Header list of 1wki.pdb file
Complete list - r 25 2 Bytes
HEADER RIBOSOME 31-MAY-04 1WKI
TITLE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L16 FROM THERMUS THERMOPHILUS
TITLE 2 HB8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LSU RIBOSOMAL PROTEIN L16P;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 GENE: RPLP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26B
KEYWDS MIXED ALPHA/BETA, RIBOSOME, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.NISHIMURA,T.YOSHIDA,M.SHIROUZU,T.TERADA,S.KURAMITSU,S.YOKOYAMA,
AUTHOR 2 T.OHKUBO,Y.KOBAYASHI,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 3 (RSGI)
REVDAT 3 13-JUL-11 1WKI 1 VERSN
REVDAT 2 24-FEB-09 1WKI 1 VERSN
REVDAT 1 14-DEC-04 1WKI 0
JRNL AUTH M.NISHIMURA,T.YOSHIDA,M.SHIROUZU,T.TERADA,S.KURAMITSU,
JRNL AUTH 2 S.YOKOYAMA,T.OHKUBO,Y.KOBAYASHI
JRNL TITL SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L16 FROM THERMUS
JRNL TITL 2 THERMOPHILUS HB8
JRNL REF J.MOL.BIOL. V. 344 1369 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15561149
JRNL DOI 10.1016/J.JMB.2004.10.011
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURE ARE BASED ON A TOTAL OF 2590 RESTRAINTS,
REMARK 3 2364 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 162 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, 64 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1WKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-04.
REMARK 100 THE RCSB ID CODE IS RCSB023675.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.4
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM L16 U-15N, 13C; 0.5MM L16
REMARK 210 U-15N, 13C; 0.5MM L16 U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; TRIPLE
REMARK 210 RESONANCE EXPERIMENTS FOR
REMARK 210 ASSIGNMENTS; 3D_13C-SEPARATED_
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 700
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 O TYR A 26 HH TYR A 137 1.59
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 PRO A 4 171.23 -51.78
REMARK 500 1 ARG A 6 -44.45 -157.43
REMARK 500 1 ARG A 14 160.69 60.62
REMARK 500 1 VAL A 27 -68.14 -161.60
REMARK 500 1 ALA A 28 118.01 61.72
REMARK 500 1 PHE A 29 142.45 62.30
REMARK 500 1 PHE A 58 98.86 -52.71
REMARK 500 1 ASP A 71 -46.94 -140.26
REMARK 500 1 LYS A 76 31.35 -98.73
REMARK 500 1 GLU A 80 33.43 -167.71
REMARK 500 1 LYS A 87 128.94 -176.14
REMARK 500 1 GLU A 91 46.44 -93.72
REMARK 500 1 ARG A 134 89.71 -47.04
REMARK 500 2 ARG A 5 113.12 59.27
REMARK 500 2 TYR A 9 44.46 -153.12
REMARK 500 2 ARG A 14 46.13 -94.42
REMARK 500 2 LEU A 17 85.03 -165.87
REMARK 500 2 VAL A 27 -41.64 -164.79
REMARK 500 2 ALA A 28 -73.82 74.84
