Header list of 1ny4.pdb file
Complete list - 23 20 Bytes
HEADER RNA BINDING PROTEIN 11-FEB-03 1NY4
TITLE SOLUTION STRUCTURE OF THE 30S RIBOSOMAL PROTEIN S28E FROM PYROCOCCUS
TITLE 2 HORIKOSHII. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET JR19.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S28E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 GENE: RPS28E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21MGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS JR19, AUTOSTRUCTURE, RIBOSOMAL PROTEIN, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, PSI, PROTEIN STRUCTURE INITIATIVE, NESG, RNA BINDING
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR J.M.ARAMINI,J.R.CORT,Y.J.HUANG,R.XIAO,T.B.ACTON,C.K.HO,L.-Y.SHIH,
AUTHOR 2 M.A.KENNEDY,G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 5 23-FEB-22 1NY4 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1NY4 1 VERSN
REVDAT 3 25-JAN-05 1NY4 1 AUTHOR KEYWDS REMARK
REVDAT 2 09-DEC-03 1NY4 1 JRNL
REVDAT 1 02-SEP-03 1NY4 0
JRNL AUTH J.M.ARAMINI,Y.J.HUANG,J.R.CORT,S.GOLDSMITH-FISCHMAN,R.XIAO,
JRNL AUTH 2 L.-Y.SHIH,C.K.HO,J.LIU,B.ROST,B.HONIG,M.A.KENNEDY,T.B.ACTON,
JRNL AUTH 3 G.T.MONTELIONE
JRNL TITL SOLUTION NMR STRUCTURE OF THE 30S RIBOSOMAL PROTEIN S28E
JRNL TITL 2 FROM PYROCOCCUS HORIKOSHII.
JRNL REF PROTEIN SCI. V. 12 2823 2003
JRNL REFN ISSN 0961-8368
JRNL PMID 14627742
JRNL DOI 10.1110/PS.03359003
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, AUTOSTRUCTURE 1.1.2, DYANA 1.5
REMARK 3 AUTHORS : VARIAN (VNMR), HUANG, MONTELIONE (AUTOSTRUCTURE),
REMARK 3 GUNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL
REMARK 3 OF 828 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 RESTRAINTS, 99 DIHEDRAL ANGLE RESTRAINTS, AND 28 HYDROGEN
REMARK 3 BOND RESTRAINTS. (13.5 CONSTRAINTS PER RESIDUE; 5.2 LONG-RANGE
REMARK 3 RESTRAINTS PER RESIDUE).
REMARK 3 STRUCTURE DETERMINATION WAS PERFORMED ITERATIVELY USING
REMARK 3 AUTOSTRUCTURE (DYANA).
REMARK 3 THE UNSTRUCTURED 11 RESIDUE C-TERMINAL TAG (AAALEHHHHHH) WAS
REMARK 3 INCLUDED IN THE
REMARK 3 STRUCTURE CALCULATIONS BUT IS OMITTED FROM THIS DEPOSITION.
REMARK 4
REMARK 4 1NY4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018339.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM JR19 U-15N,13C 20 MM MES,
REMARK 210 100 MM NACL, 5 MM CACL2, 10 MM
REMARK 210 DTT, 0.02% NAN3, PH 6.5; 1.0 MM
REMARK 210 JR19 U-15N,13C 20 MM MES, 100 MM
REMARK 210 NACL, 5 MM CACL2, 10 MM DTT,
REMARK 210 0.02% NAN3, PH 6.5; 1.0 MM JR19
REMARK 210 U-15N, 5%-13C 20 MM MES, 100 MM
REMARK 210 NACL, 5 MM CACL2, 10 MM DTT,
REMARK 210 0.02% NAN3, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 15N-NOESY, 3D 13C-NOESY
REMARK 210 (ALIPHATIC AND AROMATIC); 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA; HIGH
REMARK 210 RESOLUTION 13C,1H-HSQC; H/D
REMARK 210 EXCHANGE; BACKBONE TR
REMARK 210 EXPERIMENTS, AND 3D TOCSYS
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, SPARKY 3.106,
REMARK 210 AUTOASSIGN 1.9, HYPER 3.2,
REMARK 210 PDBSTAT 3.27
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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
REMARK 210 NMR SPECTROSCOPY. AUTOMATIC BACKBONE RESONANCE ASSIGNMENTS
REMARK 210 WERE MADE USING AUTOASSIGN. MANUAL SIDE CHAIN ASSIGNMENTS.
REMARK 210 AUTOMATIC NOESY ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN
REMARK 210 BOND RESTRAINTS WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL
REMARK 210 ANGLE RESTRAINTS WERE DETERMINED USING HYPER AND TALOS.
