Header list of 1rq8.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 04-DEC-03 1RQ8
TITLE SOLUTION STRUCTURE OF THE HYPOTHETICAL PROTEIN SAV1595 FROM
TITLE 2 STAPHYLOCOCCUS AUREUS, A PUTATIVE RNA BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: HOMOLOGOUS TO YHBY OF E.COLI.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;
SOURCE 3 ORGANISM_TAXID: 1280;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS STRUCTURAL GENOMICS, SAV1595, YHBY, UPF0044, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.LIU,D.F.WYSS
REVDAT 3 02-MAR-22 1RQ8 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1RQ8 1 VERSN
REVDAT 1 06-JUL-04 1RQ8 0
JRNL AUTH D.LIU,D.F.WYSS
JRNL TITL SOLUTION STRUCTURE OF THE HYPOTHETICAL PROTEIN SAV1595 FROM
JRNL TITL 2 STAPHYLOCOCCUS AUREUS, A PUTATIVE RNA BINDING PROTEIN.
JRNL REF J.BIOMOL.NMR V. 29 391 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15213438
JRNL DOI 10.1023/B:JNMR.0000032524.62229.93
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98, X-PLOR 98
REMARK 3 AUTHORS : ACCELRYS (X-PLOR), ACCELRYS (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RQ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020946.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0.45
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SAV1595, U-15N,13C; 75 MM
REMARK 210 PHOSPHATE BUFFER, 8%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
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 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 97
REMARK 465 GLU A 98
REMARK 465 HIS A 99
REMARK 465 HIS A 100
REMARK 465 HIS A 101
REMARK 465 HIS A 102
REMARK 465 HIS A 103
REMARK 465 HIS A 104
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 O ILE A 33 H ASP A 37 1.53
REMARK 500 O LEU A 61 H LEU A 65 1.53
REMARK 500 O VAL A 48 H ILE A 81 1.54
REMARK 500 O GLN A 75 H VAL A 82 1.55
REMARK 500 O LEU A 40 HE ARG A 85 1.56
REMARK 500 O GLU A 30 H LYS A 34 1.58
REMARK 500 O LYS A 7 H ARG A 11 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 ASN A 53 -60.50 66.38
REMARK 500 1 GLN A 75 168.16 175.96
REMARK 500 1 GLU A 86 169.42 -37.23
REMARK 500 1 LYS A 88 -48.03 -146.73
REMARK 500 1 ASN A 90 81.28 -57.25
REMARK 500 1 GLU A 92 75.72 -64.69
REMARK 500 1 LEU A 95 65.52 -173.06
REMARK 500 2 LEU A 51 34.42 -86.46
REMARK 500 2 SER A 71 -167.37 -117.37
REMARK 500 2 GLN A 75 179.03 171.73
REMARK 500 2 GLU A 86 -149.05 30.97
REMARK 500 2 LYS A 88 -58.80 -141.74
REMARK 500 2 ASN A 90 81.66 -57.45
REMARK 500 2 LYS A 91 -166.92 -100.01
REMARK 500 3 LEU A 51 40.03 -86.24
REMARK 500 3 GLN A 75 -177.64 176.76
REMARK 500 3 GLU A 86 174.22 -41.29
REMARK 500 3 LYS A 88 -48.22 -148.15
REMARK 500 3 ASN A 90 83.81 -54.17
REMARK 500 3 GLU A 92 74.00 -64.54
REMARK 500 3 LEU A 95 69.55 -175.83
REMARK 500 4 ARG A 43 -158.82 -106.35
REMARK 500 4 GLU A 44 -57.21 -121.82
REMARK 500 4 ASN A 53 14.22 59.80
REMARK 500 4 PHE A 55 -70.71 -82.35
REMARK 500 4 GLU A 86 -144.93 24.01
REMARK 500 4 LYS A 88 -62.27 -152.59
REMARK 500 4 ASN A 90 78.03 -62.09
REMARK 500 4 GLU A 92 74.23 -65.15
REMARK 500 4 LEU A 95 65.05 -168.90
REMARK 500 5 ARG A 43 -153.39 79.68
REMARK 500 5 GLU A 44 -146.60 73.75
REMARK 500 5 PHE A 55 -84.99 -77.44
REMARK 500 5 GLN A 75 -174.06 178.30
REMARK 500 5 GLU A 86 -145.14 18.65
REMARK 500 5 LYS A 88 -63.96 -156.28
REMARK 500 5 ASN A 90 77.37 -60.39
REMARK 500 5 GLU A 92 71.89 -65.26
REMARK 500 5 LEU A 95 65.93 -176.14
REMARK 500 6 LEU A 51 44.15 -88.74
REMARK 500 6 ASN A 53 -73.76 63.95
REMARK 500 6 SER A 71 -167.29 -121.43
REMARK 500 6 GLN A 75 170.33 179.14
