Header list of 1fuw.pdb file
Complete list - v 3 2 Bytes
HEADER PLANT PROTEIN 18-SEP-00 1FUW TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF A DOUBLE MUTANT SINGLE- TITLE 2 CHAIN MONELLIN(SCM) DETERMINED BY NUCLEAR MAGNETIC RESONANCE TITLE 3 SPECTROSCOPY COMPND MOL_ID: 1; COMPND 2 MOLECULE: MONELLIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 OTHER_DETAILS: CHAINS B AND A IN A SINGLE CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: DIOSCOREOPHYLLUM CUMMINSII; SOURCE 3 ORGANISM_COMMON: SERENDIPITY BERRY; SOURCE 4 ORGANISM_TAXID: 3457; 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: PET21 KEYWDS BETA-SHEET, ALPHA-HELIX, LOOP, PLANT PROTEIN EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR Y.H.SUNG,J.SHIN,J.JUNG,W.LEE REVDAT 3 03-NOV-21 1FUW 1 REMARK SEQADV REVDAT 2 24-FEB-09 1FUW 1 VERSN REVDAT 1 06-JUN-01 1FUW 0 JRNL AUTH Y.H.SUNG,J.SHIN,H.J.CHANG,J.M.CHO,W.LEE JRNL TITL SOLUTION STRUCTURE, BACKBONE DYNAMICS, AND STABILITY OF A JRNL TITL 2 DOUBLE MUTANT SINGLE-CHAIN MONELLIN. STRUCTURAL ORIGIN OF JRNL TITL 3 SWEETNESS. JRNL REF J.BIOL.CHEM. V. 276 19624 2001 JRNL REFN ISSN 0021-9258 JRNL PMID 11279156 JRNL DOI 10.1074/JBC.M100930200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1FUW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-00. REMARK 100 THE DEPOSITION ID IS D_1000011918. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM MONELLIN ;50MM PHOTASSIUM REMARK 210 PHOSPHATE BUFFER ;90% H20,10% REMARK 210 D2O; 2MM MONELLIN 15N ;50MM REMARK 210 PHOTASSIUM PHOSPHATE BUFFER ;90% REMARK 210 H2O , 10% D2O; 2MM MONELLIN ; REMARK 210 50MM PHOTASSIUM PHOSPHATE BUFFER REMARK 210 ;100% D2O; 2MM MONELLIN 15N ; REMARK 210 50MM PHOTASSIUM PHOSPHATE BUFFER REMARK 210 ;100% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; DQF-COSY; HNHA; REMARK 210 HSQC(EXCHANGE) REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 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: 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 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 46 H GLY A 55 1.57 REMARK 500 O TYR A 58 H ILE A 73 1.58 REMARK 500 O GLU A 48 HD21 ASN A 49 1.60 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 GLU A 2 128.35 177.68 REMARK 500 1 TRP A 3 -153.95 171.07 REMARK 500 1 GLU A 4 -170.82 162.89 REMARK 500 1 ILE A 5 151.99 -38.49 REMARK 500 1 ILE A 6 -65.68 -128.27 REMARK 500 1 PHE A 11 -37.08 -36.75 REMARK 500 1 GLU A 23 -30.87 -37.00 REMARK 500 1 LYS A 25 -92.37 -45.82 REMARK 500 1 THR A 33 74.11 -156.03 REMARK 500 1 ILE A 38 -93.04 -173.36 REMARK 500 1 LYS A 39 164.41 56.13 REMARK 500 1 PRO A 40 85.11 -53.47 REMARK 500 1 CYS A 41 -169.37 -76.36 REMARK 500 1 MET A 