REMARK 210 BACKBONE CONFORMATIONS FOR RESIDUES 1-3, 5-6, 18-20, 22-23,
REMARK 210 34-35, 48-49, 57-71, ARE NOT WELL-DEFINED [S(PHI) + S(PSI) <
REMARK 210 1.8] IN THIS SOLUTION NMR STRUCTURE.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 72
REMARK 465 ALA A 73
REMARK 465 ALA A 74
REMARK 465 LEU A 75
REMARK 465 GLU A 76
REMARK 465 HIS A 77
REMARK 465 HIS A 78
REMARK 465 HIS A 79
REMARK 465 HIS A 80
REMARK 465 HIS A 81
REMARK 465 HIS A 82
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 ALA A 2 -56.32 80.69
REMARK 500 1 GLU A 3 116.50 -36.65
REMARK 500 1 ASP A 4 20.53 -151.24
REMARK 500 1 THR A 18 -46.56 -135.26
REMARK 500 1 THR A 20 -75.98 63.73
REMARK 500 1 ARG A 35 -75.32 64.50
REMARK 500 1 LYS A 37 89.08 39.01
REMARK 500 1 PRO A 48 -162.56 -74.96
REMARK 500 1 ASP A 53 150.28 -43.67
REMARK 500 1 GLU A 59 -47.93 -150.84
REMARK 500 1 THR A 60 -3.07 79.96
REMARK 500 1 GLU A 61 -175.40 47.84
REMARK 500 1 ARG A 62 -59.77 -150.19
REMARK 500 1 GLU A 63 79.31 65.14
REMARK 500 1 ALA A 64 58.46 -100.11
REMARK 500 1 GLU A 66 65.24 61.27
REMARK 500 1 ARG A 70 88.01 41.27
REMARK 500 2 ALA A 2 -143.38 -74.45
REMARK 500 2 ASP A 4 19.61 -150.34
REMARK 500 2 ILE A 15 -77.65 -80.41
REMARK 500 2 THR A 20 -76.00 64.25
REMARK 500 2 ARG A 35 -76.02 69.99
REMARK 500 2 LYS A 37 89.87 41.31
REMARK 500 2 PRO A 48 -166.89 -75.00
REMARK 500 2 LEU A 57 114.93 -160.00
REMARK 500 2 GLU A 59 144.43 178.70
REMARK 500 2 THR A 60 -34.10 163.87
REMARK 500 2 ALA A 64 -70.21 -155.69
REMARK 500 2 ARG A 65 -54.15 82.33
REMARK 500 2 LYS A 68 37.19 -171.37
REMARK 500 2 ARG A 70 90.72 39.61
REMARK 500 3 GLU A 3 116.72 -36.80
REMARK 500 3 ILE A 15 -81.47 -94.61
REMARK 500 3 THR A 18 45.36 -166.26
REMARK 500 3 THR A 20 -80.65 67.02
REMARK 500 3 ARG A 35 -47.52 84.33
REMARK 500 3 ASP A 36 30.51 -92.54
REMARK 500 3 LYS A 37 88.57 -51.25
REMARK 500 3 THR A 60 7.99 82.18
REMARK 500 3 ALA A 64 -64.60 -175.91
REMARK 500 3 ARG A 65 -61.68 77.99
REMARK 500 3 GLU A 66 69.94 65.73
REMARK 500 4 GLU A 3 118.24 -36.39
REMARK 500 4 ASP A 4 20.34 -150.97
REMARK 500 4 THR A 18 56.31 -145.83
REMARK 500 4 LYS A 37 88.52 37.53
REMARK 500 4 ILE A 56 -135.69 -96.99
REMARK 500 4 LEU A 57 140.63 87.98
REMARK 500 4 GLU A 59 -29.27 -38.55
REMARK 500 4 THR A 60 49.00 -80.89
REMARK 500
REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JR19 RELATED DB: TARGETDB
DBREF 1NY4 A 1 71 UNP P61030 RS28_PYRHO 1 71
SEQADV 1NY4 ALA A 72 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 ALA A 73 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 ALA A 74 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 LEU A 75 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 GLU A 76 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 77 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 78 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 79 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 80 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 81 UNP P61030 EXPRESSION TAG
SEQADV 1NY4 HIS A 82 UNP P61030 EXPRESSION TAG
SEQRES 1 A 82 MET ALA GLU ASP GLU GLY TYR PRO ALA GLU VAL ILE GLU
SEQRES 2 A 82 ILE ILE GLY ARG THR GLY THR THR GLY ASP VAL THR GLN
SEQRES 3 A 82 VAL LYS VAL ARG ILE LEU GLU GLY ARG ASP LYS GLY ARG
SEQRES 4 A 82 VAL ILE ARG ARG ASN VAL ARG GLY PRO VAL ARG VAL GLY
SEQRES 5 A 82 ASP ILE LEU ILE LEU ARG GLU THR GLU ARG GLU ALA ARG
SEQRES 6 A 82 GLU ILE LYS SER ARG ARG ALA ALA ALA LEU GLU HIS HIS
SEQRES 7 A 82 HIS HIS HIS HIS
SHEET 1 A 4 VAL A 40 ARG A 46 0
SHEET 2 A 4 VAL A 24 ILE A 31 -1 N VAL A 29 O ILE A 41
SHEET 3 A 4 PRO A 8 ILE A 14 -1 N GLU A 10 O ARG A 30
SHEET 4 A 4 ILE A 54 ILE A 56 -1 O LEU A 55 N ALA A 9
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