Header list of 1sqr.pdb file
Complete list - r 2 2 Bytes
HEADER RIBOSOME 19-MAR-04 1SQR
TITLE SOLUTION STRUCTURE OF THE 50S RIBOSOMAL PROTEIN L35AE FROM PYROCOCCUS
TITLE 2 FURIOSUS. NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET PFR48.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L35AE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 GENE: RPL35AE, PF1872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS PFR48, AUTOSTRUCTURE, RIBOSOMAL PROTEIN, NORTHEAST STRUCTURAL
KEYWDS 2 GENOMICS CONSORTIUM, BETA-BARREL, NESG, STRUCTURAL GENOMICS, PSI,
KEYWDS 3 PROTEIN STRUCTURE INITIATIVE, RIBOSOME
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.A.SNYDER,J.M.ARAMINI,Y.J.HUANG,R.XIAO,J.R.CORT,R.SHASTRY,L.C.MA,
AUTHOR 2 J.LIU,B.ROST,T.B.ACTON,M.A.KENNEDY,G.T.MONTELIONE,NORTHEAST
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1SQR 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1SQR 1 VERSN
REVDAT 2 25-JAN-05 1SQR 1 AUTHOR
REVDAT 1 16-NOV-04 1SQR 0
JRNL AUTH D.A.SNYDER,J.M.ARAMINI,Y.J.HUANG,R.XIAO,J.R.CORT,R.SHASTRY,
JRNL AUTH 2 L.C.MA,J.LIU,B.ROST,T.B.ACTON,M.A.KENNEDY,G.T.MONTELIONE
JRNL TITL SOLUTION STRUCTURE OF THE 50S RIBOSOMAL PROTEIN L35AE FROM
JRNL TITL 2 PYROCOCCUS FURIOSUS: NORTHEAST STRUCTURAL GENOMICS
JRNL TITL 3 CONSORTIUM TARGET PFR48
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH 2.0.6, AUTOSTRUCTURE 2.0.0
REMARK 3 AUTHORS : SCHWIETERS, ET AL. (X-PLOR), HUANG AND MONTELIONE
REMARK 3 (AUTOSTRUCTURE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1157 CONFORMATIONALLY-RESTRICTING NOE-DERIVED DISTANCE
REMARK 3 RESTRAINTS, 177 DIHEDRAL ANGLE RESTRAINTS, AND 32 HYDROGEN BOND
REMARK 3 RESTRAINTS. (14.4 CONSTRAINTS PER RESIDUE; 6.1 LONG-RANGE
REMARK 3 RESTRAINTS PER RESIDUE). STRUCTURE DETERMINATION WAS PERFORMED
REMARK 3 ITERATIVELY USING AUTOSTRUCTURE (XPLOR). THE UNSTRUCTURED 8
REMARK 3 RESIDUE C-TERMINAL TAG (LEHHHHHH) WAS INCLUDED IN THE STRUCTURE
REMARK 3 CALCULATIONS BUT IS OMITTED FROM THIS DEPOSITION.
REMARK 4
REMARK 4 1SQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021928.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.07 MM PFR48 U-15N,13C 20 MM
REMARK 210 MES, 100 MM NACL, 5 MM CACL2, 10
REMARK 210 MM DTT, 0.02% NAN3, PH 6.5; 1.07
REMARK 210 MM PFR48 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; 0.1 MM
REMARK 210 PFR48 U-15N,5%-13C 20 MM MES,
REMARK 210 100 MM NACL, 5 MM CACL2, 10 MM
REMARK 210 DTT, 0.02% NAN3, PH 6.5; 0.5 MM
REMARK 210 PFR48 U-15N 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 13C-NOESY (ALIPHATIC), HCCH
REMARK 210 -COSY; 3D 13C-NOESY (ALIPHATIC AND AROMATIC), 13C,1H-HSQC; 4D_
REMARK 210 13C-SEPARATED_NOESY; 3D-TOCSYS; H/D EXCHANGE; 3D 15N-NOESY,
REMARK 210 BACKBONE TR EXPERIMENTS; HIGH-RESOLUTION/NON-CONSTANT-TIME 13C,
REMARK 210 1H-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, NMRPIPE 2.1, SPARKY
REMARK 210 3.106, PDBSTAT 3.32, HYPER 3.2,
REMARK 210 AUTOASSIGN 1.9, TALOS 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. AUTOMATIC BACKBONE RESONANCE ASSIGNMENTS WERE MADE
