Header list of 1pc0.pdb file
Complete list - 23 20 Bytes
HEADER RNA BINDING PROTEIN 15-MAY-03 1PC0
TITLE NMR STRUCTURE OF THE ARCHAEAL HOMOLOGUE OF RNASE P PROTEIN RPP29
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN AF1917;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUE 17-77;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: AF1917;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMAL-C2T
KEYWDS SANDWICH, BETA-SHEET, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.J.SIDOTE,D.W.HOFFMAN
REVDAT 3 23-FEB-22 1PC0 1 REMARK
REVDAT 2 24-FEB-09 1PC0 1 VERSN
REVDAT 1 09-DEC-03 1PC0 0
JRNL AUTH D.J.SIDOTE,D.W.HOFFMAN
JRNL TITL NMR STRUCTURE OF AN ARCHAEAL HOMOLOGUE OF RIBONUCLEASE P
JRNL TITL 2 PROTEIN RPP29
JRNL REF BIOCHEMISTRY V. 42 13541 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14622001
JRNL DOI 10.1021/BI030170Z
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER, A. T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 651 RESTRAINTS, 554 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 70 DIHEDRAL ANGLE RESTRAINTS,27 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1PC0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019222.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 5.8; 3.0
REMARK 210 IONIC STRENGTH : 100MM; 100MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM RPP29 U-15N;10MM
REMARK 210 POSTASSIUM PHOSPHATE PH 5.8
REMARK 210 100MM SODIUM CHLORIDE 10MM
REMARK 210 SODIUM AZIDE; 1.8 MM RPP29 U-15N;
REMARK 210 10MM POSTASSIUM PHOSPHATE PH 3.0
REMARK 210 100MM SODIUM CHLORIDE 10MM
REMARK 210 SODIUM AZIDE; 1.8 MM RPP29 U-15N;
REMARK 210 U-13C; 10MM POSTASSIUM
REMARK 210 PHOSPHATE PH 5.8 100MM SODIUM
REMARK 210 CHLORIDE 10MM SODIUM AZIDE; 1.8
REMARK 210 MM RPP29; 10MM POSTASSIUM
REMARK 210 PHOSPHATE PH 5.8 100MM SODIUM
REMARK 210 CHLORIDE 10MM SODIUM AZIDE; 1.8
REMARK 210 MM RPP29; 10MM POSTASSIUM
REMARK 210 PHOSPHATE PH 3.0 100MM SODIUM
REMARK 210 CHLORIDE 10MM SODIUM AZIDE; 1.8
REMARK 210 MM RPP29; 10MM POSTASSIUM
REMARK 210 PHOSPHATE PH 5.8 100MM SODIUM
REMARK 210 CHLORIDE 10MM SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 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 : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES.
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 SER A 25 133.09 89.90
REMARK 500 1 PRO A 26 82.43 -54.37
REMARK 500 1 ASN A 27 157.39 177.77
REMARK 500 1 SER A 29 55.03 -177.43
REMARK 500 1 ASP A 39 73.84 71.16
REMARK 500 1 ASN A 43 -91.80 -149.60
REMARK 500 1 THR A 49 -88.75 -103.40
REMARK 500 1 GLU A 50 -53.01 -141.16
REMARK 500 1 LYS A 58 -33.44 -36.59
REMARK 500 1 ARG A 61 -175.16 54.41
REMARK 500 2 SER A 25 99.59 69.28
REMARK 500 2 ASN A 27 151.56 -36.78
REMARK 500 2 SER A 29 53.45 -94.60
REMARK 500 2 GLU A 30 171.19 -42.73
REMARK 500 2 THR A 41 40.95 -149.86
REMARK 500 2 ASN A 43 -66.26 -171.56
REMARK 500 2 THR A 49 -88.22 -107.09
REMARK 500 2 GLU A 50 -55.61 -138.63
REMARK 500 2 LYS A 58 65.44 64.23
REMARK 500 2 ARG A 59 177.43 65.01
REMARK 500 2 ARG A 61 -163.34 -58.68
REMARK 500 2 LYS A 68 66.42 -69.44
REMARK 500 3 SER A 25 103.63 66.85
REMARK 500 3 ASN A 27 156.51 -37.45
REMARK 500 3 GLU A 30 150.03 62.04
REMARK 500 3 GLU A 40 -77.01 -43.17
REMARK 500 3 GLN A 42 63.72 60.43
REMARK 500 3 ASN A 43 -61.77 179.46
REMARK 500 3 THR A 49 -92.72 -131.23
REMARK 500 3 GLU A 50 -91.28 -90.39
REMARK 500 3 LYS A 68 66.58 -68.33
REMARK 500 4 SER A 25 107.41 75.84
REMARK 500 4 ASN A 27 159.89 -40.00
REMARK 500 4 GLU A 30 -171.77 45.60
REMARK 500 4 THR A 41 50.03 -162.16
REMARK 500 4 ASN A 43 -74.48 -175.76
REMARK 500 4 THR A 49 -89.22 -109.27
REMARK 500 4 GLU A 50 -59.86 -130.43
REMARK 500 4 LYS A 51 -8.01 -59.27
REMARK 500 4 LYS A 58 -31.45 -39.36
REMARK 500 4 ARG A 61 -172.02 56.17
REMARK 500 5 SER A 25 120.34 61.87
REMARK 500 5 ASN A 27 168.96 -46.28
REMARK 500 5 GLU A 30 171.80 61.11
REMARK 500 5 THR A 41 45.35 -163.70
REMARK 500 5 ASN A 43 -65.31 -172.10
REMARK 500 5 THR A 49 -114.62 -134.77
REMARK 500 5 GLU A 50 -89.90 -64.19
REMARK 500 5 LYS A 58 39.69 25.24
REMARK 500 5 ARG A 59 -168.26 178.46
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PC0 A 17 77 UNP O28362 RNP1_ARCFU 17 77
SEQRES 1 A 61 GLY LEU MET VAL GLU VAL VAL GLU SER PRO ASN HIS SER
SEQRES 2 A 61 GLU VAL GLY ILE LYS GLY GLU VAL VAL ASP GLU THR GLN
SEQRES 3 A 61 ASN THR LEU LYS ILE MET THR GLU LYS GLY LEU LYS VAL
SEQRES 4 A 61 VAL ALA LYS ARG GLY ARG THR PHE ARG VAL TRP TYR LYS
SEQRES 5 A 61 GLY LYS ILE MET ARG ILE LYS GLY ASP
SHEET 1 A 6 LEU A 53 VAL A 56 0
SHEET 2 A 6 LEU A 45 MET A 48 -1 N LEU A 45 O VAL A 56
SHEET 3 A 6 VAL A 31 VAL A 38 -1 N VAL A 38 O LYS A 46
SHEET 4 A 6 MET A 19 GLU A 24 -1 N VAL A 20 O GLY A 35
SHEET 5 A 6 THR A 62 TRP A 66 -1 O ARG A 64 N GLU A 21
SHEET 6 A 6 ILE A 71 LYS A 75 -1 O ILE A 74 N PHE A 63
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 - 23 20 Bytes