Header list of 1ge9.pdb file
Complete list - b 23 2 Bytes
HEADER RIBOSOME 19-OCT-00 1GE9
TITLE SOLUTION STRUCTURE OF THE RIBOSOME RECYCLING FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOME RECYCLING FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS THREE-HELIX BUNDLE, RIBOSOME
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR T.YOSHIDA,S.UCHIYAMA,H.NAKANO,H.KASHIMORI,H.KIJIMA,T.OHSHIMA,
AUTHOR 2 Y.SAIHARA,T.ISHINO,T.SHIMAHARA,T.YOSHIDA,K.YOKOSE,T.OHKUBO,A.KAJI,
AUTHOR 3 Y.KOBAYASHI
REVDAT 5 23-FEB-22 1GE9 1 REMARK
REVDAT 4 24-FEB-09 1GE9 1 VERSN
REVDAT 3 01-APR-03 1GE9 1 JRNL
REVDAT 2 21-JAN-03 1GE9 1 REMARK
REVDAT 1 16-MAY-01 1GE9 0
JRNL AUTH T.YOSHIDA,S.UCHIYAMA,H.NAKANO,H.KASHIMORI,H.KIJIMA,
JRNL AUTH 2 T.OHSHIMA,Y.SAIHARA,T.ISHINO,H.SHIMAHARA,T.YOSHIDA,K.YOKOSE,
JRNL AUTH 3 T.OHKUBO,A.KAJI,Y.KOBAYASHI
JRNL TITL SOLUTION STRUCTURE OF THE RIBOSOME RECYCLING FACTOR FROM
JRNL TITL 2 AQUIFEX AEOLICUS.
JRNL REF BIOCHEMISTRY V. 40 2387 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11327859
JRNL DOI 10.1021/BI002474G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9, CNS 0.9
REMARK 3 AUTHORS : BRUNGER (CNS), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GE9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000005069.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM RIBOSOME RECYCLING FACTOR
REMARK 210 U-15N; 20MM ACETATE BUFFER, 20MM
REMARK 210 NACL; 93% D2O, 7% D2O; 0.5MM
REMARK 210 RIBOSOME RECYCLING FACTOR U-15N,
REMARK 210 13C; 20MM ACETATE BUFFER, 20MM
REMARK 210 NACL; 93% D2O, 7% D2O; 0.5MM
REMARK 210 RIBOSOME RECYCLING FACTOR U-15N,
REMARK 210 13C; 20MM ACETATE BUFFER, 20MM
REMARK 210 NACL; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 RELAXATION TIME MEASUREMENTS;
REMARK 210 TRIPLE RESONANCE EXPERIMENTS FOR
REMARK 210 ASSIGNMENTS; QUANTITATIVE J
REMARK 210 CORRELATION FOR COUPLING
REMARK 210 CONSTANTS; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
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 LYS A 177 H ILE A 181 1.51
REMARK 500 O ILE A 81 H ILE A 85 1.58
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 3 -157.54 -130.32
REMARK 500 1 VAL A 40 -106.08 -80.77
REMARK 500 1 GLU A 41 -21.03 79.09
REMARK 500 1 ILE A 43 65.72 -66.84
REMARK 500 1 ILE A 54 37.97 -91.79
REMARK 500 1 THR A 59 135.08 -174.05
REMARK 500 1 HIS A 65 -57.54 68.73
REMARK 500 1 ASN A 98 20.07 -147.49
REMARK 500 1 LEU A 107 85.72 -63.75
REMARK 500 1 THR A 108 -169.05 -74.60
REMARK 500 1 GLU A 145 8.89 58.01
REMARK 500 2 LYS A 3 -50.78 -161.57
REMARK 500 2 ARG A 31 82.92 -61.47
REMARK 500 2 LEU A 39 -45.04 -22.93
REMARK 500 2 VAL A 40 -75.96 -77.55
REMARK 500 2 GLU A 41 -40.54 79.30
REMARK 500 2 ILE A 43 80.54 -53.29
