Header list of 1emw.pdb file
Complete list - b 16 2 Bytes
HEADER RIBOSOME 20-MAR-00 1EMW
TITLE SOLUTION STRUCTURE OF THE RIBOSOMAL PROTEIN S16 FROM THERMUS
TITLE 2 THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S16 RIBOSOMAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS MIXED ALPHA/BETA PROTEIN, RIBOSOME
EXPDTA SOLUTION NMR
NUMMDL 47
AUTHOR P.ALLARD,A.V.RAK,B.T.WIMBERLY,W.M.CLEMONS JR.,A.KALININ,M.HELGSTRAND,
AUTHOR 2 M.B.GARBER,V.RAMAKRISHNAN,T.HARD
REVDAT 3 16-FEB-22 1EMW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1EMW 1 VERSN
REVDAT 1 09-AUG-00 1EMW 0
JRNL AUTH P.ALLARD,A.V.RAK,B.T.WIMBERLY,W.M.CLEMONS JR.,A.KALININ,
JRNL AUTH 2 M.HELGSTRAND,M.B.GARBER,V.RAMAKRISHNAN,T.HARD
JRNL TITL ANOTHER PIECE OF THE RIBOSOME: SOLUTION STRUCTURE OF S16 AND
JRNL TITL 2 ITS LOCATION IN THE 30S SUBUNIT.
JRNL REF STRUCTURE FOLD.DES. V. 8 875 2000
JRNL REFN ISSN 0969-2126
JRNL PMID 10997906
JRNL DOI 10.1016/S0969-2126(00)00177-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1283 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 47 DIHEDRAL ANGLE RESTRAINTS,31 DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS.
REMARK 4
REMARK 4 1EMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010733.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.2 M LICL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : S16; U-15N,13C; 50MM PHOSPHATE
REMARK 210 BUFFER; 200 MM LICL; 1.2 MM S16;
REMARK 210 U-15N; 50MM PHOSPHATE BUFFER;
REMARK 210 200 MM LICL; 1.6 MM S16; 50MM
REMARK 210 PHOSPHATE BUFFER; 200 MM LICL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, X-PLOR 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 47
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
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 HG1 THR A 22 O LYS A 31 1.59
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 12 40.86 -143.27
REMARK 500 1 HIS A 13 -64.65 -135.44
REMARK 500 1 ASP A 23 -161.53 -71.69
REMARK 500 1 LYS A 27 -55.02 -127.65
REMARK 500 1 LYS A 43 42.21 -96.97
REMARK 500 1 ASP A 47 58.86 -165.02
REMARK 500 1 ASP A 52 70.84 -100.04
REMARK 500 1 VAL A 53 -30.90 -34.93
REMARK 500 1 VAL A 62 32.70 -99.14
REMARK 500 1 ARG A 85 61.79 -111.02
REMARK 500 2 PHE A 9 -152.97 -119.08
REMARK 500 2 LYS A 12 51.06 -176.64
REMARK 500 2 HIS A 13 -51.41 -123.74
REMARK 500 2 HIS A 16 124.89 -174.94
REMARK 500 2 ASP A 23 -159.81 -78.60
REMARK 500 2 ALA A 24 46.12 -160.83
REMARK 500 2 ARG A 25 61.35 -173.88
REMARK 500 2 ARG A 26 148.30 -176.22
REMARK 500 2 ARG A 28 -60.64 -165.66
REMARK 500 2 ASP A 29 39.71 -92.73
REMARK 500 2 LYS A 31 95.53 -175.16
REMARK 500 2 TYR A 32 178.72 -55.56
REMARK 500 2 VAL A 53 -30.21 -35.73
REMARK 500 2 VAL A 62 32.25 -98.70
REMARK 500 2 ASP A 68 48.27 -83.82
REMARK 500 2 THR A 69 -56.59 -166.03
REMARK 500 2 VAL A 79 -66.91 -95.30
REMARK 500 3 PHE A 9 -151.95 -122.89
REMARK 500 3 LYS A 12 47.98 -179.35
REMARK 500 3 HIS A 13 -64.86 -124.40
REMARK 500 3 ALA A 24 43.21 -153.14