REMARK 500 6 SER A 79 -1.13 71.86
REMARK 500 6 GLU A 86 -146.10 27.28
REMARK 500 6 LYS A 88 -62.20 -150.82
REMARK 500 6 ASN A 90 80.45 -60.05
REMARK 500 6 GLU A 92 73.53 -64.77
REMARK 500 6 LEU A 95 62.64 -164.75
REMARK 500 7 ASN A 53 -59.16 65.83
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 1 ARG A 8 0.19 SIDE CHAIN
REMARK 500 1 ARG A 11 0.20 SIDE CHAIN
REMARK 500 1 ARG A 43 0.28 SIDE CHAIN
REMARK 500 1 ARG A 70 0.32 SIDE CHAIN
REMARK 500 1 ARG A 85 0.31 SIDE CHAIN
REMARK 500 2 ARG A 8 0.32 SIDE CHAIN
REMARK 500 2 ARG A 11 0.22 SIDE CHAIN
REMARK 500 2 ARG A 43 0.24 SIDE CHAIN
REMARK 500 2 ARG A 70 0.16 SIDE CHAIN
REMARK 500 2 ARG A 85 0.21 SIDE CHAIN
REMARK 500 3 ARG A 8 0.20 SIDE CHAIN
REMARK 500 3 ARG A 11 0.30 SIDE CHAIN
REMARK 500 3 ARG A 43 0.30 SIDE CHAIN
REMARK 500 3 ARG A 70 0.23 SIDE CHAIN
REMARK 500 3 ARG A 85 0.30 SIDE CHAIN
REMARK 500 4 ARG A 8 0.23 SIDE CHAIN
REMARK 500 4 ARG A 11 0.31 SIDE CHAIN
REMARK 500 4 ARG A 43 0.28 SIDE CHAIN
REMARK 500 4 ARG A 70 0.31 SIDE CHAIN
REMARK 500 4 ARG A 85 0.25 SIDE CHAIN
REMARK 500 5 ARG A 8 0.18 SIDE CHAIN
REMARK 500 5 ARG A 11 0.25 SIDE CHAIN
REMARK 500 5 ARG A 43 0.32 SIDE CHAIN
REMARK 500 5 ARG A 70 0.24 SIDE CHAIN
REMARK 500 5 ARG A 85 0.32 SIDE CHAIN
REMARK 500 6 ARG A 8 0.27 SIDE CHAIN
REMARK 500 6 ARG A 11 0.27 SIDE CHAIN
REMARK 500 6 ARG A 43 0.30 SIDE CHAIN
REMARK 500 6 ARG A 70 0.25 SIDE CHAIN
REMARK 500 6 ARG A 85 0.19 SIDE CHAIN
REMARK 500 7 ARG A 8 0.27 SIDE CHAIN
REMARK 500 7 ARG A 11 0.30 SIDE CHAIN
REMARK 500 7 ARG A 43 0.31 SIDE CHAIN
REMARK 500 7 ARG A 70 0.32 SIDE CHAIN
REMARK 500 7 ARG A 85 0.21 SIDE CHAIN
REMARK 500 8 ARG A 8 0.28 SIDE CHAIN
REMARK 500 8 ARG A 11 0.26 SIDE CHAIN
REMARK 500 8 ARG A 43 0.27 SIDE CHAIN
REMARK 500 8 ARG A 70 0.21 SIDE CHAIN
REMARK 500 8 ARG A 85 0.15 SIDE CHAIN
REMARK 500 9 ARG A 8 0.25 SIDE CHAIN
REMARK 500 9 ARG A 11 0.32 SIDE CHAIN
REMARK 500 9 ARG A 43 0.29 SIDE CHAIN
REMARK 500 9 ARG A 70 0.20 SIDE CHAIN
REMARK 500 9 ARG A 85 0.20 SIDE CHAIN
REMARK 500 10 ARG A 8 0.29 SIDE CHAIN
REMARK 500 10 ARG A 11 0.29 SIDE CHAIN
REMARK 500 10 ARG A 43 0.15 SIDE CHAIN
REMARK 500 10 ARG A 70 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RQ8 A 1 96 UNP Q99TQ4 Q99TQ4_STAAM 1 96
SEQADV 1RQ8 LEU A 97 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 GLU A 98 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 99 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 100 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 101 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 102 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 103 UNP Q99TQ4 EXPRESSION TAG
SEQADV 1RQ8 HIS A 104 UNP Q99TQ4 EXPRESSION TAG
SEQRES 1 A 104 MET LEU THR GLY LYS GLN LYS ARG TYR LEU ARG SER LEU
SEQRES 2 A 104 ALA HIS ASN ILE ASP PRO ILE PHE GLN ILE GLY LYS GLY
SEQRES 3 A 104 GLY ILE ASN GLU ASN MET ILE LYS GLN ILE ASP ASP THR
SEQRES 4 A 104 LEU GLU ASN ARG GLU LEU ILE LYS VAL HIS VAL LEU GLN
SEQRES 5 A 104 ASN ASN PHE ASP ASP LYS LYS GLU LEU ALA GLU THR LEU
SEQRES 6 A 104 SER GLU ALA THR ARG SER GLU LEU VAL GLN VAL ILE GLY
SEQRES 7 A 104 SER MET ILE VAL ILE TYR ARG GLU SER LYS GLU ASN LYS
SEQRES 8 A 104 GLU ILE GLU LEU PRO LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 3 ALA A 14 1 12
HELIX 2 2 ASN A 29 ARG A 43 1 15
HELIX 3 3 ASN A 54 ARG A 70 1 17
SHEET 1 A 4 GLN A 22 ILE A 23 0
SHEET 2 A 4 LEU A 45 VAL A 50 1 O HIS A 49 N ILE A 23
SHEET 3 A 4 MET A 80 ARG A 85 -1 O ILE A 81 N VAL A 48
SHEET 4 A 4 SER A 71 ILE A 77 -1 N GLN A 75 O VAL A 82
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