REMARK 500 2 LYS A 44 87.01 -59.29
REMARK 500 2 ILE A 54 44.47 -94.33
REMARK 500 2 ASN A 98 23.17 -155.12
REMARK 500 2 GLU A 145 12.13 52.66
REMARK 500 3 LYS A 3 -74.27 -159.89
REMARK 500 3 ARG A 31 81.03 -61.51
REMARK 500 3 LEU A 39 -43.19 -28.93
REMARK 500 3 GLU A 41 -70.92 132.40
REMARK 500 3 GLU A 42 25.20 -161.56
REMARK 500 3 ILE A 43 46.35 28.46
REMARK 500 3 LYS A 44 94.80 -44.38
REMARK 500 3 LEU A 57 -53.16 -132.40
REMARK 500 3 ASN A 98 24.29 -156.74
REMARK 500 3 GLU A 145 -24.68 68.39
REMARK 500 3 SER A 183 -75.38 -77.24
REMARK 500 4 ARG A 31 85.17 -51.75
REMARK 500 4 LEU A 39 -48.29 -26.92
REMARK 500 4 ILE A 43 31.41 38.75
REMARK 500 4 LYS A 44 79.89 4.22
REMARK 500 4 ILE A 54 -100.88 -60.75
REMARK 500 4 LYS A 55 -60.53 67.34
REMARK 500 4 HIS A 65 39.34 -69.99
REMARK 500 4 VAL A 72 -172.01 -63.13
REMARK 500 4 ASN A 98 23.43 -152.81
REMARK 500 4 GLU A 145 10.52 54.21
REMARK 500 4 SER A 183 -79.67 -90.56
REMARK 500 5 LEU A 39 -49.00 -28.49
REMARK 500 5 VAL A 40 -106.33 -75.12
REMARK 500 5 GLU A 41 -21.72 79.33
REMARK 500 5 ILE A 54 33.09 -89.07
REMARK 500 5 HIS A 65 -56.25 66.62
REMARK 500 5 ASN A 98 18.50 -147.63
REMARK 500 5 LEU A 107 96.80 -48.01
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GE9 A 1 184 UNP O66928 RRF_AQUAE 1 184
SEQRES 1 A 184 MET ILE LYS GLU LEU GLU ASP ILE PHE LYS GLU ALA GLU
SEQRES 2 A 184 LYS ASP MET LYS LYS ALA VAL GLU TYR TYR LYS ASN GLU
SEQRES 3 A 184 ILE ALA GLY LEU ARG THR SER ARG ALA SER THR ALA LEU
SEQRES 4 A 184 VAL GLU GLU ILE LYS VAL GLU TYR TYR GLY SER LYS VAL
SEQRES 5 A 184 PRO ILE LYS GLN LEU GLY THR ILE SER VAL PRO GLU HIS
SEQRES 6 A 184 ASN GLN ILE VAL ILE GLN VAL TRP ASP GLN ASN ALA VAL
SEQRES 7 A 184 PRO ALA ILE GLU LYS ALA ILE ARG GLU GLU LEU ASN LEU
SEQRES 8 A 184 ASN PRO THR VAL GLN GLY ASN VAL ILE ARG VAL THR LEU
SEQRES 9 A 184 PRO PRO LEU THR GLU GLU ARG ARG ARG GLU LEU VAL ARG
SEQRES 10 A 184 LEU LEU HIS LYS ILE THR GLU GLU ALA ARG VAL ARG VAL
SEQRES 11 A 184 ARG ASN VAL ARG ARG GLU ALA LYS GLU MET ILE GLU GLU
SEQRES 12 A 184 LEU GLU GLY ILE SER GLU ASP GLU LYS LYS ARG ALA LEU
SEQRES 13 A 184 GLU ARG LEU GLN LYS LEU THR ASP LYS TYR ILE ASP GLU
SEQRES 14 A 184 ILE ASN LYS LEU MET GLU ALA LYS GLU LYS GLU ILE MET
SEQRES 15 A 184 SER VAL
HELIX 1 1 GLU A 4 LEU A 30 1 27
HELIX 2 2 ASN A 76 ASN A 90 1 15
HELIX 3 3 THR A 108 LEU A 144 1 37
HELIX 4 4 SER A 148 MET A 182 1 35
SHEET 1 A 2 VAL A 45 GLU A 46 0
SHEET 2 A 2 LYS A 51 VAL A 52 -1 O VAL A 52 N VAL A 45
SHEET 1 B 4 THR A 59 SER A 61 0
SHEET 2 B 4 GLN A 67 GLN A 71 -1 O VAL A 69 N SER A 61
SHEET 3 B 4 VAL A 99 THR A 103 -1 N ILE A 100 O ILE A 70
SHEET 4 B 4 THR A 94 GLN A 96 -1 N THR A 94 O ARG A 101
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