Header list of 2cqm.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSLATION 20-MAY-05 2CQM
TITLE SOLUTION STRUCTURE OF THE MITOCHONDRIAL RIBOSOMAL PROTEIN L17 ISOLOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL PROTEIN L17 ISOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MITOCHONDRIAL RIBOSOMAL PROTEIN L17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MRPL17;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040315-54;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ALPHA AND BETA (A+B), STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT
KEYWDS 2 ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CQM 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQM 1 VERSN
REVDAT 1 20-NOV-05 2CQM 0
JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE MITOCHONDRIAL RIBOSOMAL PROTEIN
JRNL TITL 2 L17 ISOLOG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CQM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024513.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL; 200MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, OLIVIA 1.10.5,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 GLU A 40 25.01 40.31
REMARK 500 1 ARG A 41 131.43 -175.97
REMARK 500 1 ASP A 67 41.45 -80.87
REMARK 500 1 GLU A 82 102.57 -41.70
REMARK 500 1 VAL A 92 -72.93 -131.32
REMARK 500 1 GLN A 100 158.09 -39.79
REMARK 500 1 LYS A 126 78.50 -64.93
REMARK 500 1 PRO A 132 -179.52 -69.78
REMARK 500 2 SER A 26 84.15 -61.96
REMARK 500 2 GLU A 40 25.13 39.80
REMARK 500 2 ARG A 41 130.61 -176.97
REMARK 500 2 ASP A 67 41.98 -81.02
REMARK 500 2 GLU A 82 107.95 -52.64
REMARK 500 2 VAL A 92 -73.95 -127.37
REMARK 500 2 LEU A 115 156.35 -49.75
REMARK 500 2 ASP A 116 149.90 -34.42
REMARK 500 2 SER A 140 97.58 -64.45
REMARK 500 3 GLU A 40 25.52 38.60
REMARK 500 3 ARG A 41 131.43 -177.91
REMARK 500 3 ASP A 67 38.83 -82.40
REMARK 500 3 VAL A 92 -71.56 -128.13
REMARK 500 3 PRO A 111 -178.96 -69.74
REMARK 500 3 LYS A 119 103.99 -48.22
REMARK 500 3 LYS A 126 77.76 -63.99
REMARK 500 4 GLU A 40 25.05 39.45
REMARK 500 4 ARG A 41 131.56 -179.44
REMARK 500 4 VAL A 92 -68.59 -130.34
REMARK 500 4 SER A 114 161.58 -46.98
REMARK 500 4 ALA A 118 115.14 -161.14
REMARK 500 4 LYS A 119 82.36 -66.92
REMARK 500 4 LYS A 126 75.62 -60.42
REMARK 500 4 SER A 137 142.08 -171.56
REMARK 500 5 SER A 22 42.10 -98.92
REMARK 500 5 GLU A 40 24.93 39.85
REMARK 500 5 ARG A 41 131.43 -177.66
REMARK 500 5 ASP A 67 42.52 -80.42
REMARK 500 5 VAL A 92 -74.75 -132.63
REMARK 500 5 TYR A 97 37.09 -97.36
REMARK 500 5 PRO A 111 -176.46 -69.78
REMARK 500 5 LEU A 135 160.68 -41.92
REMARK 500 5 PRO A 136 2.12 -69.83
REMARK 500 5 PRO A 139 -179.66 -69.78
REMARK 500 6 SER A 25 41.08 -97.83
REMARK 500 6 GLU A 40 25.04 39.53
REMARK 500 6 ARG A 41 130.76 -178.00
REMARK 500 6 ASP A 67 39.70 -81.44
REMARK 500 6 VAL A 92 -74.61 -131.33
REMARK 500 6 GLN A 100 132.61 -34.20
REMARK 500 6 LYS A 119 83.98 -68.13
REMARK 500 7 SER A 25 -60.95 -95.76
REMARK 500
REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000109.1 RELATED DB: TARGETDB
DBREF 2CQM A 28 136 UNP Q9NRX2 Q9NRX2_HUMAN 28 136
SEQADV 2CQM GLY A 21 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 22 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 23 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM GLY A 24 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 25 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 26 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM GLY A 27 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 137 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM GLY A 138 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM PRO A 139 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 140 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM SER A 141 UNP Q9NRX2 CLONING ARTIFACT
SEQADV 2CQM GLY A 142 UNP Q9NRX2 CLONING ARTIFACT
SEQRES 1 A 122 GLY SER SER GLY SER SER GLY LEU LEU ARG ASN LEU LEU
SEQRES 2 A 122 THR GLY LEU VAL ARG HIS GLU ARG ILE GLU ALA PRO TRP
SEQRES 3 A 122 ALA ARG VAL ASP GLU MET ARG GLY TYR ALA GLU LYS LEU
SEQRES 4 A 122 ILE ASP TYR GLY LYS LEU GLY ASP THR ASN GLU ARG ALA
SEQRES 5 A 122 MET ARG MET ALA ASP PHE TRP LEU THR GLU LYS ASP LEU
SEQRES 6 A 122 ILE PRO LYS LEU PHE GLN VAL LEU ALA PRO ARG TYR LYS
SEQRES 7 A 122 ASP GLN THR GLY GLY TYR THR ARG MET LEU GLN ILE PRO
SEQRES 8 A 122 ASN ARG SER LEU ASP ARG ALA LYS MET ALA VAL ILE GLU
SEQRES 9 A 122 TYR LYS GLY ASN CYS LEU PRO PRO LEU PRO LEU PRO SER
SEQRES 10 A 122 GLY PRO SER SER GLY
HELIX 1 1 LEU A 28 ARG A 38 1 11
HELIX 2 2 TRP A 46 LEU A 65 1 20
HELIX 3 3 GLU A 70 TRP A 79 1 10
HELIX 4 4 LYS A 83 GLN A 91 1 9
HELIX 5 5 LEU A 93 ARG A 96 1 4
SHEET 1 A 3 ARG A 41 ALA A 44 0
SHEET 2 A 3 ALA A 121 TYR A 125 -1 O ALA A 121 N ALA A 44
SHEET 3 A 3 THR A 105 GLN A 109 -1 N LEU A 108 O VAL A 122
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 9 2 Bytes