Header list of 1slj.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 05-MAR-04 1SLJ
TITLE SOLUTION STRUCTURE OF THE S1 DOMAIN OF RNASE E FROM E. COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE E;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: S1 DOMAIN;
COMPND 5 SYNONYM: RNASE E;
COMPND 6 EC: 3.1.4.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: RNE, AMS, HMP1, B1084;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS OB-FOLD, RNA-BINDING, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.SCHUBERT,R.E.EDGE,P.LARIO,M.A.COOK,N.C.J.STRYNADKA,G.A.MACKIE,
AUTHOR 2 L.P.MCINTOSH
REVDAT 3 02-MAR-22 1SLJ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SLJ 1 VERSN
REVDAT 1 17-AUG-04 1SLJ 0
JRNL AUTH M.SCHUBERT,R.E.EDGE,P.LARIO,M.A.COOK,N.C.STRYNADKA,
JRNL AUTH 2 G.A.MACKIE,L.P.MCINTOSH
JRNL TITL STRUCTURAL CHARACTERIZATION OF THE RNASE E S1 DOMAIN AND
JRNL TITL 2 IDENTIFICATION OF ITS OLIGONUCLEOTIDE-BINDING AND
JRNL TITL 3 DIMERIZATION INTERFACES.
JRNL REF J.MOL.BIOL. V. 341 37 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15312761
JRNL DOI 10.1016/J.JMB.2004.05.061
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA/CNS
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), LINGE (ARIA/CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2884 RESTRAINTS, INCLUDING
REMARK 3 2113 UNAMBIGUOUS AND 597 AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 159 DIHEDRAL ANGLE RESTRAINTS, 15 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1SLJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021813.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 75MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM RNASE E S1 U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER; 50MM NACL; 92%
REMARK 210 H2O, 8% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C_15N/13C-
REMARK 210 SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY_AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY
REMARK 210 METHOD USED : SIMULATED 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 : 4
REMARK 210
REMARK 210 REMARK: A MIXING TIME OF 100MS WAS USED.
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 HB2 GLU A 76 H ALA A 123 1.13
REMARK 500 HG21 ILE A 46 HD13 ILE A 49 1.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 5 TYR A 77 CE1 TYR A 77 CZ -0.085
REMARK 500 5 TYR A 77 CZ TYR A 77 CE2 0.110
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 HIS A 32 68.35 -154.54
REMARK 500 1 LEU A 34 -105.16 61.81
REMARK 500 1 GLU A 35 -174.40 -173.16
REMARK 500 1 HIS A 65 141.50 63.84
REMARK 500 1 PRO A 79 141.76 -39.13
REMARK 500 1 ARG A 109 12.13 -144.10
REMARK 500 1 ASN A 111 -31.04 -130.50
REMARK 500 1 PHE A 119 46.93 -81.07
REMARK 500 1 ALA A 123 80.43 72.29
REMARK 500 2 HIS A 32 -17.70 69.85
REMARK 500 2 GLN A 36 -58.00 69.65
REMARK 500 2 LYS A 37 -17.92 -142.89
