Header list of 1j7h.pdb file
Complete list - b 23 2 Bytes
HEADER UNKNOWN FUNCTION 16-MAY-01 1J7H TITLE SOLUTION STRUCTURE OF HI0719, A HYPOTHETICAL PROTEIN FROM HAEMOPHILUS TITLE 2 INFLUENZAE COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN HI0719; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE; SOURCE 3 ORGANISM_TAXID: 727; SOURCE 4 GENE: YJGF; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B KEYWDS ALPHA/BETA FOLD, HOMOTRIMER, STRUCTURE 2 FUNCTION PROJECT, S2F, KEYWDS 2 STRUCTURAL GENOMICS, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR L.PARSONS,N.BONANDER,E.EISENSTEIN,M.GILSON,V.KAIRYS,J.ORBAN,STRUCTURE AUTHOR 2 2 FUNCTION PROJECT (S2F) REVDAT 3 23-FEB-22 1J7H 1 REMARK REVDAT 2 24-FEB-09 1J7H 1 VERSN REVDAT 1 11-FEB-03 1J7H 0 JRNL AUTH L.PARSONS,N.BONANDER,E.EISENSTEIN,M.GILSON,V.KAIRYS,J.ORBAN JRNL TITL SOLUTION STRUCTURE AND FUNCTIONAL LIGAND SCREENING OF JRNL TITL 2 HI0719, A HIGHLY CONSERVED PROTEIN FROM BACTERIA TO HUMANS JRNL TITL 3 IN THE YJGF/YER057C/UK114 FAMILY JRNL REF BIOCHEMISTRY V. 42 80 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12515541 JRNL DOI 10.1021/BI020541W REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.5, CNS 1.0 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE, REMARK 3 SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1J7H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-01. REMARK 100 THE DEPOSITION ID IS D_1000013455. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : SAMPLE 1: 1.5 MM HI0719 U-15N, REMARK 210 13C; 50 MM SODIUM PHOSPHATE REMARK 210 BUFFER; 100 MM SODIUM CHLORIDE; REMARK 210 3 MM DEUTERATED DTT; 90% H2O, 10% REMARK 210 D2O, SAMPLE 2: 3.0 MM HI0719, REMARK 210 50/50 MIXTURE U-15N, 13C AND REMARK 210 UNLABELED; 50 MM SODIUM REMARK 210 PHOSPHATE BUFFER; 100 MM SODIUM REMARK 210 CHLORIDE; 3 MM DEUTERATED DTT, REMARK 210 100% D2O; 3.0 MM HI0719, 50/50 REMARK 210 MIXTURE U-15N, 13C AND UNLABELED; REMARK 210 50 MM SODIUM PHOSPHATE BUFFER; REMARK 210 100 MM SODIUM CHLORIDE; 3 MM REMARK 210 DEUTERATED DTT REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA; REMARK 210 3D 13C-EDITED, 12C-FILTERED REMARK 210 HMQC-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 1.8, NMRDRAW 1.8, CNS REMARK 210 1.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES REMARK 210 SUBMITTED REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR REMARK 210 SPECTROSCOPY 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HI0719 RELATED DB: TARGETDB DBREF 1J7H A 1 130 UNP P44839 Y719_HAEIN 1 130 DBREF 1J7H B 1 130 UNP P44839 Y719_HAEIN 1 130 DBREF 1J7H C 1 130 UNP P44839 Y719_HAEIN 1 130 SEQRES 1 A 130 MET MET THR GLN ILE ILE HIS THR GLU LYS ALA PRO ALA SEQRES 2 A 130 ALA ILE GLY PRO TYR VAL GLN ALA VAL ASP LEU GLY ASN SEQRES 3 A 130 LEU VAL LEU THR SER GLY GLN ILE PRO VAL ASN PRO ALA SEQRES 4 A 130 THR GLY GLU VAL PRO ALA ASP ILE VAL ALA GLN ALA ARG SEQRES 5 A 130 GLN SER LEU GLU ASN VAL LYS ALA ILE ILE GLU LYS ALA SEQRES 6 A 130 GLY LEU THR ALA ALA ASP ILE VAL LYS THR THR VAL PHE SEQRES 7 A 130 VAL LYS ASP LEU ASN ASP PHE ALA ALA VAL ASN ALA GLU SEQRES 8 A 130 TYR GLU ARG PHE PHE LYS GLU ASN ASN HIS PRO ASN PHE SEQRES 9 A 130 PRO ALA ARG SER CYS VAL GLU VAL ALA ARG LEU PRO LYS SEQRES 10 A 130 ASP VAL GLY LEU GLU ILE GLU ALA ILE ALA VAL ARG LYS SEQRES 1 B 130 MET MET THR GLN