REMARK 500 2 PHE A 58 108.84 -53.43
REMARK 500 2 ARG A 60 32.96 -98.21
REMARK 500 2 LYS A 87 -45.76 -149.00
REMARK 500 2 GLU A 91 43.59 -94.65
REMARK 500 2 ARG A 134 90.05 -47.40
REMARK 500 3 LEU A 2 99.25 59.47
REMARK 500 3 ARG A 6 32.38 -140.35
REMARK 500 3 LYS A 11 33.71 -98.99
REMARK 500 3 TYR A 26 -75.60 -83.53
REMARK 500 3 VAL A 27 -83.12 -157.36
REMARK 500 3 ALA A 28 -173.56 50.29
REMARK 500 3 PHE A 29 -78.88 64.71
REMARK 500 3 PHE A 58 106.14 -48.10
REMARK 500 3 GLU A 80 84.50 60.14
REMARK 500 3 LYS A 87 118.68 -162.77
REMARK 500 3 GLU A 91 46.17 -93.80
REMARK 500 3 ARG A 134 3.12 -56.88
REMARK 500 3 ASP A 135 26.44 -164.12
REMARK 500 4 LEU A 2 82.64 -160.33
REMARK 500 4 ARG A 5 96.40 61.17
REMARK 500 4 ARG A 6 89.17 -164.47
REMARK 500 4 LYS A 8 117.62 62.26
REMARK 500 4 ARG A 14 -76.28 -77.49
REMARK 500 4 LYS A 22 178.49 65.42
REMARK 500 4 ALA A 28 -72.20 -91.79
REMARK 500 4 PHE A 29 -56.04 -138.59
REMARK 500 4 PHE A 58 103.91 -52.48
REMARK 500 4 GLU A 80 75.75 60.64
REMARK 500 4 GLU A 91 52.00 -90.67
REMARK 500 4 ARG A 134 89.56 -46.84
REMARK 500 5 TYR A 9 35.11 -165.42
REMARK 500
REMARK 500 THIS ENTRY HAS 394 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TTK003000816.1 RELATED DB: TARGETDB
DBREF 1WKI A 1 141 UNP P60489 RL16_THET8 1 141
SEQRES 1 A 141 MET LEU MET PRO ARG ARG MET LYS TYR ARG LYS GLN GLN
SEQRES 2 A 141 ARG GLY ARG LEU LYS GLY ALA THR LYS GLY GLY ASP TYR
SEQRES 3 A 141 VAL ALA PHE GLY ASP TYR GLY LEU VAL ALA LEU GLU PRO
SEQRES 4 A 141 ALA TRP ILE THR ALA GLN GLN ILE GLU ALA ALA ARG VAL
SEQRES 5 A 141 ALA MET VAL ARG HIS PHE ARG ARG GLY GLY LYS ILE PHE
SEQRES 6 A 141 ILE ARG ILE PHE PRO ASP LYS PRO TYR THR LYS LYS PRO
SEQRES 7 A 141 LEU GLU VAL ARG MET GLY LYS GLY LYS GLY ASN VAL GLU
SEQRES 8 A 141 GLY TYR VAL ALA VAL VAL LYS PRO GLY ARG VAL MET PHE
SEQRES 9 A 141 GLU VAL ALA GLY VAL THR GLU GLU GLN ALA MET GLU ALA
SEQRES 10 A 141 LEU ARG ILE ALA GLY HIS LYS LEU PRO ILE LYS THR LYS
SEQRES 11 A 141 ILE VAL ARG ARG ASP ALA TYR ASP GLU ALA GLN
HELIX 1 1 ALA A 44 HIS A 57 1 14
HELIX 2 2 GLU A 111 LYS A 124 1 14
SHEET 1 A 4 LYS A 63 PHE A 65 0
SHEET 2 A 4 PHE A 104 ALA A 107 -1 O ALA A 107 N LYS A 63
SHEET 3 A 4 TYR A 32 ALA A 36 -1 N PHE A 104 O LEU A 34
SHEET 4 A 4 THR A 129 ARG A 133 -1 O ARG A 133 N TYR A 32
SHEET 1 B 3 THR A 129 ARG A 133 0
SHEET 2 B 3 TYR A 32 ALA A 36 -1 O ALA A 36 N THR A 129
SHEET 3 B 3 ARG A 101 VAL A 102 -1 N ARG A 101 O ALA A 36
SHEET 1 C 3 ALA A 40 THR A 43 0
SHEET 2 C 3 GLY A 92 VAL A 97 -1 O VAL A 97 N ALA A 40
SHEET 3 C 3 LYS A 72 TYR A 74 -1 N LYS A 72 O VAL A 94
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 - r 25 2 Bytes