Header list of 1fyj.pdb file
Complete list - b 23 2 Bytes
HEADER LIGASE 02-OCT-00 1FYJ
TITLE SOLUTION STRUCTURE OF MULTI-FUNCTIONAL PEPTIDE MOTIF-1 PRESENT IN
TITLE 2 HUMAN GLUTAMYL-PROLYL TRNA SYNTHETASE (EPRS).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIFUNCTIONAL AMINOACYL-TRNA SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 677-733;
COMPND 5 EC: 6.1.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS HELIX-TURN-HELIX, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.-J.JEONG,G.-S.HWANG,K.H.KIM,M.J.KIM,S.KIM,K.-S.KIM
REVDAT 5 23-FEB-22 1FYJ 1 REMARK
REVDAT 4 24-FEB-09 1FYJ 1 VERSN
REVDAT 3 01-APR-03 1FYJ 1 JRNL
REVDAT 2 31-DEC-02 1FYJ 1 REMARK
REVDAT 1 14-MAR-01 1FYJ 0
JRNL AUTH E.J.JEONG,G.S.HWANG,K.H.KIM,M.J.KIM,S.KIM,K.S.KIM
JRNL TITL STRUCTURAL ANALYSIS OF MULTIFUNCTIONAL PEPTIDE MOTIFS IN
JRNL TITL 2 HUMAN BIFUNCTIONAL TRNA SYNTHETASE: IDENTIFICATION OF
JRNL TITL 3 RNA-BINDING RESIDUES AND FUNCTIONAL IMPLICATIONS FOR TANDEM
JRNL TITL 4 REPEATS.
JRNL REF BIOCHEMISTRY V. 39 15775 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11123902
JRNL DOI 10.1021/BI001393H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO,F. (NMRPIPE), BUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 814 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 91 DIHEDRAL ANGLE RESTRAINTS,29 HYDROGEN BONDS RESTRAINTS, AND
REMARK 3 49 J COUPLING CONSTANTS ARE USED.
REMARK 4
REMARK 4 1FYJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012017.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NO SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : ~2MM EPRS-R1 U-15N; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; DQF-COSY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP 4.2.5, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY 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 : 6
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: 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 THR A 47 25.16 -156.21
REMARK 500 1 GLU A 50 -166.37 38.05
REMARK 500 1 ASN A 55 177.71 54.25
REMARK 500 2 THR A 47 23.47 -156.26
REMARK 500 2 GLU A 50 92.14 33.54
REMARK 500 2 ASN A 55 177.35 54.62
REMARK 500 3 THR A 47 19.29 -151.51
REMARK 500 3 GLU A 50 -176.33 39.75
REMARK 500 3 ASN A 55 59.45 -143.75
REMARK 500 4 ALA A 24 170.33 -58.47
REMARK 500 4 THR A 47 29.39 -165.78
REMARK 500 4 GLU A 50 98.48 32.31
REMARK 500 4 ASN A 55 174.50 56.60
REMARK 500 5 LYS A 46 -77.71 -62.82
REMARK 500 5 THR A 47 40.45 -161.49
REMARK 500 5 GLU A 50 92.87 32.21
REMARK 500 6 THR A 47 32.79 -165.94
REMARK 500 6 GLU A 50 114.98 39.47
REMARK 500 6 ASN A 55 179.91 55.52
REMARK 500 7 THR A 47 -70.92 -156.37
REMARK 500 7 GLN A 49 -30.26 -140.98
REMARK 500 7 ASN A 55 174.77 57.58
REMARK 500 8 THR A 47 29.57 -161.43
REMARK 500 8 GLU A 50 -157.76 35.97
REMARK 500 8 ASN A 55 165.55 55.46
REMARK 500 9 THR A 47 45.29 -160.18
REMARK 500 9 GLU A 50 178.44 -52.41
REMARK 500 9 TYR A 51 102.94 -55.13
