Header list of 1qkh.pdb file
Complete list - n 17 2 Bytes
HEADER RIBOSOMAL PROTEIN 20-JUL-99 1QKH
TITLE SOLUTION STRUCTURE OF THE RIBOSOMAL PROTEIN S19 FROM THERMUS
TITLE 2 THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PACA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTTHS19
KEYWDS RIBOSOME, RIBOSOMAL PROTEIN, THERMUS THERMOPHILUS, S19
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR M.HELGSTRAND,A.V.RAK,P.ALLARD,N.DAVYDOVA,M.B.GARBER,T.HARD
REVDAT 6 17-JAN-18 1QKH 1 JRNL REMARK
REVDAT 5 24-FEB-09 1QKH 1 VERSN
REVDAT 4 08-OCT-99 1QKH 1 JRNL
REVDAT 3 14-SEP-99 1QKH 1 REMARK
REVDAT 2 02-AUG-99 1QKH 1 HELIX
REVDAT 1 21-JUL-99 1QKH 0
JRNL AUTH M.HELGSTRAND,A.V.RAK,P.ALLARD,N.DAVYDOVA,M.B.GARBER,T.HARD
JRNL TITL SOLUTION STRUCTURE OF THE RIBOSOMAL PROTEIN S19 FROM THERMUS
JRNL TITL 2 THERMOPHILUS.
JRNL REF J. MOL. BIOL. V. 292 1071 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10512703
JRNL DOI 10.1006/JMBI.1999.3122
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER STRUCTURAL STATISTICS: 21 SA STRUCTURES
REMARK 3 SAAVEMIN[A] RMS DEVIATIONS FROM EXP. RESTRAINTS
REMARK 3 NOE DISTANCE RESTRAINTS (1104) 0.036 A 0.032 A
REMARK 3 DIHEDRAL ANGLE RESTRAINTS (42) 0.380 DEG 0.380 DEG
REMARK 3 DEVIATIONS FROM IDEAL GEOMETRY BONDS 0.0045 A
REMARK 3 0.0041 A ANGLES 0.71 DEG 0.66 DEG IMPROPERS 0.54
REMARK 3 DEG 0.49 DEG
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED USING 1104
REMARK 3 DISTANCE RESTRAINTS, 42 DIHEDRAL ANGLE RESTRAINTS AND 14
REMARK 3 HYDROGEN BOND RESTRAINTS. 50 STRUCTURES WERE CALCULATED AND
REMARK 3 REFINED USING AN AB INITIO SIMULATED ANNEALING PROTOCOL FOR X-
REMARK 3 PLOR AND THEN REFINED IN TWO STEPS. AN R-6 AVERAGING PROTOCOL
REMARK 3 WAS USED FOR NON-STEREOSPECIFICALLY ASSIGNED PROTONS [1]. DURING
REMARK 3 THE SIMULATED ANNEALING STEP AND THE FIRST REFINEMENT STEP ONLY
REMARK 3 THE REPULSIVE PART OF THE VAN DER WAALS INTERACTION WAS
REMARK 3 INCLUDED. IN THE SECOND REFINEMENT STEP THE VAN DER WAALS
REMARK 3 INTERACTION WAS PARAMETERIZED USING A LENNARD-JONES POTENTIAL
REMARK 3 INCLUDING THE ATTRACTIVE PART. 21 STRUCTURES WERE SELECTED ON
REMARK 3 THE BASIS OF CUMULATIVE RMSD VALUES OF STRUCTURES, ORDERED AFTER
REMARK 3 OVERALL ENERGY, AND RAMACHANDRAN BEHAVIOR FOR REGIONS WITH LOW
REMARK 3 RESTRAINT DENSITIES. [1] BRUNGER, A. T., CLORE, G. M.,
REMARK 3 GRONENBORN, A. M. & KARPLUS, M. (1986). THREE-DIMENSIONAL
REMARK 3 STRUCTURE OF PROTEINS DETERMINED BY MOLECULAR DYNAMICS WITH
REMARK 3 INTERPROTON DISTANCE RESTRAINTS: APPLICATION TO CRAMBIN. PROC
REMARK 3 NATL ACAD SCI USA 83, 3801-3805. OTHER DETAILS OF STRUCTURE
REMARK 3 REFINEMENT CAN BE FOUND IN THE JRNL CITATION.