ILE ILE HIS THR GLU LYS ALA PRO ALA SEQRES 2 B 130 ALA ILE GLY PRO TYR VAL GLN ALA VAL ASP LEU GLY ASN SEQRES 3 B 130 LEU VAL LEU THR SER GLY GLN ILE PRO VAL ASN PRO ALA SEQRES 4 B 130 THR GLY GLU VAL PRO ALA ASP ILE VAL ALA GLN ALA ARG SEQRES 5 B 130 GLN SER LEU GLU ASN VAL LYS ALA ILE ILE GLU LYS ALA SEQRES 6 B 130 GLY LEU THR ALA ALA ASP ILE VAL LYS THR THR VAL PHE SEQRES 7 B 130 VAL LYS ASP LEU ASN ASP PHE ALA ALA VAL ASN ALA GLU SEQRES 8 B 130 TYR GLU ARG PHE PHE LYS GLU ASN ASN HIS PRO ASN PHE SEQRES 9 B 130 PRO ALA ARG SER CYS VAL GLU VAL ALA ARG LEU PRO LYS SEQRES 10 B 130 ASP VAL GLY LEU GLU ILE GLU ALA ILE ALA VAL ARG LYS SEQRES 1 C 130 MET MET THR GLN ILE ILE HIS THR GLU LYS ALA PRO ALA SEQRES 2 C 130 ALA ILE GLY PRO TYR VAL GLN ALA VAL ASP LEU GLY ASN SEQRES 3 C 130 LEU VAL LEU THR SER GLY GLN ILE PRO VAL ASN PRO ALA SEQRES 4 C 130 THR GLY GLU VAL PRO ALA ASP ILE VAL ALA GLN ALA ARG SEQRES 5 C 130 GLN SER LEU GLU ASN VAL LYS ALA ILE ILE GLU LYS ALA SEQRES 6 C 130 GLY LEU THR ALA ALA ASP ILE VAL LYS THR THR VAL PHE SEQRES 7 C 130 VAL LYS ASP LEU ASN ASP PHE ALA ALA VAL ASN ALA GLU SEQRES 8 C 130 TYR GLU ARG PHE PHE LYS GLU ASN ASN HIS PRO ASN PHE SEQRES 9 C 130 PRO ALA ARG SER CYS VAL GLU VAL ALA ARG LEU PRO LYS SEQRES 10 C 130 ASP VAL GLY LEU GLU ILE GLU ALA ILE ALA VAL ARG LYS HELIX 1 1 ASP A 46 GLY A 66 1 21 HELIX 2 2 THR A 68 ALA A 70 5 3 HELIX 3 3 ASP A 84 LYS A 97 1 14 HELIX 4 4 LEU A 115 VAL A 119 5 5 HELIX 5 5 ASP B 46 GLY B 66 1 21 HELIX 6 6 THR B 68 ALA B 70 5 3 HELIX 7 7 ASP B 84 LYS B 97 1 14 HELIX 8 8 LEU B 115 VAL B 119 5 5 HELIX 9 9 ASP C 46 GLY C 66 1 21 HELIX 10 10 THR C 68 ALA C 70 5 3 HELIX 11 11 ASP C 84 LYS C 97 1 14 HELIX 12 12 LEU C 115 VAL C 119 5 5 SHEET 1 A 5 ALA A 21 ASP A 23 0 SHEET 2 A 5 LEU A 27 THR A 30 -1 O LEU A 29 N VAL A 22 SHEET 3 A 5 LEU A 121 VAL A 128 -1 O ALA A 125 N THR A 30 SHEET 4 A 5 ILE A 72 VAL A 79 -1 N VAL A 73 O ILE A 126 SHEET 5 A 5 ALA A 106 ARG A 107 1 N ALA A 106 O VAL A 73 SHEET 1 B 5 ALA A 21 ASP A 23 0 SHEET 2 B 5 LEU A 27 THR A 30 -1 O LEU A 29 N VAL A 22 SHEET 3 B 5 LEU A 121 VAL A 128 -1 O ALA A 125 N THR A 30 SHEET 4 B 5 ILE A 72 VAL A 79 -1 N VAL A 73 O ILE A 126 SHEET 5 B 5 VAL A 110 GLU A 111 1 O VAL A 110 N VAL A 79 SHEET 1 C 5 ALA B 21 ASP B 23 0 SHEET 2 C 5 LEU B 27 THR B 30 -1 O LEU B 29 N VAL B 22 SHEET 3 C 5 LEU B 121 VAL B 128 -1 O ALA B 125 N THR B 30 SHEET 4 C 5 ILE B 72 VAL B 79 -1 N VAL B 73 O ILE B 126 SHEET 5 C 5 ALA B 106 ARG B 107 1 N ALA B 106 O VAL B 73 SHEET 1 D 5 ALA B 21 ASP B 23 0 SHEET 2 D 5 LEU B 27 THR B 30 -1 O LEU B 29 N VAL B 22 SHEET 3 D 5 LEU B 121 VAL B 128 -1 O ALA B 125 N THR B 30 SHEET 4 D 5 ILE B 72 VAL B 79 -1 N VAL B 73 O ILE B 126 SHEET 5 D 5 VAL B 110 GLU B 111 1 O VAL B 110 N VAL B 79 SHEET 1 E 5 ALA C 21 ASP C 23 0 SHEET 2 E 5 LEU C 27 THR C 30 -1 O LEU C 29 N VAL C 22 SHEET 3 E 5 LEU C 121 VAL C 128 -1 O ALA C 125 N THR C 30 SHEET 4 E 5 ILE C 72 VAL C 79 -1 N VAL C 73 O ILE C 126 SHEET 5 E 5 ALA C 106 ARG C 107 1 N ALA C 106 O VAL C 73 SHEET 1 F 5 ALA C 21 ASP C 23 0 SHEET 2 F 5 LEU C 27 THR C 30 -1 O LEU C 29 N VAL C 22 SHEET 3 F 5 LEU C 121 VAL C 128 -1 O ALA C 125 N THR C 30 SHEET 4 F 5 ILE C 72 VAL C 79 -1 N VAL C 73 O ILE C 126 SHEET 5 F 5 VAL C 110 GLU C 111 1 O VAL C 110 N VAL C 79 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 23 2 Bytes