REMARK 210 USING AUTOASSIGN. MANUAL SIDE CHAIN ASSIGNMENTS. AUTOMATIC NOESY
REMARK 210 ASSIGNMENTS AS WELL AS DISTANCE AND HYDROGEN BOND RESTRAINTS
REMARK 210 WERE DETERMINED USING AUTOSTRUCTURE. DIHEDRAL ANGLE RESTRAINTS
REMARK 210 WERE DETERMINED USING HYPER AND TALOS. BACKBONE DIHEDRAL ANGLES
REMARK 210 FOR RESIDUES 1, 13-20, 26-27, 39-40, 47-51, 54, 63-66 AND 73-79
REMARK 210 ARE NOT WELL-DEFINED [S(PHI) + S(PSI) < 1.8] IN THIS SOLUTION
REMARK 210 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 LEU A 88
REMARK 465 GLU A 89
REMARK 465 HIS A 90
REMARK 465 HIS A 91
REMARK 465 HIS A 92
REMARK 465 HIS A 93
REMARK 465 HIS A 94
REMARK 465 HIS A 95
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 LEU A 8 -61.32 -109.86
REMARK 500 1 ARG A 12 62.51 -100.16
REMARK 500 1 SER A 13 117.63 -38.80
REMARK 500 1 GLU A 15 -162.35 -58.33
REMARK 500 1 GLN A 17 16.71 -158.47
REMARK 500 1 HIS A 18 -5.25 -173.79
REMARK 500 1 ASN A 19 173.66 68.30
REMARK 500 1 LEU A 27 -85.32 -19.33
REMARK 500 1 ASP A 28 -91.86 -93.10
REMARK 500 1 PRO A 48 178.11 -47.96
REMARK 500 1 VAL A 58 -63.46 -99.00
REMARK 500 1 THR A 63 -94.85 51.10
REMARK 500 1 LYS A 64 50.17 -94.50
REMARK 500 1 GLN A 78 95.07 47.66
REMARK 500 1 ILE A 86 73.49 -109.40
REMARK 500 2 ARG A 12 59.31 -91.66
REMARK 500 2 SER A 13 -82.74 56.09
REMARK 500 2 LYS A 14 -170.84 63.22
REMARK 500 2 GLU A 15 -179.49 -55.34
REMARK 500 2 ASN A 16 92.86 47.35
REMARK 500 2 GLN A 17 133.00 -37.91
REMARK 500 2 HIS A 18 11.13 -176.41
REMARK 500 2 ASN A 19 171.29 53.70
REMARK 500 2 PRO A 26 72.41 -59.57
REMARK 500 2 LEU A 27 -116.33 51.99
REMARK 500 2 ASP A 28 -92.78 -74.00
REMARK 500 2 ASN A 30 47.40 -92.29
REMARK 500 2 SER A 49 39.97 -69.01
REMARK 500 2 THR A 63 -88.11 51.55
REMARK 500 2 LYS A 64 51.74 -90.18
REMARK 500 2 ALA A 66 -177.89 -68.71
REMARK 500 2 LYS A 73 -77.72 -81.55
REMARK 500 2 ALA A 79 23.80 -163.10
REMARK 500 2 ILE A 86 72.46 -107.97
REMARK 500 3 ARG A 12 61.11 -104.57
REMARK 500 3 SER A 13 60.18 36.65
REMARK 500 3 LYS A 14 -80.09 -38.78
REMARK 500 3 GLU A 15 -88.90 -66.10
REMARK 500 3 ASN A 16 102.69 -163.89
REMARK 500 3 HIS A 18 -59.25 -169.69
REMARK 500 3 ASN A 19 -32.59 166.72
REMARK 500 3 PRO A 26 87.54 -61.44
REMARK 500 3 LEU A 27 -133.82 36.32
REMARK 500 3 ASP A 28 -92.73 -44.04
REMARK 500 3 ASN A 30 41.69 -82.60
REMARK 500 3 ILE A 39 -19.88 -48.52
REMARK 500 3 SER A 49 5.07 -69.66
REMARK 500 3 THR A 63 156.41 55.95
REMARK 500 3 LYS A 64 -21.05 68.98
REMARK 500 3 ALA A 66 147.57 176.38
REMARK 500
REMARK 500 THIS ENTRY HAS 170 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 1 ARG A 2 0.23 SIDE CHAIN
REMARK 500 1 ARG A 12 0.31 SIDE CHAIN
REMARK 500 1 ARG A 59 0.21 SIDE CHAIN
REMARK 500 1 ARG A 68 0.26 SIDE CHAIN
REMARK 500 1 ARG A 70 0.21 SIDE CHAIN
REMARK 500 2 ARG A 2 0.30 SIDE CHAIN
REMARK 500 2 ARG A 11 0.24 SIDE CHAIN
REMARK 500 2 ARG A 12 0.31 SIDE CHAIN
REMARK 500 2 ARG A 32 0.20 SIDE CHAIN
REMARK 500 2 ARG A 41 0.11 SIDE CHAIN