REMARK 500 9 ASN A 55 174.31 55.00
REMARK 500 10 LYS A 46 -85.01 -63.71
REMARK 500 10 THR A 47 51.75 -159.97
REMARK 500 10 ASN A 55 178.69 55.63
REMARK 500 11 LYS A 23 19.94 58.97
REMARK 500 11 THR A 47 16.13 -157.91
REMARK 500 11 GLU A 50 175.18 40.91
REMARK 500 11 ASN A 55 179.82 54.46
REMARK 500 12 THR A 47 28.89 -165.55
REMARK 500 12 GLU A 50 100.22 30.26
REMARK 500 12 ASN A 55 -178.15 52.01
REMARK 500 13 THR A 47 16.47 -156.61
REMARK 500 13 GLU A 50 -175.10 40.64
REMARK 500 14 THR A 47 18.21 -156.16
REMARK 500 14 GLU A 50 -156.03 35.92
REMARK 500 14 ASN A 55 177.80 55.98
REMARK 500 15 THR A 47 12.52 -159.46
REMARK 500 15 GLU A 50 85.80 30.28
REMARK 500 15 ASN A 55 -178.81 53.34
REMARK 500 16 LYS A 46 -74.93 -65.83
REMARK 500 16 THR A 47 30.17 -160.05
REMARK 500 16 GLU A 50 97.56 31.23
REMARK 500
REMARK 500 THIS ENTRY HAS 64 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 ARG A 8 0.22 SIDE CHAIN
REMARK 500 1 ARG A 17 0.27 SIDE CHAIN
REMARK 500 2 ARG A 8 0.32 SIDE CHAIN
REMARK 500 2 ARG A 17 0.32 SIDE CHAIN
REMARK 500 3 ARG A 8 0.30 SIDE CHAIN
REMARK 500 3 ARG A 17 0.27 SIDE CHAIN
REMARK 500 4 ARG A 8 0.28 SIDE CHAIN
REMARK 500 4 ARG A 17 0.32 SIDE CHAIN
REMARK 500 5 ARG A 8 0.31 SIDE CHAIN
REMARK 500 5 ARG A 17 0.29 SIDE CHAIN
REMARK 500 6 ARG A 8 0.25 SIDE CHAIN
REMARK 500 6 ARG A 17 0.32 SIDE CHAIN
REMARK 500 7 ARG A 8 0.29 SIDE CHAIN
REMARK 500 7 ARG A 17 0.23 SIDE CHAIN
REMARK 500 8 ARG A 8 0.32 SIDE CHAIN
REMARK 500 8 ARG A 17 0.27 SIDE CHAIN
REMARK 500 9 ARG A 8 0.22 SIDE CHAIN
REMARK 500 9 ARG A 17 0.30 SIDE CHAIN
REMARK 500 10 ARG A 8 0.24 SIDE CHAIN
REMARK 500 10 ARG A 17 0.32 SIDE CHAIN
REMARK 500 11 ARG A 8 0.31 SIDE CHAIN
REMARK 500 11 ARG A 17 0.27 SIDE CHAIN
REMARK 500 12 ARG A 8 0.32 SIDE CHAIN
REMARK 500 12 ARG A 17 0.26 SIDE CHAIN
REMARK 500 13 ARG A 8 0.31 SIDE CHAIN
REMARK 500 13 ARG A 17 0.28 SIDE CHAIN
REMARK 500 14 ARG A 8 0.32 SIDE CHAIN
REMARK 500 14 ARG A 17 0.24 SIDE CHAIN
REMARK 500 15 ARG A 8 0.31 SIDE CHAIN
REMARK 500 15 ARG A 17 0.32 SIDE CHAIN
REMARK 500 16 ARG A 8 0.25 SIDE CHAIN
REMARK 500 16 ARG A 17 0.28 SIDE CHAIN
REMARK 500 17 ARG A 8 0.32 SIDE CHAIN
REMARK 500 17 ARG A 17 0.24 SIDE CHAIN
REMARK 500 18 ARG A 8 0.26 SIDE CHAIN
REMARK 500 18 ARG A 17 0.32 SIDE CHAIN
REMARK 500 19 ARG A 8 0.31 SIDE CHAIN
REMARK 500 19 ARG A 17 0.32 SIDE CHAIN
REMARK 500 20 ARG A 8 0.26 SIDE CHAIN
REMARK 500 20 ARG A 17 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FYJ A 1 57 UNP P07814 SYEP_HUMAN 677 733
SEQRES 1 A 57 ASP SER LEU VAL LEU TYR ASN ARG VAL ALA VAL GLN GLY
SEQRES 2 A 57 ASP VAL VAL ARG GLU LEU LYS ALA LYS LYS ALA PRO LYS
SEQRES 3 A 57 GLU ASP VAL ASP ALA ALA VAL LYS GLN LEU LEU SER LEU
SEQRES 4 A 57 LYS ALA GLU TYR LYS GLU LYS THR GLY GLN GLU TYR LYS
SEQRES 5 A 57 PRO GLY ASN PRO PRO
HELIX 1 1 ASP A 1 LYS A 22 1 22
HELIX 2 2 PRO A 25 GLY A 48 1 24
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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