42 156.66 176.36 REMARK 500 1 GLU A 48 -90.65 -72.51 REMARK 500 1 ASN A 49 -45.39 -150.50 REMARK 500 1 ARG A 51 42.01 84.92 REMARK 500 1 ILE A 53 -77.54 -147.47 REMARK 500 1 LYS A 67 -173.40 158.03 REMARK 500 1 ARG A 70 132.69 177.77 REMARK 500 1 LYS A 78 -28.47 99.52 REMARK 500 1 THR A 79 40.27 174.96 REMARK 500 1 ARG A 80 -166.64 -125.87 REMARK 500 1 LYS A 83 159.93 160.53 REMARK 500 1 LEU A 85 -76.53 -145.25 REMARK 500 1 ARG A 86 141.98 -28.26 REMARK 500 1 PHE A 87 58.03 -168.77 REMARK 500 1 PRO A 90 173.80 -52.19 REMARK 500 2 GLU A 2 119.96 67.16 REMARK 500 2 TRP A 3 -88.48 -142.34 REMARK 500 2 GLU A 4 163.75 161.73 REMARK 500 2 ILE A 8 19.77 -144.15 REMARK 500 2 LYS A 25 -76.95 -96.21 REMARK 500 2 LEU A 32 92.58 -69.99 REMARK 500 2 ILE A 38 -110.43 -162.19 REMARK 500 2 LYS A 39 164.02 61.15 REMARK 500 2 PRO A 40 86.36 -51.87 REMARK 500 2 CYS A 41 -165.73 -79.45 REMARK 500 2 LYS A 44 117.39 -170.79 REMARK 500 2 GLU A 48 -82.76 -76.62 REMARK 500 2 ASN A 49 -57.47 -168.50 REMARK 500 2 ILE A 53 -88.06 -144.60 REMARK 500 2 LYS A 54 59.60 75.86 REMARK 500 2 TYR A 56 112.65 -175.04 REMARK 500 2 VAL A 62 90.45 -63.37 REMARK 500 2 LYS A 67 -173.60 177.58 REMARK 500 2 PHE A 69 69.83 -166.92 REMARK 500 2 THR A 79 18.60 -145.27 REMARK 500 2 ARG A 80 46.11 70.91 REMARK 500 2 ARG A 82 81.59 165.05 REMARK 500 REMARK 500 THIS ENTRY HAS 503 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1MNL RELATED DB: PDB REMARK 900 1MNL CONTAINS THE WILD TYPE SINGLE-CHAIN MONELLIN. REMARK 900 RELATED ID: 1MOL RELATED DB: PDB REMARK 900 1MOL CONTAINS THE NATURAL MONELLIN AND SINGLE-CHAIN MONELLIN. DBREF 1FUW A 1 50 UNP P02882 MONB_DIOCU 1 50 DBREF 1FUW A 51 91 UNP P02881 MONA_DIOCU 2 42 SEQADV 1FUW GLU A 7 UNP P02882 ASP 7 ENGINEERED MUTATION SEQADV 1FUW LYS A 39 UNP P02882 ARG 39 ENGINEERED MUTATION SEQADV 1FUW ASN A 49 UNP P02882 GLU 49 SEE REMARK 999 SEQADV 1FUW GLU A 50 UNP P02882 ASN 50 SEE REMARK 999 SEQRES 1 A 91 GLY GLU TRP GLU ILE ILE GLU ILE GLY PRO PHE THR GLN SEQRES 2 A 91 ASN LEU GLY LYS PHE ALA VAL ASP GLU GLU ASN LYS ILE SEQRES 3 A 91 GLY GLN TYR GLY ARG LEU THR PHE ASN LYS VAL ILE LYS SEQRES 4 A 91 PRO CYS MET LYS LYS THR ILE TYR GLU ASN GLU ARG GLU SEQRES 5 A 91 ILE LYS GLY TYR GLU TYR GLN LEU TYR VAL TYR ALA SER SEQRES 6 A 91 ASP LYS LEU PHE ARG ALA ASP ILE SER GLU ASP TYR LYS SEQRES 7 A 91 THR ARG GLY ARG LYS LEU LEU ARG PHE ASN GLY PRO VAL HELIX 1 1 GLY A 9 GLU A 23 1 15 SHEET 1 A 4 VAL A 37 ILE A 46 0 SHEET 2 A 4 GLY A 55 VAL A 62 -1 N GLY A 55 O ILE A 46 SHEET 3 A 4 ALA A 71 GLU A 75 -1 O ALA A 71 N LEU A 60 SHEET 4 A 4 ARG A 82 LEU A 84 -1 N LYS A 83 O SER A 74 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 - v 3 2 Bytes