Header list of 1d6t.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 15-OCT-99 1D6T
TITLE RNASE P PROTEIN FROM STAPHYLOCOCCUS AUREUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE P;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNASE P PROTEIN;
COMPND 5 EC: 3.1.26.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS ENDONUCLEASE, RNASE, SUBUNIT, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.SPITZFADEN
REVDAT 4 16-FEB-22 1D6T 1 REMARK
REVDAT 3 24-FEB-09 1D6T 1 VERSN
REVDAT 2 27-OCT-00 1D6T 1 DBREF
REVDAT 1 18-OCT-00 1D6T 0
JRNL AUTH C.SPITZFADEN,N.NICHOLSON,J.J.JONES,S.GUTH,R.LEHR,
JRNL AUTH 2 C.D.PRESCOTT,L.A.HEGG,D.S.EGGLESTON
JRNL TITL THE STRUCTURE OF RIBONUCLEASE P PROTEIN FROM STAPHYLOCOCCUS
JRNL TITL 2 AUREUS REVEALS A UNIQUE BINDING SITE FOR SINGLE-STRANDED
JRNL TITL 3 RNA.
JRNL REF J.MOL.BIOL. V. 295 105 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10623511
JRNL DOI 10.1006/JMBI.1999.3341
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1D6T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000009845.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1.5MM RNASEP PROTEIN, U-15N,13C,
REMARK 210 PH 6.0, (500MM SODIUM CHLORIDE,
REMARK 210 20MM SODIUM ACETATE, 20MM SODIUM
REMARK 210 PHOSPHATE)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 TYR A 7 OH
REMARK 470 ARG A 8 NH1 NH2
REMARK 470 ARG A 17 NH1 NH2
REMARK 470 TYR A 19 OH
REMARK 470 ARG A 28 NH1 NH2
REMARK 470 TYR A 33 OH
REMARK 470 ARG A 44 NH1 NH2
REMARK 470 ARG A 59 NH1 NH2
REMARK 470 ARG A 64 NH1 NH2
REMARK 470 ARG A 67 NH1 NH2
REMARK 470 ARG A 87 NH1 NH2
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
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 GLU A 4 -146.57 -120.01
REMARK 500 1 ARG A 17 -73.47 -42.55
REMARK 500 1 LYS A 20 -79.21 -75.19
REMARK 500 1 VAL A 25 -142.90 -128.89
REMARK 500 1 ALA A 26 128.68 160.38
REMARK 500 1 ASN A 27 -87.87 -87.78
REMARK 500 1 GLN A 29 13.15 -140.39
REMARK 500 1 ASN A 36 95.04 48.75
REMARK 500 1 ASN A 37 -37.86 -38.76
REMARK 500 1 LYS A 38 73.78 -169.81
REMARK 500 1 ASP A 41 13.43 -146.85
REMARK 500 1 PHE A 43 88.82 -67.54
REMARK 500 1 ARG A 44 93.66 -51.70
REMARK 500 1 LEU A 53 -73.04 -35.95
REMARK 500 1 LYS A 80 49.27 159.64
REMARK 500 1 ASP A 81 111.17 34.80
REMARK 500 1 GLN A 88 -52.00 171.47
REMARK 500 1 HIS A 104 -77.60 -134.99
REMARK 500 1 LYS A 110 23.95 87.80
REMARK 500 1 LYS A 114 -43.20 -157.88
REMARK 500 1 LYS A 115 98.04 95.34
REMARK 500 2 GLU A 4 -156.86 -115.46
REMARK 500 2 TYR A 7 -33.97 -36.45
REMARK 500 2 ARG A 8 -169.01 -112.35
REMARK 500 2 LYS A 20 -87.47 -73.74
REMARK 500 2 VAL A 25 -144.47 -123.41
REMARK 500 2 ALA A 26 131.23 160.81
REMARK 500 2 ASN A 27 -95.35 -89.06
REMARK 500 2 GLN A 29 23.99 -140.77
REMARK 500 2 ASN A 36 80.57 42.04
REMARK 500 2 GLU A 39 39.05 179.42
REMARK 500 2 HIS A 42 176.70 177.84
REMARK 500 2 ARG A 44 125.41 -34.85
REMARK 500 2 LEU A 53 -75.56 -40.25
REMARK 500 2 ALA A 79 126.06 -39.16
REMARK 500 2 LYS A 80 110.62 162.26
REMARK 500 2 ARG A 87 -167.57 -52.87
REMARK 500 2 HIS A 104 -75.95 -133.90
REMARK 500 2 LYS A 110 17.14 88.56
REMARK 500 2 ASN A 113 -39.14 -37.40
REMARK 500 2 LYS A 114 -86.53 -159.82
REMARK 500 2 LYS A 115 88.71 179.50
REMARK 500 3 LEU A 2 -45.92 86.40
REMARK 500 3 GLU A 4 -160.75 -78.17
REMARK 500 3 LYS A 10 -34.11 174.52
REMARK 500 3 ARG A 17 -75.01 -41.68
REMARK 500 3 LYS A 20 -80.08 -72.96
REMARK 500 3 ASN A 27 -96.85 -74.20
REMARK 500 3 GLN A 29 50.13 -144.11
REMARK 500 3 PHE A 30 143.09 177.89
REMARK 500
REMARK 500 THIS ENTRY HAS 454 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D6T A 1 117 UNP P0A0H5 RNPA_STAAU 1 117
SEQRES 1 A 117 MET LEU LEU GLU LYS ALA TYR ARG ILE LYS LYS ASN ALA
SEQRES 2 A 117 ASP PHE GLN ARG ILE TYR LYS LYS GLY HIS SER VAL ALA
SEQRES 3 A 117 ASN ARG GLN PHE VAL VAL TYR THR CYS ASN ASN LYS GLU
SEQRES 4 A 117 ILE ASP HIS PHE ARG LEU GLY ILE SER VAL SER LYS LYS
SEQRES 5 A 117 LEU GLY ASN ALA VAL LEU ARG ASN LYS ILE LYS ARG ALA
SEQRES 6 A 117 ILE ARG GLU ASN PHE LYS VAL HIS LYS SER HIS ILE LEU
SEQRES 7 A 117 ALA LYS ASP ILE ILE VAL ILE ALA ARG GLN PRO ALA LYS
SEQRES 8 A 117 ASP MET THR THR LEU GLN ILE GLN ASN SER LEU GLU HIS
SEQRES 9 A 117 VAL LEU LYS ILE ALA LYS VAL PHE ASN LYS LYS ILE LYS
HELIX 1 1 GLU A 4 TYR A 7 5 4
HELIX 2 2 ASN A 12 GLY A 22 1 11
HELIX 3 3 VAL A 57 HIS A 73 1 17
HELIX 4 4 LYS A 74 HIS A 76 5 3
HELIX 5 5 GLN A 88 MET A 93 5 6
HELIX 6 6 LEU A 96 GLU A 103 1 8
HELIX 7 7 HIS A 104 LYS A 110 1 7
SHEET 1 A 2 HIS A 23 SER A 24 0
SHEET 2 A 2 TYR A 33 THR A 34 -1 O THR A 34 N HIS A 23
SHEET 1 B 3 PHE A 30 VAL A 31 0
SHEET 2 B 3 ILE A 82 ALA A 86 -1 N ILE A 85 O VAL A 31
SHEET 3 B 3 LEU A 45 SER A 48 1 O GLY A 46 N VAL A 84
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 16 2 Bytes