REMARK 500 2 ARG A 59 0.24 SIDE CHAIN
REMARK 500 2 ARG A 68 0.13 SIDE CHAIN
REMARK 500 2 ARG A 70 0.17 SIDE CHAIN
REMARK 500 3 ARG A 2 0.12 SIDE CHAIN
REMARK 500 3 ARG A 11 0.20 SIDE CHAIN
REMARK 500 3 ARG A 12 0.28 SIDE CHAIN
REMARK 500 3 ARG A 32 0.16 SIDE CHAIN
REMARK 500 3 ARG A 41 0.20 SIDE CHAIN
REMARK 500 3 ARG A 59 0.31 SIDE CHAIN
REMARK 500 3 ARG A 68 0.27 SIDE CHAIN
REMARK 500 3 ARG A 70 0.18 SIDE CHAIN
REMARK 500 4 ARG A 2 0.27 SIDE CHAIN
REMARK 500 4 ARG A 11 0.15 SIDE CHAIN
REMARK 500 4 ARG A 12 0.21 SIDE CHAIN
REMARK 500 4 ARG A 32 0.30 SIDE CHAIN
REMARK 500 4 ARG A 41 0.22 SIDE CHAIN
REMARK 500 4 ARG A 59 0.23 SIDE CHAIN
REMARK 500 4 ARG A 68 0.18 SIDE CHAIN
REMARK 500 4 ARG A 70 0.13 SIDE CHAIN
REMARK 500 5 ARG A 2 0.31 SIDE CHAIN
REMARK 500 5 ARG A 11 0.30 SIDE CHAIN
REMARK 500 5 ARG A 12 0.09 SIDE CHAIN
REMARK 500 5 ARG A 32 0.24 SIDE CHAIN
REMARK 500 5 ARG A 41 0.30 SIDE CHAIN
REMARK 500 5 ARG A 68 0.31 SIDE CHAIN
REMARK 500 5 ARG A 70 0.20 SIDE CHAIN
REMARK 500 6 ARG A 2 0.31 SIDE CHAIN
REMARK 500 6 ARG A 11 0.29 SIDE CHAIN
REMARK 500 6 ARG A 12 0.22 SIDE CHAIN
REMARK 500 6 ARG A 32 0.18 SIDE CHAIN
REMARK 500 6 ARG A 41 0.16 SIDE CHAIN
REMARK 500 6 ARG A 59 0.31 SIDE CHAIN
REMARK 500 6 ARG A 68 0.15 SIDE CHAIN
REMARK 500 6 ARG A 70 0.10 SIDE CHAIN
REMARK 500 7 ARG A 2 0.10 SIDE CHAIN
REMARK 500 7 ARG A 11 0.24 SIDE CHAIN
REMARK 500 7 ARG A 32 0.17 SIDE CHAIN
REMARK 500 7 ARG A 41 0.31 SIDE CHAIN
REMARK 500 7 ARG A 59 0.31 SIDE CHAIN
REMARK 500 7 ARG A 68 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 73 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFR48 RELATED DB: TARGETDB
DBREF 1SQR A 1 87 UNP Q8TZV6 RL35A_PYRFU 1 87
SEQADV 1SQR LEU A 88 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR GLU A 89 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 90 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 91 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 92 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 93 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 94 UNP Q8TZV6 CLONING ARTIFACT
SEQADV 1SQR HIS A 95 UNP Q8TZV6 CLONING ARTIFACT
SEQRES 1 A 95 MET ARG ILE LYS GLY VAL VAL LEU SER TYR ARG ARG SER
SEQRES 2 A 95 LYS GLU ASN GLN HIS ASN ASN VAL MET ILE ILE LYS PRO
SEQRES 3 A 95 LEU ASP VAL ASN SER ARG GLU GLU ALA SER LYS LEU ILE
SEQRES 4 A 95 GLY ARG LEU VAL LEU TRP LYS SER PRO SER GLY LYS ILE
SEQRES 5 A 95 LEU LYS GLY LYS ILE VAL ARG VAL HIS GLY THR LYS GLY
SEQRES 6 A 95 ALA VAL ARG ALA ARG PHE GLU LYS GLY LEU PRO GLY GLN
SEQRES 7 A 95 ALA LEU GLY ASP TYR VAL GLU ILE VAL LEU GLU HIS HIS
SEQRES 8 A 95 HIS HIS HIS HIS
HELIX 1 1 SER A 31 ILE A 39 1 9
SHEET 1 A 6 LEU A 42 TRP A 45 0
SHEET 2 A 6 LEU A 53 VAL A 60 -1 O LEU A 53 N TRP A 45
SHEET 3 A 6 VAL A 67 ARG A 70 -1 O ARG A 68 N ARG A 59
SHEET 4 A 6 VAL A 21 PRO A 26 -1 N MET A 22 O ALA A 69
SHEET 5 A 6 LYS A 4 ARG A 11 -1 N VAL A 6 O LYS A 25
SHEET 6 A 6 TYR A 83 GLU A 85 -1 O VAL A 84 N GLY A 5
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