REMARK 4
REMARK 4 1QKH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1290002955.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.250
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HN(CO)CA; CBCANH;
REMARK 210 CBCA(CO)NH; C(CO)NH-TOCSY; HCCH-
REMARK 210 TOCSY; (HB)CB(CGCD)HD; (HB)
REMARK 210 CB(CGCDCE)HE; 15N-EDITED NOESY-
REMARK 210 HSQC; 15N-EDITED TOCSY-HSQC; 3D
REMARK 210 HNHA; 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 5.3, PRONTO (VERSION
REMARK 210 970523) 970523), X-PLOR (VERSION
REMARK 210 3.851) 3.851), MOLMOL (VERSION
REMARK 210 2.6) 2.6), PROCHECK-NMR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : CUMULATIVE RMSD OF STRUCTURES
REMARK 210 SORTED AFTER TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-21
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 2
REMARK 465 ARG A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 LYS A 6
REMARK 465 LYS A 7
REMARK 465 ARG A 81
REMARK 465 GLY A 82
REMARK 465 HIS A 83
REMARK 465 GLY A 84
REMARK 465 LYS A 85
REMARK 465 GLU A 86
REMARK 465 ALA A 87
REMARK 465 LYS A 88
REMARK 465 ALA A 89
REMARK 465 THR A 90
REMARK 465 LYS A 91
REMARK 465 LYS A 92
REMARK 465 LYS A 93
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 28 59.68 -107.30
REMARK 500 1 ARG A 29 -154.34 -102.88
REMARK 500 1 TRP A 34 35.01 -144.49
REMARK 500 1 SER A 35 -96.03 -84.63
REMARK 500 1 ARG A 36 -61.91 -171.81
REMARK 500 1 VAL A 45 -1.19 -57.50
REMARK 500 1 LYS A 55 -24.90 -140.65
REMARK 500 1 PRO A 59 87.37 -66.08
REMARK 500 1 THR A 63 -155.47 -101.03
REMARK 500 1 ASN A 65 24.15 -146.92
REMARK 500 1 HIS A 69 -85.04 -122.03
REMARK 500 1 LYS A 70 -30.64 178.68
REMARK 500 1 LEU A 71 -16.00 174.46
REMARK 500 2 ASP A 12 108.70 -47.93
REMARK 500 2 LYS A 28 77.40 -113.10
REMARK 500 2 ARG A 29 -154.85 -116.93
REMARK 500 2 TRP A 34 75.71 -152.46
REMARK 500 2 SER A 35 -82.20 -123.28
REMARK 500 2 ARG A 36 -64.17 -167.97
REMARK 500 2 SER A 38 124.92 -37.90
REMARK 500 2 VAL A 45 0.63 -61.24
REMARK 500 2 LYS A 55 -26.27 -140.87
REMARK 500 2 PRO A 59 90.32 -65.77
REMARK 500 2 THR A 63 -157.20 -94.92
REMARK 500 2 ASN A 65 19.72 -148.79
REMARK 500 2 HIS A 69 -81.42 -128.13
REMARK 500 2 LYS A 70 -31.46 177.76
REMARK 500 2 LEU A 71 -16.45 173.73
REMARK 500 3 ARG A 29 -154.34 -113.44
REMARK 500 3 TRP A 34 30.72 -145.54
REMARK 500 3 SER A 35 -96.91 -86.33
REMARK 500 3 ARG A 36 -66.34 -170.27
REMARK 500 3 ARG A 37 45.24 -99.73
REMARK 500 3 VAL A 45 5.03 -62.14
REMARK 500 3 LYS A 55 -27.82 -140.48
REMARK 500 3 PRO A 59 87.51 -65.09
REMARK 500 3 THR A 63 -153.98 -104.99
REMARK 500 3 HIS A 69 -84.99 -121.72
REMARK 500 3 LYS A 70 -30.54 178.36
REMARK 500 3 LEU A 71 -15.31 173.30
REMARK 500 3 PRO A 76 48.88 -86.66
REMARK 500 3 THR A 77 -56.43 -139.46
REMARK 500 4 ASP A 12 102.88 -48.93
REMARK 500 4 ARG A 29 -157.19 -115.84
REMARK 500 4 TRP A 34 37.01 -145.74
REMARK 500 4 SER A 35 -155.45 -100.21
REMARK 500 4 ARG A 37 35.26 -99.38
REMARK 500 4 VAL A 45 7.34 -66.68
REMARK 500 4 LYS A 55 -24.97 -140.71
REMARK 500 4 PRO A 59 88.75 -66.65
REMARK 500
REMARK 500 THIS ENTRY HAS 304 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 29 0.30 SIDE CHAIN
