Header list of 1jh3.pdb file
Complete list - b 23 2 Bytes
HEADER LIGASE 27-JUN-01 1JH3
TITLE SOLUTION STRUCTURE OF TYROSYL-TRNA SYNTHETASE C-TERMINAL DOMAIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 321-419);
COMPND 5 EC: 6.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 GENE: TYRS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-20B(+)
KEYWDS AMINOACYL-TRNA SYNTHETASE, ANTICODON-ARM BINDING DOMAIN, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.I.GUIJARRO,A.PINTAR,A.PROCHNICKA-CHALUFOUR,V.GUEZ,B.GILQUIN,
AUTHOR 2 H.BEDOUELLE,M.DELEPIERRE
REVDAT 4 23-FEB-22 1JH3 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JH3 1 VERSN
REVDAT 2 25-DEC-02 1JH3 1 REMARK
REVDAT 1 20-MAR-02 1JH3 0
JRNL AUTH J.I.GUIJARRO,A.PINTAR,A.PROCHNICKA-CHALUFOUR,V.GUEZ,
JRNL AUTH 2 B.GILQUIN,H.BEDOUELLE,M.DELEPIERRE
JRNL TITL STRUCTURE AND DYNAMICS OF THE ANTICODON ARM BINDING DOMAIN
JRNL TITL 2 OF BACILLUS STEAROTHERMOPHILUS TYROSYL-TRNA SYNTHETASE
JRNL REF STRUCTURE V. 10 311 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12005430
JRNL DOI 10.1016/S0969-2126(02)00699-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PINTAR,V.GUEZ,C.CASTAGNE,H.BEDOUELLE,M.DELEPIERRE
REMARK 1 TITL SECONDARY STRUCTURE OF THE C-TERMINAL DOMAIN OF THE
REMARK 1 TITL 2 TYROSYL-TRANSFER RNA SYNTHETASE FROM BACILLUS
REMARK 1 TITL 3 STEAROTHERMOPHILUS: A NOVEL TYPE OF ANTICODON BINDING
REMARK 1 TITL 4 DOMAIN?
REMARK 1 REF FEBS LETT. V. 446 81 1999
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(99)00191-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XEASY 1.2, OPAL 2.6
REMARK 3 AUTHORS : BARTELS, XIA, BILLETER, GUNTERT (XEASY),
REMARK 3 LUGINBUHL, GUNTERT, BILLETER (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED USING
REMARK 3 1352 MEANINGFUL UPPER DISTANCE RESTRAINTS,
REMARK 3 71 DIHEDRAL ANGLE RESTRAINTS AND 33 HYDROGEN BONDS.
REMARK 4
REMARK 4 1JH3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013764.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM PROTEIN, U-15N; 0.8MM
REMARK 210 PROTEIN, U-15N, U-13C; 1.0MM
REMARK 210 PROTEIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, VNMR 6.1B
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 3 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 TYR A 94 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 5 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 6 ILE A 59 CB - CA - C ANGL. DEV. = 13.4 DEGREES
REMARK 500 7 ILE A 59 CA - CB - CG1 ANGL. DEV. = 12.2 DEGREES
REMARK 500 7 GLN A 67 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 7 TYR A 94 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 8 ILE A 59 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 8 ARG A 88 CD - NE - CZ ANGL. DEV. = 12.6 DEGREES
REMARK 500 9 ARG A 88 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 10 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 ILE A 59 CB - CA - C ANGL. DEV. = 12.4 DEGREES