REMARK 500 2 ASN A 40 109.52 -50.66
REMARK 500 2 GLU A 54 58.01 39.87
REMARK 500 2 HIS A 65 146.77 68.59
REMARK 500 2 PRO A 79 135.45 -37.97
REMARK 500 2 ALA A 80 -7.19 -56.51
REMARK 500 2 VAL A 93 -51.91 -120.30
REMARK 500 2 GLU A 108 90.87 -66.85
REMARK 500 2 PHE A 119 47.06 -78.40
REMARK 500 2 ALA A 123 -173.89 158.34
REMARK 500 3 SER A 31 -74.33 -50.54
REMARK 500 3 LEU A 34 -94.84 -79.38
REMARK 500 3 GLU A 35 16.89 -143.94
REMARK 500 3 ASN A 40 91.57 -66.28
REMARK 500 3 HIS A 65 -159.77 61.28
REMARK 500 3 ALA A 80 -16.98 -48.99
REMARK 500 3 VAL A 93 -54.86 -121.94
REMARK 500 3 ARG A 109 18.91 -143.98
REMARK 500 3 SER A 121 19.75 -66.85
REMARK 500 3 ALA A 123 61.54 158.44
REMARK 500 4 HIS A 65 144.37 70.34
REMARK 500 4 PRO A 79 137.12 -26.72
REMARK 500 4 ARG A 109 -82.71 -105.53
REMARK 500 4 PHE A 119 44.45 -78.15
REMARK 500 4 ALA A 123 56.21 76.94
REMARK 500 5 HIS A 32 52.24 -99.26
REMARK 500 5 GLN A 36 74.02 65.35
REMARK 500 5 HIS A 65 143.28 71.25
REMARK 500 5 PRO A 79 143.65 -39.08
REMARK 500 5 ALA A 80 -7.35 -58.95
REMARK 500 5 PHE A 119 45.03 -80.25
REMARK 500 5 SER A 121 33.48 -85.03
REMARK 500 5 ALA A 123 37.67 -161.66
REMARK 500 6 HIS A 32 47.72 -152.02
REMARK 500 6 LEU A 34 -74.38 -128.48
REMARK 500 6 GLU A 54 60.23 39.23
REMARK 500 6 PRO A 79 138.02 -38.65
REMARK 500 6 VAL A 93 -54.77 -122.50
REMARK 500 6 ARG A 109 49.28 -146.65
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 5 TYR A 77 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SMX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE S1 DOMAIN OF RNASE E FROM E. COLI (NATIVE)
REMARK 900 RELATED ID: 1SN8 RELATED DB: PDB
DBREF 1SLJ A 35 125 UNP P21513 RNE_ECOLI 35 125
SEQADV 1SLJ GLY A 30 UNP P21513 CLONING ARTIFACT
SEQADV 1SLJ SER A 31 UNP P21513 CLONING ARTIFACT
SEQADV 1SLJ HIS A 32 UNP P21513 CLONING ARTIFACT
SEQADV 1SLJ MET A 33 UNP P21513 CLONING ARTIFACT
SEQADV 1SLJ LEU A 34 UNP P21513 CLONING ARTIFACT
SEQRES 1 A 96 GLY SER HIS MET LEU GLU GLN LYS LYS ALA ASN ILE TYR
SEQRES 2 A 96 LYS GLY LYS ILE THR ARG ILE GLU PRO SER LEU GLU ALA
SEQRES 3 A 96 ALA PHE VAL ASP TYR GLY ALA GLU ARG HIS GLY PHE LEU
SEQRES 4 A 96 PRO LEU LYS GLU ILE ALA ARG GLU TYR PHE PRO ALA ASN
SEQRES 5 A 96 TYR SER ALA HIS GLY ARG PRO ASN ILE LYS ASP VAL LEU
SEQRES 6 A 96 ARG GLU GLY GLN GLU VAL ILE VAL GLN ILE ASP LYS GLU
SEQRES 7 A 96 GLU ARG GLY ASN LYS GLY ALA ALA LEU THR THR PHE ILE
SEQRES 8 A 96 SER LEU ALA GLY SER
HELIX 1 1 LYS A 71 ILE A 73 5 3
HELIX 2 2 ASN A 89 VAL A 93 5 5
SHEET 1 A 6 GLU A 99 VAL A 102 0
SHEET 2 A 6 TYR A 42 ILE A 49 -1 N TYR A 42 O VAL A 102
SHEET 3 A 6 ALA A 55 ASP A 59 -1 O PHE A 57 N THR A 47
SHEET 4 A 6 GLY A 66 PRO A 69 -1 O LEU A 68 N ALA A 56
SHEET 5 A 6 ALA A 114 LEU A 116 1 O ALA A 114 N PHE A 67
SHEET 6 A 6 ILE A 104 LYS A 106 -1 N LYS A 106 O ALA A 115
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 2 2 Bytes