Header list of 1jfj.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 20-JUN-01 1JFJ TITLE NMR SOLUTION STRUCTURE OF AN EF-HAND CALCIUM BINDING PROTEIN FROM TITLE 2 ENTAMOEBA HISTOLYTICA COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALCIUM-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: EHCABP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA; SOURCE 3 ORGANISM_TAXID: 5759; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3C KEYWDS EF-HAND, HELIX-LOOP-HELIX, CALCIUM-BINDING PROTEIN, METAL BINDING KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.S.ATREYA,S.C.SAHU,A.BHATTACHARYA,K.V.R.CHARY,G.GOVIL REVDAT 5 23-FEB-22 1JFJ 1 REMARK SEQADV REVDAT 4 24-FEB-09 1JFJ 1 VERSN REVDAT 3 01-APR-03 1JFJ 1 JRNL REVDAT 2 25-DEC-02 1JFJ 1 REMARK REVDAT 1 19-DEC-01 1JFJ 0 JRNL AUTH H.S.ATREYA,S.C.SAHU,A.BHATTACHARYA,K.V.CHARY,G.GOVIL JRNL TITL NMR DERIVED SOLUTION STRUCTURE OF AN EF-HAND CALCIUM-BINDING JRNL TITL 2 PROTEIN FROM ENTAMOEBA HISTOLYTICA. JRNL REF BIOCHEMISTRY V. 40 14392 2001 JRNL REFN ISSN 0006-2960 JRNL PMID 11724551 JRNL DOI 10.1021/BI0114978 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUENTERT, MUMENTHALER AND WUTHRICH (DYANA), REMARK 3 GUENTERT, MUMENTHALER AND WUTHRICH (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON A TOTAL OF REMARK 3 1265 NOE-DERIVED DISTANCE CONSTRAINTS, 200 DIHEDRAL ANGLE REMARK 3 CONSTRAINTS REMARK 4 REMARK 4 1JFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUN-01. REMARK 100 THE DEPOSITION ID IS D_1000013710. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 10MM CACL2 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 3MM EHCABP, 30MM DEUTERATED TRIS REMARK 210 BUFFER, 30MM CALC2; 3MM EHCABP, REMARK 210 30MM DEUTERATED TRIS BUFFER, REMARK 210 30MM CACL2 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: 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: 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 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 LYS A 29 -75.54 -78.73 REMARK 500 1 ALA A 31 54.97 -143.07 REMARK 500 1 ILE A 32 51.48 -97.78 REMARK 500 1 LYS A 33 45.21 75.47 REMARK 500 1 GLN A 39 -37.51 -38.87 REMARK 500 1 ASP A 46 93.54 -57.42 REMARK 500 1 SER A 64 27.17 -146.11 REMARK 500 1 GLN A 66 51.82 -167.36 REMARK 500 1 ASP A 69 -53.40 -179.65 REMARK 500 1 ASP A 89 -49.09 -140.82 REMARK 500 1 ALA A 118 -60.27 72.43 REMARK 500 2 LYS A 29 -81.85 -76.04 REMARK 500 2 ALA A 31 57.49 -145.84 REMARK 500 2 ILE A 32 55.90 -92.55 REMARK 500 2 GLU A 35 -31.90 -39.47 REMARK 500 2 ASP A 46 103.20 -53.34 REMARK 500 2 SER A 64 64.68 -68.81 REMARK 500 2 ILE A 65 39.06 -91.23 REMARK 500 2 LEU A 70 76.42 -114.83 REMARK 500 2 ASP A 