REMARK 500 11 ILE A 59 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 11 VAL A 85 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 12 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 12 TYR A 93 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 13 ILE A 59 CB - CA - C ANGL. DEV. = 12.8 DEGREES
REMARK 500 16 VAL A 39 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 17 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 17 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 18 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 19 TYR A 93 CB - CG - CD2 ANGL. DEV. = -4.7 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 1 LYS A 20 9.08 -55.06
REMARK 500 1 ARG A 65 109.00 -55.46
REMARK 500 1 LEU A 73 -93.11 -112.38
REMARK 500 1 ARG A 82 -82.83 -129.12
REMARK 500 1 PHE A 83 -165.62 -119.55
REMARK 500 1 LYS A 91 -97.55 -135.91
REMARK 500 1 LYS A 92 -159.89 -159.17
REMARK 500 1 TYR A 93 75.90 -110.23
REMARK 500 2 LEU A 2 -61.78 -121.83
REMARK 500 2 SER A 4 -165.41 -73.96
REMARK 500 2 LYS A 20 7.19 -56.18
REMARK 500 2 ASN A 62 -6.63 64.23
REMARK 500 2 ARG A 65 108.56 -59.89
REMARK 500 2 LEU A 73 -97.30 -113.86
REMARK 500 2 GLU A 80 -6.21 -53.61
REMARK 500 2 ARG A 82 -63.61 -138.20
REMARK 500 2 LYS A 91 -156.05 -148.59
REMARK 500 2 LYS A 92 -150.75 -97.68
REMARK 500 3 SER A 4 -1.75 58.69
REMARK 500 3 ILE A 7 63.14 -38.80
REMARK 500 3 LYS A 20 -9.57 -55.55
REMARK 500 3 ARG A 65 106.84 -52.44
REMARK 500 3 LEU A 73 -93.14 -109.61
REMARK 500 3 ARG A 78 -79.58 -114.44
REMARK 500 3 GLU A 80 0.05 -55.01
REMARK 500 3 ARG A 82 -65.92 -104.58
REMARK 500 3 LYS A 90 -50.66 137.53
REMARK 500 3 LYS A 91 -110.51 -113.00
REMARK 500 3 LYS A 92 -154.78 -148.04
REMARK 500 3 TYR A 93 78.85 -115.00
REMARK 500 4 SER A 4 -153.94 52.12
REMARK 500 4 ILE A 7 54.59 -90.57
REMARK 500 4 LEU A 10 68.01 -151.91
REMARK 500 4 LYS A 20 -9.01 -57.96
REMARK 500 4 LEU A 73 -95.20 -114.76
REMARK 500 4 ARG A 82 -49.17 -141.17
REMARK 500 4 ARG A 87 79.47 -100.48
REMARK 500 4 LYS A 91 -78.06 -142.27
REMARK 500 4 LYS A 92 -152.63 -159.36
REMARK 500 4 TYR A 93 75.12 -100.98
REMARK 500 5 LEU A 2 -52.31 -148.17
REMARK 500 5 PHE A 3 98.42 -58.52
REMARK 500 5 SER A 4 54.36 -150.68
REMARK 500 5 ILE A 7 41.90 -91.17
REMARK 500 5 LYS A 20 -5.55 -59.16
REMARK 500 5 ASN A 62 -14.06 67.24
REMARK 500 5 GLN A 67 35.09 -94.19
REMARK 500 5 LEU A 73 -75.18 -106.97
REMARK 500 5 THR A 74 -142.21 -131.06
REMARK 500 5 ARG A 78 -71.90 -126.80
REMARK 500
REMARK 500 THIS ENTRY HAS 215 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 1 HIS A 77 0.10 SIDE CHAIN
REMARK 500 1 TYR A 98 0.12 SIDE CHAIN
REMARK 500 2 HIS A 77 0.10 SIDE CHAIN
REMARK 500 2 ARG A 78 0.14 SIDE CHAIN
REMARK 500 2 PHE A 83 0.08 SIDE CHAIN
REMARK 500 2 TYR A 94 0.09 SIDE CHAIN
REMARK 500 3 ARG A 48 0.11 SIDE CHAIN
REMARK 500 3 HIS A 77 0.09 SIDE CHAIN
REMARK 500 3 ARG A 88 0.09 SIDE CHAIN
REMARK 500 3 TYR A 98 0.15 SIDE CHAIN
REMARK 500 5 TYR A 94 0.10 SIDE CHAIN
REMARK 500 5 TYR A 98 0.20 SIDE CHAIN
REMARK 500 6 HIS A 77 0.10 SIDE CHAIN
REMARK 500 7 TYR A 60 0.09 SIDE CHAIN
