HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-FEB-04 1SF0
TITLE BACKBONE SOLUTION STRUCTURE OF MIXED ALPHA/BETA PROTEIN PF1061
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PF1061;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 186497;
SOURCE 4 STRAIN: DSM 3638;
SOURCE 5 GENE: PF1061;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3STAR PRIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24D BAM
KEYWDS RESIDUAL DIPOLAR COUPLINGS, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, SOUTHEAST COLLABORATORY FOR STRUCTURAL
KEYWDS 3 GENOMICS, SECSG, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
AUTHOR J.H.PRESTEGARD,K.L.MAYER,H.VALAFAR,SOUTHEAST COLLABORATORY FOR
AUTHOR 2 STRUCTURAL GENOMICS (SECSG)
REVDAT 5 13-JUL-11 1SF0 1 VERSN
REVDAT 4 24-FEB-09 1SF0 1 VERSN
REVDAT 3 08-MAR-05 1SF0 1 JRNL
REVDAT 2 01-FEB-05 1SF0 1 AUTHOR KEYWDS REMARK
REVDAT 1 13-APR-04 1SF0 0
JRNL AUTH H.VALAFAR,K.L.MAYER,C.M.BOUGAULT,P.D.LEBLOND,F.E.JENNEY,
JRNL AUTH 2 P.S.BRERETON,M.W.ADAMS,J.H.PRESTEGARD
JRNL TITL BACKBONE SOLUTION STRUCTURES OF PROTEINS USING RESIDUAL
JRNL TITL 2 DIPOLAR COUPLINGS: APPLICATION TO A NOVEL STRUCTURAL
JRNL TITL 3 GENOMICS TARGET.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 5 241 2005
JRNL REFN ISSN 1345-711X
JRNL PMID 15704012
JRNL DOI 10.1007/S10969-005-4899-5
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR-NIH 2.9.1
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA, CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RDCS WERE USED IN THE INITIAL ASSEMBLY
REMARK 3 OF FOUR FRAGMENTS. RDCS FROM TWO MEDIA WERE USED TO SET RELATIVE
REMARK 3 ORIENTATIONS OF THE FRAGMENTS. TRANSLATIONAL RELATIONSHIPS OF
REMARK 3 FRAGMENTS WERE DICTATED BY SEQUENCE CONNECTIVITIES AND LONG-RANGE
REMARK 3 NOES. THE ASSEMBLED STRUCTURE WAS MINIMIZED USING A MOLECULAR
REMARK 3 FORCE FIELD AND RDC ERROR FUNCTION. A TOTAL OF 486 RESTRAINTS
REMARK 3 WERE USED: 380 RESIDUAL DIPOLAR COUPLING RESTRAINTS, 85 NOE
REMARK 3 RESTRAINTS (OF WHICH 64 WERE SEQUENTIAL, 11 SHORT-RANGE AND 10
REMARK 3 LONG-RANGE), AND 21 DIHEDRAL RESTRAINTS. ALL SIDECHAIN ATOMS
REMARK 3 BEYOND CB ARE MISSING.
