 236 1 10
HELIX 22 22 ASN B 243 ALA B 257 1 15
HELIX 23 23 ARG B 266 GLY B 269 5 4
HELIX 24 24 ASP B 339 GLY B 351 1 13
HELIX 25 25 THR B 354 GLY B 363 1 10
HELIX 26 26 GLY B 368 ALA B 384 1 17
HELIX 27 27 ARG B 407 GLY B 416 1 10
HELIX 28 28 PRO B 420 ARG B 430 1 11
HELIX 29 29 LEU B 455 GLN B 467 1 13
HELIX 30 30 GLY B 468 ILE B 472 5 5
HELIX 31 31 ALA B 482 ARG B 486 5 5
HELIX 32 32 GLU B 489 GLY B 506 1 18
HELIX 33 33 GLU B 519 PHE B 524 1 6
HELIX 34 34 ALA B 538 ALA B 542 5 5
HELIX 35 35 LEU B 548 ARG B 564 1 17
HELIX 36 36 SER B 604 ARG B 619 1 16
HELIX 37 37 HIS B 656 LEU B 663 1 8
HELIX 38 38 PRO B 706 ALA B 718 1 13
HELIX 39 39 ASP B 758 ALA B 774 1 17
SHEET 1 A 7 GLN A 120 ALA A 121 0
SHEET 2 A 7 PHE A 194 PHE A 203 1 O ARG A 195 N GLN A 120
SHEET 3 A 7 VAL A 215 GLY A 225 -1 O PHE A 216 N VAL A 202
SHEET 4 A 7 THR A 311 GLY A 318 -1 O THR A 311 N GLY A 225
SHEET 5 A 7 GLY A 281 VAL A 286 -1 N GLY A 282 O GLY A 316
SHEET 6 A 7 VAL A 261 TRP A 270 -1 N GLU A 262 O MET A 285
SHEET 7 A 7 VAL A 251 PRO A 255 -1 N ARG A 252 O ALA A 268
SHEET 1 B 7 GLN A 120 ALA A 121 0
SHEET 2 B 7 PHE A 194 PHE A 203 1 O ARG A 195 N GLN A 120
SHEET 3 B 7 VAL A 215 GLY A 225 -1 O PHE A 216 N VAL A 202
SHEET 4 B 7 THR A 311 GLY A 318 -1 O THR A 311 N GLY A 225
SHEET 5 B 7 GLY A 281 VAL A 286 -1 N GLY A 282 O GLY A 316
SHEET 6 B 7 VAL A 261 TRP A 270 -1 N GLU A 262 O MET A 285
SHEET 7 B 7 TRP A 277 LEU A 278 -1 O LEU A 278 N VAL A 269
SHEET 1 C 2 VAL A 127 SER A 129 0
SHEET 2 C 2 LEU A 173 LEU A 175 -1 N LEU A 174 O GLU A 128
SHEET 1 D 2 LEU A 154 THR A 155 0
SHEET 2 D 2 LEU B 532 LEU B 533 -1 N LEU B 532 O THR A 155
SHEET 1 E 3 VAL B 3 PRO B 4 0
SHEET 2 E 3 GLU B 153 LEU B 156 -1 O LEU B 156 N VAL B 3
SHEET 3 E 3 ILE B 35 VAL B 38 -1 O GLU B 36 N VAL B 155
SHEET 1 F 3 VAL B 45 ARG B 49 0
SHEET 2 F 3 ILE B 85 ALA B 90 -1 N VAL B 87 O ALA B 48
SHEET 3 F 3 PHE B 135 PRO B 136 -1 O PHE B 135 N GLY B 86
SHEET 1 G 3 GLU B 52 PRO B 55 0
SHEET 2 G 3 LYS B 62 ASP B 67 -1 N ARG B 63 O HIS B 54
SHEET 3 G 3 THR B 71 SER B 76 -1 O VAL B 72 N LEU B 66
SHEET 1 H 2 THR B 94 GLU B 95 0
SHEET 2 H 2 LYS B 102 VAL B 103 -1 N VAL B 103 O THR B 94
SHEET 1 I 2 GLU B 105 ILE B 108 0
SHEET 2 I 2 VAL B 111 PHE B 114 -1 O VAL B 111 N ILE B 108
SHEET 1 J 5 HIS B 261 ASP B 264 0
SHEET 2 J 5 ALA B 330 GLU B 334 -1 O ALA B 332 N PHE B 263
SHEET 3 J 5 PHE B 213 PHE B 219 -1 O GLY B 216 N LEU B 333
SHEET 4 J 5 ARG B 387 ALA B 389 -1 N ARG B 387 O PHE B 219
SHEET 5 J 5 ALA B 193 GLU B 194 1 N GLU B 194 O VAL B 388
SHEET 1 K 4 HIS B 261 ASP B 264 0
SHEET 2 K 4 ALA B 330 GLU B 334 -1 O ALA B 332 N PHE B 263
SHEET 3 K 4 PHE B 213 PHE B 219 -1 O GLY B 216 N LEU B 333
SHEET 4 K 4 LEU B 393 ALA B 395 -1 N LEU B 393 O LEU B 215
SHEET 1 L 4 ALA B 201 VAL B 204 0
SHEET 2 L 4 GLY B 271 ARG B 276 1 O ILE B 272 N LYS B 203
SHEET 3 L 4 LEU B 298 ARG B 304 -1 N VAL B 299 O ARG B 275
SHEET 4 L 4 GLU B 307 GLY B 312 -1 O GLU B 307 N ARG B 304
SHEET 1 M 2 ARG B 434 VAL B 435 0
SHEET 2 M 2 VAL B 444 THR B 445 -1 N THR B 445 O ARG B 434
SHEET 1 N 2 GLN B 508 GLU B 509 0
SHEET 2 N 2 LEU B 570 PHE B 571 1 N PHE B 571 O GLN B 508
SHEET 1 O 2 PHE B 515 MET B 516 0
SHEET 2 O 2 ALA B 543 LEU B 544 -1 O ALA B 543 N MET B 516
SHEET 1 P 6 ARG B 575 PHE B 577 0
SHEET 2 P 6 GLU B 581 PHE B 590 -1 N GLU B 582 O VAL B 576
SHEET 3 P 6 VAL B 668 LEU B 675 -1 O HIS B 669 N LEU B 589
SHEET 4 P 6 GLU B 647 GLY B 653 -1 O PHE B 651 N GLU B 672
SHEET 5 P 6 SER B 639 VAL B 644 -1 O GLY B 640 N LEU B 652
SHEET 6 P 6 PHE B 624 ALA B 628 -1 O ARG B 625 N LEU B 643
SHEET 1 Q 3 ASP B 696 VAL B 699 0
SHEET 2 Q 3 LYS B 741 HIS B 746 -1 N LEU B 743 O VAL B 699
SHEET 3 Q 3 ALA B 726 GLN B 732 -1 O ALA B 726 N HIS B 746
CISPEP 1 PRO A 192 PRO A 193 0 0.02
CISPEP 2 GLU A 262 PRO A 263 0 0.31
CISPEP 3 GLY B 439 PRO B 440 0 -2.03
CISPEP 4 LEU B 675 PRO B 676 0 -1.86
CISPEP 5 PRO B 734 PRO B 735 0 5.59
CRYST1 175.000 175.000 140.600 90.00 90.00 120.00 P 32 2 1 6
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 0.005714 0.003299 0.000000 0.00000
SCALE2 0.000000 0.006598 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007112 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