85 94.70 -65.53 REMARK 500 2 ASP A 89 -47.86 -144.62 REMARK 500 2 ILE A 106 78.11 -68.80 REMARK 500 2 ASP A 117 79.74 -68.00 REMARK 500 2 ASP A 121 -42.73 -178.36 REMARK 500 3 ASP A 14 -47.96 -153.12 REMARK 500 3 LYS A 29 -75.32 -74.50 REMARK 500 3 ALA A 31 51.80 -148.29 REMARK 500 3 ILE A 32 -70.58 -109.02 REMARK 500 3 ASP A 46 105.72 -42.54 REMARK 500 3 SER A 64 55.63 -174.21 REMARK 500 3 ILE A 65 43.08 -108.85 REMARK 500 3 ALA A 118 -60.76 71.07 REMARK 500 4 ASP A 10 76.00 -65.52 REMARK 500 4 LYS A 29 -77.40 -86.56 REMARK 500 4 ALA A 31 53.50 -147.70 REMARK 500 4 GLU A 35 -29.83 -39.74 REMARK 500 4 ASP A 46 95.23 -49.57 REMARK 500 4 ILE A 65 41.28 -101.32 REMARK 500 4 ASP A 85 91.38 -54.13 REMARK 500 4 ASP A 89 -48.90 -134.02 REMARK 500 4 GLU A 107 -27.94 -39.62 REMARK 500 4 ASP A 117 77.71 -65.79 REMARK 500 4 ASP A 121 -44.66 -176.91 REMARK 500 5 ASP A 14 -48.01 -137.31 REMARK 500 5 LYS A 29 -71.39 -74.73 REMARK 500 5 ALA A 31 57.43 -141.92 REMARK 500 5 ILE A 32 55.27 -91.10 REMARK 500 5 GLU A 35 -33.95 -38.97 REMARK 500 5 ASP A 46 94.48 -48.53 REMARK 500 5 GLN A 66 -48.47 -175.50 REMARK 500 REMARK 500 THIS ENTRY HAS 202 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JFK RELATED DB: PDB REMARK 900 1JFK CONTAINS SAME PROTEIN COMPLEX WITH CALCIUM. REMARK 900 RELATED ID: 4271 RELATED DB: BMRB REMARK 900 4271 CONTAINS ASSIGNED CHEMICAL SHIFT LISTS DBREF 1JFJ A 1 134 UNP P38505 CALBP_ENTHI 1 134 SEQADV 1JFJ GLU A 131 UNP P38505 UNK 131 CONFLICT SEQRES 1 A 134 MET ALA GLU ALA LEU PHE LYS GLU ILE ASP VAL ASN GLY SEQRES 2 A 134 ASP GLY ALA VAL SER TYR GLU GLU VAL LYS ALA PHE VAL SEQRES 3 A 134 SER LYS LYS ARG ALA ILE LYS ASN GLU GLN LEU LEU GLN SEQRES 4 A 134 LEU ILE PHE LYS SER ILE ASP ALA ASP GLY ASN GLY GLU SEQRES 5 A 134 ILE ASP GLN ASN GLU PHE ALA LYS PHE TYR GLY SER ILE SEQRES 6 A 134 GLN GLY GLN ASP LEU SER ASP ASP LYS ILE GLY LEU LYS SEQRES 7 A 134 VAL LEU TYR LYS LEU MET ASP VAL ASP GLY ASP GLY LYS SEQRES 8 A 134 LEU THR LYS GLU GLU VAL THR SER PHE PHE LYS LYS HIS SEQRES 9 A 134 GLY ILE GLU LYS VAL ALA GLU GLN VAL MET LYS ALA ASP SEQRES 10 A 134 ALA ASN GLY ASP GLY TYR ILE THR LEU GLU GLU PHE LEU SEQRES 11 A 134 GLU PHE SER LEU HELIX 1 1 MET A 1 ASP A 10 1 10 HELIX 2 2 TYR A 19 LYS A 28 1 10 HELIX 3 3 LYS A 33 ASP A 46 1 14 HELIX 4 4 GLN A 55 TYR A 62 1 8 HELIX 5 5 LEU A 70 ASP A 85 1 16 HELIX 6 6 LYS A 94 LYS A 102 1 9 HELIX 7 7 ILE A 106 ALA A 118 1 13 HELIX 8 8 LEU A 126 LEU A 134 1 9 SHEET 1 A 2 ALA A 16 SER A 18 0 SHEET 2 A 2 GLU A 52 ASP A 54 -1 O ILE A 53 N VAL A 17 SHEET 1 B 2 LYS A 91 THR A 93 0 SHEET 2 B 2 TYR A 123 THR A 125 -1 N ILE A 124 O LEU A 92 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