REMARK 500 1 ARG A 36 0.30 SIDE CHAIN
REMARK 500 1 ARG A 37 0.31 SIDE CHAIN
REMARK 500 1 ARG A 78 0.32 SIDE CHAIN
REMARK 500 2 ARG A 29 0.31 SIDE CHAIN
REMARK 500 2 ARG A 36 0.30 SIDE CHAIN
REMARK 500 2 ARG A 37 0.29 SIDE CHAIN
REMARK 500 2 ARG A 78 0.32 SIDE CHAIN
REMARK 500 3 ARG A 29 0.31 SIDE CHAIN
REMARK 500 3 ARG A 36 0.32 SIDE CHAIN
REMARK 500 3 ARG A 37 0.29 SIDE CHAIN
REMARK 500 3 ARG A 78 0.32 SIDE CHAIN
REMARK 500 4 ARG A 29 0.31 SIDE CHAIN
REMARK 500 4 ARG A 36 0.32 SIDE CHAIN
REMARK 500 4 ARG A 37 0.32 SIDE CHAIN
REMARK 500 4 ARG A 78 0.31 SIDE CHAIN
REMARK 500 5 ARG A 29 0.32 SIDE CHAIN
REMARK 500 5 ARG A 36 0.32 SIDE CHAIN
REMARK 500 5 ARG A 37 0.31 SIDE CHAIN
REMARK 500 5 ARG A 78 0.32 SIDE CHAIN
REMARK 500 6 ARG A 29 0.32 SIDE CHAIN
REMARK 500 6 ARG A 36 0.26 SIDE CHAIN
REMARK 500 6 ARG A 37 0.30 SIDE CHAIN
REMARK 500 6 ARG A 78 0.32 SIDE CHAIN
REMARK 500 7 ARG A 29 0.29 SIDE CHAIN
REMARK 500 7 ARG A 36 0.32 SIDE CHAIN
REMARK 500 7 ARG A 37 0.28 SIDE CHAIN
REMARK 500 7 ARG A 78 0.32 SIDE CHAIN
REMARK 500 8 ARG A 29 0.32 SIDE CHAIN
REMARK 500 8 ARG A 36 0.32 SIDE CHAIN
REMARK 500 8 ARG A 37 0.32 SIDE CHAIN
REMARK 500 8 ARG A 78 0.30 SIDE CHAIN
REMARK 500 9 ARG A 29 0.30 SIDE CHAIN
REMARK 500 9 ARG A 36 0.28 SIDE CHAIN
REMARK 500 9 ARG A 37 0.31 SIDE CHAIN
REMARK 500 9 ARG A 78 0.31 SIDE CHAIN
REMARK 500 10 ARG A 29 0.32 SIDE CHAIN
REMARK 500 10 ARG A 36 0.29 SIDE CHAIN
REMARK 500 10 ARG A 37 0.32 SIDE CHAIN
REMARK 500 10 ARG A 78 0.32 SIDE CHAIN
REMARK 500 11 ARG A 29 0.32 SIDE CHAIN
REMARK 500 11 ARG A 36 0.31 SIDE CHAIN
REMARK 500 11 ARG A 37 0.32 SIDE CHAIN
REMARK 500 11 ARG A 78 0.29 SIDE CHAIN
REMARK 500 12 ARG A 29 0.31 SIDE CHAIN
REMARK 500 12 ARG A 36 0.32 SIDE CHAIN
REMARK 500 12 ARG A 37 0.31 SIDE CHAIN
REMARK 500 12 ARG A 78 0.32 SIDE CHAIN
REMARK 500 13 ARG A 29 0.31 SIDE CHAIN
REMARK 500 13 ARG A 36 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 84 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: KABSCH AND SANDER
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QKF RELATED DB: PDB
REMARK 900 THE MINIMIZED AVERAGE SOLUTION STRUCTURE THE EXPERIMENTAL
REMARK 900 RESTRAINTS ARE PRESENTED IN PDB ENTRY 1QKH MR.
DBREF 1QKH A 2 93 UNP P80381 RS19_THETH 2 93
SEQRES 1 A 92 PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP HIS
SEQRES 2 A 92 LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY GLU
SEQRES 3 A 92 LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR ILE
SEQRES 4 A 92 VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR ASN
SEQRES 5 A 92 GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN MET
SEQRES 6 A 92 VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR
SEQRES 7 A 92 TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS LYS
SEQRES 8 A 92 LYS
HELIX 1 H1 ASP A 13 LYS A 25 1 13
HELIX 2 H2 PRO A 42 MET A 44 5 3
SHEET 1 S1 3 LEU A 30 LYS A 32 0
SHEET 2 S1 3 HIS A 47 TYR A 52 1 N ALA A 50 O ILE A 31
SHEET 3 S1 3 HIS A 57 ILE A 62 -1 N VAL A 58 O VAL A 51
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 - n 17 2 Bytes