REMARK 500 3 ARG A 25 52.74 -163.53
REMARK 500 3 ARG A 28 104.77 -175.28
REMARK 500 3 THR A 44 -41.20 -145.14
REMARK 500 3 VAL A 53 -32.81 -32.72
REMARK 500 3 VAL A 62 32.61 -98.96
REMARK 500 3 THR A 67 171.73 -54.22
REMARK 500 3 THR A 69 -56.61 -167.25
REMARK 500 3 VAL A 79 -60.71 -98.95
REMARK 500 3 GLU A 86 69.56 -169.33
REMARK 500 4 VAL A 2 105.15 -53.82
REMARK 500 4 PHE A 9 -152.16 -120.38
REMARK 500 4 SER A 11 -81.80 -63.97
REMARK 500 4 LYS A 12 46.79 -145.50
REMARK 500 4 HIS A 13 -65.84 -134.81
REMARK 500 4 LYS A 27 -76.13 -63.59
REMARK 500 4 LYS A 43 43.87 -91.98
REMARK 500 4 THR A 44 -53.47 -133.36
REMARK 500 4 TRP A 48 -35.04 -175.22
REMARK 500 4 VAL A 53 -29.67 -36.47
REMARK 500
REMARK 500 THIS ENTRY HAS 587 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QD7 RELATED DB: PDB
REMARK 900 PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT
DBREF 1EMW A 1 67 UNP P80379 RS16_THETH 1 67
SEQADV 1EMW ARG A 5 UNP P80379 SER 5 CONFLICT
SEQADV 1EMW LEU A 6 UNP P80379 VAL 6 CONFLICT
SEQADV 1EMW ALA A 7 UNP P80379 SER 7 CONFLICT
SEQADV 1EMW ALA A 24 UNP P80379 VAL 24 CONFLICT
SEQADV 1EMW LYS A 31 UNP P80379 ALA 31 CONFLICT
SEQADV 1EMW ASP A 68 UNP P80379 SEE REMARK 999
SEQADV 1EMW THR A 69 UNP P80379 SEE REMARK 999
SEQADV 1EMW ALA A 70 UNP P80379 SEE REMARK 999
SEQADV 1EMW ARG A 71 UNP P80379 SEE REMARK 999
SEQADV 1EMW ARG A 72 UNP P80379 SEE REMARK 999
SEQADV 1EMW LEU A 73 UNP P80379 SEE REMARK 999
SEQADV 1EMW LEU A 74 UNP P80379 SEE REMARK 999
SEQADV 1EMW ARG A 75 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLN A 76 UNP P80379 SEE REMARK 999
SEQADV 1EMW ALA A 77 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLY A 78 UNP P80379 SEE REMARK 999
SEQADV 1EMW VAL A 79 UNP P80379 SEE REMARK 999
SEQADV 1EMW PHE A 80 UNP P80379 SEE REMARK 999
SEQADV 1EMW ARG A 81 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLN A 82 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLU A 83 UNP P80379 SEE REMARK 999
SEQADV 1EMW ALA A 84 UNP P80379 SEE REMARK 999
SEQADV 1EMW ARG A 85 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLU A 86 UNP P80379 SEE REMARK 999
SEQADV 1EMW GLY A 87 UNP P80379 SEE REMARK 999
SEQADV 1EMW ALA A 88 UNP P80379 SEE REMARK 999
SEQRES 1 A 88 MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS
SEQRES 2 A 88 ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG
SEQRES 3 A 88 LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR
SEQRES 4 A 88 ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP
SEQRES 5 A 88 VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN
SEQRES 6 A 88 PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY
SEQRES 7 A 88 VAL PHE ARG GLN GLU ALA ARG GLU GLY ALA
HELIX 1 1 ASP A 52 VAL A 62 1 11
HELIX 2 2 THR A 67 ARG A 75 1 9
SHEET 1 A 4 LYS A 3 ARG A 8 0
SHEET 2 A 4 TYR A 17 THR A 22 -1 O ARG A 18 N ALA A 7
SHEET 3 A 4 GLU A 34 TYR A 39 -1 O GLU A 34 N VAL A 21
SHEET 4 A 4 LYS A 50 VAL A 51 -1 N LYS A 50 O TYR A 38
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