REMARK 4
REMARK 4 1SF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021650.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 300; 293
REMARK 210 PH : 5.5; 6; 6
REMARK 210 IONIC STRENGTH : 200 MM KCL; 100 MM KCL; 100 MM
REMARK 210 KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM 1016054 U-15N, 16% 13C 50
REMARK 210 MM PHOSPHATE BUFFER; 200 MM KCL;
REMARK 210 90% H2O, 10% D2O;; 0.5 MM 1016054
REMARK 210 U-15N, 16% 13C; 50 MM PHOSPHATE
REMARK 210 BUFFER; 100 MM KCL; PEG BICELLES
REMARK 210 (C12E5-HEXANOL IN 0.98 RATIO);
REMARK 210 90% H2O, 10% D2O;; 0.5 MM 1016054
REMARK 210 U-15N, 16% 13C; 50 MM PHOSPHATE
REMARK 210 BUFFER; 100 MM KCL; PEG-CTAB (27:
REMARK 210 1)BICELLES (C12E5-HEXANOL IN 0.87
REMARK 210 RATIO); 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SOFT HNCA-E.COSY; MODIFIED HNCO;
REMARK 210 15N COUPLED HSQC; 3D_15N -
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_TOCSY; SOFT HNCA-
REMARK 210 E.COSY; MODIFIED HNCO; 15N
REMARK 210 COUPLED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 5.0.4, REDCRAFT 1.0,
REMARK 210 REDCAT 1.0
REMARK 210 METHOD USED : RDC DIRECTED FRAGMENT ASSEMBLY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING PREDOMINANTLY RESIDUAL
REMARK 210 DIPOLAR COUPLINGS FROM BACKBONE ATOM PAIRS. IT IS A BACKBONE
REMARK 210 STRUCTURE MODELED AS AN ALA-GLY-PRO POLYPEPTIDE.
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 RES C SSSEQI
REMARK 465 ALA A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
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 ASN A 12 57.32 79.65
REMARK 500 GLU A 16 156.77 -36.43
REMARK 500 GLU A 18 -133.49 -72.02
REMARK 500 ARG A 20 -91.88 -140.65
REMARK 500 GLU A 21 118.90 157.74
REMARK 500 MET A 23 -167.60 -59.11
REMARK 500 LYS A 24 141.33 -173.39
REMARK 500 ASN A 35 47.68 -77.73
REMARK 500 SER A 38 55.97 -98.32
REMARK 500 ALA A 39 158.42 154.90
REMARK 500 GLU A 53 156.18 -39.20
REMARK 500 LYS A 55 -149.87 -149.20
REMARK 500 ASP A 56 30.77 31.40
REMARK 500 PHE A 59 -148.94 -81.81
REMARK 500 ILE A 63 149.30 152.29
REMARK 500 PRO A 64 84.87 -41.16
REMARK 500 VAL A 65 31.51 -92.48
REMARK 500 SER A 67 139.86 -174.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PFU-1016054-001 RELATED DB: TARGETDB
DBREF 1SF0 A 2 69 UNP Q8U1Z3 Q8U1Z3_PYRFU 4 71
SEQADV 1SF0 ALA A -7 UNP Q8U1Z3 CLONING ARTIFACT
SEQADV 1SF0 HIS A -6 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 HIS A -5 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 HIS A -4 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 HIS A -3 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 HIS A -2 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 HIS A -1 UNP Q8U1Z3 EXPRESSION TAG
SEQADV 1SF0 GLY A 0 UNP Q8U1Z3 CLONING ARTIFACT
SEQADV 1SF0 SER A 1 UNP Q8U1Z3 CLONING ARTIFACT
SEQRES 1 A 77 ALA HIS HIS HIS HIS HIS HIS GLY SER LYS MET ILE LYS
SEQRES 2 A 77 VAL LYS VAL ILE GLY ARG ASN ILE GLU LYS GLU ILE GLU
SEQRES 3 A 77 TRP ARG GLU GLY MET LYS VAL ARG ASP ILE LEU ARG ALA
SEQRES 4 A 77 VAL GLY PHE ASN THR GLU SER ALA ILE ALA LYS VAL ASN
SEQRES 5 A 77 GLY LYS VAL VAL LEU GLU ASP ASP GLU VAL LYS ASP GLY
SEQRES 6 A 77 ASP PHE VAL GLU VAL ILE PRO VAL VAL SER GLY GLY
HELIX 1 1 LYS A 24 ALA A 31 1 8
SHEET 1 A 2 LYS A 5 LYS A 7 0
SHEET 2 A 2 PHE A 59 GLU A 61 1 O VAL A 60 N LYS A 5
SHEET 1 B 2 LYS A 42 VAL A 43 0
SHEET 2 B 2 LYS A 46 VAL A 47 -1 O LYS A 46 N VAL A 43
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
(ATOM LINES ARE NOT SHOWN.)
END