REMARK 500 7 HIS A 77 0.10 SIDE CHAIN
REMARK 500 7 ARG A 88 0.10 SIDE CHAIN
REMARK 500 7 TYR A 94 0.07 SIDE CHAIN
REMARK 500 8 HIS A 77 0.10 SIDE CHAIN
REMARK 500 8 TYR A 93 0.08 SIDE CHAIN
REMARK 500 9 PHE A 19 0.07 SIDE CHAIN
REMARK 500 9 HIS A 77 0.10 SIDE CHAIN
REMARK 500 9 ARG A 78 0.09 SIDE CHAIN
REMARK 500 9 ARG A 82 0.09 SIDE CHAIN
REMARK 500 9 TYR A 94 0.07 SIDE CHAIN
REMARK 500 9 ARG A 97 0.08 SIDE CHAIN
REMARK 500 10 HIS A 77 0.10 SIDE CHAIN
REMARK 500 11 ARG A 78 0.10 SIDE CHAIN
REMARK 500 11 TYR A 93 0.07 SIDE CHAIN
REMARK 500 11 TYR A 98 0.09 SIDE CHAIN
REMARK 500 12 PHE A 19 0.08 SIDE CHAIN
REMARK 500 12 ARG A 87 0.08 SIDE CHAIN
REMARK 500 13 ARG A 48 0.08 SIDE CHAIN
REMARK 500 13 ARG A 65 0.09 SIDE CHAIN
REMARK 500 13 TYR A 94 0.09 SIDE CHAIN
REMARK 500 14 HIS A 77 0.10 SIDE CHAIN
REMARK 500 14 ARG A 88 0.10 SIDE CHAIN
REMARK 500 14 TYR A 98 0.07 SIDE CHAIN
REMARK 500 15 HIS A 77 0.10 SIDE CHAIN
REMARK 500 15 ARG A 78 0.12 SIDE CHAIN
REMARK 500 15 TYR A 98 0.08 SIDE CHAIN
REMARK 500 16 ARG A 51 0.12 SIDE CHAIN
REMARK 500 16 ARG A 88 0.09 SIDE CHAIN
REMARK 500 17 HIS A 77 0.11 SIDE CHAIN
REMARK 500 17 ARG A 78 0.13 SIDE CHAIN
REMARK 500 17 ARG A 88 0.11 SIDE CHAIN
REMARK 500 17 TYR A 94 0.08 SIDE CHAIN
REMARK 500 17 TYR A 98 0.08 SIDE CHAIN
REMARK 500 20 HIS A 77 0.12 SIDE CHAIN
REMARK 500 20 ARG A 88 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2TS1 RELATED DB: PDB
REMARK 900 2TS1 CONTAINS THE STRUCTURE OF THE N-TERMINAL DOMAIN (1-319) OF THE
REMARK 900 SAME PROTEIN IN COMPLEX WITH TYROSYL-ADENYLATE.
DBREF 1JH3 A 1 99 UNP P00952 SYY_BACST 321 419
SEQADV 1JH3 LEU A 100 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 GLU A 101 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 102 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 103 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 104 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 105 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 106 UNP P00952 EXPRESSION TAG
SEQADV 1JH3 HIS A 107 UNP P00952 EXPRESSION TAG
SEQRES 1 A 107 ALA LEU PHE SER GLY ASP ILE ALA ASN LEU THR ALA ALA
SEQRES 2 A 107 GLU ILE GLU GLN GLY PHE LYS ASP VAL PRO SER PHE VAL
SEQRES 3 A 107 HIS GLU GLY GLY ASP VAL PRO LEU VAL GLU LEU LEU VAL
SEQRES 4 A 107 SER ALA GLY ILE SER PRO SER LYS ARG GLN ALA ARG GLU
SEQRES 5 A 107 ASP ILE GLN ASN GLY ALA ILE TYR VAL ASN GLY GLU ARG
SEQRES 6 A 107 LEU GLN ASP VAL GLY ALA ILE LEU THR ALA GLU HIS ARG
SEQRES 7 A 107 LEU GLU GLY ARG PHE THR VAL ILE ARG ARG GLY LYS LYS
SEQRES 8 A 107 LYS TYR TYR LEU ILE ARG TYR ALA LEU GLU HIS HIS HIS
SEQRES 9 A 107 HIS HIS HIS
HELIX 1 1 THR A 11 LYS A 20 1 10
HELIX 2 2 PRO A 33 GLY A 42 1 10
HELIX 3 3 SER A 46 ASN A 56 1 11
SHEET 1 A 5 SER A 24 HIS A 27 0
SHEET 2 A 5 TYR A 93 TYR A 98 1 O LEU A 95 N PHE A 25
SHEET 3 A 5 PHE A 83 ARG A 88 -1 O THR A 84 N ILE A 96
SHEET 4 A 5 ILE A 59 VAL A 61 -1 O TYR A 60 N ARG A 87
SHEET 5 A 5 GLU A 64 ARG A 65 -1 N GLU A 64 O VAL A 61
CRYST1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes