Header list of 1fa3.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 12-JUL-00 1FA3
TITLE SOLUTION STRUCTURE OF MNEI, A SWEET PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MNEI SWEET PROTEIN RELATED TO MONELLIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-22B+
KEYWDS 5 STRANDED BETA SHEET 1 HELIX, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.A.TEMUSSI,R.SPADACCINI
REVDAT 6 23-FEB-22 1FA3 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1FA3 1 VERSN
REVDAT 4 01-APR-03 1FA3 1 JRNL
REVDAT 3 21-MAR-01 1FA3 3 ATOM
REVDAT 2 17-JAN-01 1FA3 1 JRNL
REVDAT 1 16-NOV-00 1FA3 0
JRNL AUTH R.SPADACCINI,O.CRESCENZI,T.TANCREDI,N.DE CASAMASSIMI,
JRNL AUTH 2 G.SAVIANO,R.SCOGNAMIGLIO,A.DI DONATO,P.A.TEMUSSI
JRNL TITL SOLUTION STRUCTURE OF A SWEET PROTEIN: NMR STUDY OF MNEI, A
JRNL TITL 2 SINGLE CHAIN MONELLIN.
JRNL REF J.MOL.BIOL. V. 305 505 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11152608
JRNL DOI 10.1006/JMBI.2000.4304
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, AMBER 5.0
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1169 DISTANCE CONSTRAINTS,
REMARK 3 184 DIHEDRAL ANGLE RESTRAINTS AND 60 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1FA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011430.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308; 308
REMARK 210 PH : 2.9; 2.9; 2.9
REMARK 210 IONIC STRENGTH : 18.5 MM PHOSPHATE BUFFER; 18.5
REMARK 210 MM PHOSPHATE BUFFER; 18.5 MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM MNEI U-15N; 18.5MM PHOSPHATE
REMARK 210 BUFFER K; 90% H2O, 10% D2O; 2MM
REMARK 210 MNEI; 18.5MM PHOSPHATE BUFFER K;
REMARK 210 90% H2O, 10% D2O; 2MM MNEI;
REMARK 210 18.5MM PHOSPHATE BUFFER; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 HSQC; HNHB; E-COSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS ENERGY
REMARK 210 RESTRAINED MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 TRP A 3 72.80 32.34
REMARK 500 1 ASN A 35 -66.23 -105.82
REMARK 500 1 GLU A 48 -149.03 -153.90
REMARK 500 1 ASN A 49 -46.25 70.44
REMARK 500 1 GLU A 50 165.83 67.14
REMARK 500 1 ARG A 53 154.08 73.25
REMARK 500 2 GLU A 2 -172.39 62.43
REMARK 500 2 ASN A 35 -66.09 -104.07
REMARK 500 2 LYS A 36 -168.59 -164.93
REMARK 500 2 GLU A 48 -153.73 -102.51
REMARK 500 2 ASN A 49 -38.06 -178.43
REMARK 500 2 GLU A 50 82.06 -60.87
REMARK 500 2 PHE A 52 159.26 81.82
REMARK 500 3 ASN A 35 -63.18 -103.20
REMARK 500 3 PHE A 52 73.24 -170.61
REMARK 500 3 ARG A 53 89.91 62.39
REMARK 500 3 ASP A 68 17.76 53.34
REMARK 500 3 LEU A 87 -64.54 -106.33
REMARK 500 4 ASN A 49 -36.54 -168.13
REMARK 500 4 PHE A 52 167.98 61.43
REMARK 500 4 SER A 67 -60.85 72.37
REMARK 500 4 ASP A 68 0.23 -177.10
REMARK 500 4 THR A 81 16.29 -144.95
REMARK 500 5 TRP A 3 98.42 53.27
REMARK 500 5 ASN A 35 -66.19 -120.84
REMARK 500 5 THR A 81 15.35 -143.14
REMARK 500 6 ASN A 35 -68.50 -101.02
REMARK 500 6 GLU A 48 -143.97 -82.49
REMARK 500 6 ASN A 49 -48.03 -166.26
REMARK 500 6 ARG A 53 68.53 36.64
REMARK 500 7 ASN A 35 -66.87 -106.49
REMARK 500 7 LYS A 36 -169.39 -167.40
REMARK 500 7 GLU A 50 -176.07 59.70
REMARK 500 7 PHE A 52 -55.43 -140.02
REMARK 500 7 ARG A 53 148.48 -172.48
REMARK 500 7 GLU A 54 96.00 -165.77
REMARK 500 7 SER A 67 -64.17 70.74
REMARK 500 7 ASP A 68 11.09 179.72
REMARK 500 8 ASN A 35 -67.41 -100.27
REMARK 500 8 LYS A 36 -159.50 -169.57
REMARK 500 8 ASN A 49 -51.25 -158.69
REMARK 500 8 GLU A 50 105.20 -54.66
REMARK 500 8 PHE A 52 84.46 74.16
REMARK 500 9 ASN A 35 -64.51 -102.82
REMARK 500 9 GLU A 50 84.57 -7.42
REMARK 500 9 PHE A 52 -66.18 -156.67
REMARK 500 9 ARG A 53 145.99 -170.79
REMARK 500 9 GLU A 54 114.34 -162.36
REMARK 500 9 LYS A 85 143.18 -174.94
REMARK 500 10 GLU A 2 71.96 179.90
REMARK 500
REMARK 500 THIS ENTRY HAS 107 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 TYR A 29 0.10 SIDE CHAIN
REMARK 500 1 TYR A 58 0.07 SIDE CHAIN
REMARK 500 2 TYR A 58 0.07 SIDE CHAIN
REMARK 500 2 ARG A 88 0.08 SIDE CHAIN
REMARK 500 3 TYR A 29 0.08 SIDE CHAIN
REMARK 500 3 TYR A 60 0.07 SIDE CHAIN
REMARK 500 3 TYR A 79 0.07 SIDE CHAIN
REMARK 500 4 TYR A 58 0.08 SIDE CHAIN
REMARK 500 4 ARG A 72 0.09 SIDE CHAIN
REMARK 500 5 TYR A 47 0.09 SIDE CHAIN
REMARK 500 6 TYR A 47 0.07 SIDE CHAIN
REMARK 500 6 TYR A 58 0.07 SIDE CHAIN
REMARK 500 7 PHE A 18 0.12 SIDE CHAIN
REMARK 500 7 TYR A 47 0.09 SIDE CHAIN
REMARK 500 7 TYR A 58 0.07 SIDE CHAIN
REMARK 500 7 TYR A 63 0.09 SIDE CHAIN
REMARK 500 8 PHE A 18 0.15 SIDE CHAIN
REMARK 500 8 PHE A 34 0.10 SIDE CHAIN
REMARK 500 8 TYR A 47 0.06 SIDE CHAIN
REMARK 500 8 TYR A 65 0.08 SIDE CHAIN
REMARK 500 9 TYR A 29 0.10 SIDE CHAIN
REMARK 500 9 TYR A 47 0.07 SIDE CHAIN
REMARK 500 9 TYR A 60 0.11 SIDE CHAIN
REMARK 500 10 TYR A 29 0.08 SIDE CHAIN
REMARK 500 10 TYR A 58 0.10 SIDE CHAIN
REMARK 500 10 TYR A 65 0.07 SIDE CHAIN
REMARK 500 11 TYR A 29 0.08 SIDE CHAIN
REMARK 500 11 TYR A 58 0.07 SIDE CHAIN
REMARK 500 11 PHE A 89 0.09 SIDE CHAIN
REMARK 500 12 PHE A 18 0.11 SIDE CHAIN
REMARK 500 12 TYR A 29 0.08 SIDE CHAIN
REMARK 500 12 TYR A 60 0.12 SIDE CHAIN
REMARK 500 13 TYR A 47 0.09 SIDE CHAIN
REMARK 500 13 TYR A 58 0.06 SIDE CHAIN
REMARK 500 13 TYR A 65 0.07 SIDE CHAIN
REMARK 500 14 TYR A 29 0.09 SIDE CHAIN
REMARK 500 14 TYR A 58 0.08 SIDE CHAIN
REMARK 500 14 PHE A 89 0.11 SIDE CHAIN
REMARK 500 15 TYR A 29 0.10 SIDE CHAIN
REMARK 500 15 TYR A 60 0.07 SIDE CHAIN
REMARK 500 15 PHE A 71 0.08 SIDE CHAIN
REMARK 500 16 TYR A 47 0.08 SIDE CHAIN
REMARK 500 16 TYR A 58 0.07 SIDE CHAIN
REMARK 500 17 TYR A 47 0.09 SIDE CHAIN
REMARK 500 17 PHE A 71 0.07 SIDE CHAIN
REMARK 500 17 TYR A 79 0.11 SIDE CHAIN
REMARK 500 18 PHE A 18 0.08 SIDE CHAIN
REMARK 500 18 TYR A 29 0.10 SIDE CHAIN
REMARK 500 18 TYR A 58 0.07 SIDE CHAIN
REMARK 500 19 TYR A 58 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FA3 A 1 48 UNP P02882 MONB_DIOCU 1 48
DBREF 1FA3 A 52 96 UNP P02881 MONA_DIOCU 1 45
SEQADV 1FA3 ASN A 49 UNP P02882 GLU 49 CONFLICT
SEQADV 1FA3 GLU A 50 UNP P02882 ASN 50 CONFLICT
SEQADV 1FA3 GLY A 51 P02882 INSERTION
SEQRES 1 A 96 GLY GLU TRP GLU ILE ILE ASP ILE GLY PRO PHE THR GLN
SEQRES 2 A 96 ASN LEU GLY LYS PHE ALA VAL ASP GLU GLU ASN LYS ILE
SEQRES 3 A 96 GLY GLN TYR GLY ARG LEU THR PHE ASN LYS VAL ILE ARG
SEQRES 4 A 96 PRO CYS MET LYS LYS THR ILE TYR GLU ASN GLU GLY PHE
SEQRES 5 A 96 ARG GLU ILE LYS GLY TYR GLU TYR GLN LEU TYR VAL TYR
SEQRES 6 A 96 ALA SER ASP LYS LEU PHE ARG ALA ASP ILE SER GLU ASP
SEQRES 7 A 96 TYR LYS THR ARG GLY ARG LYS LEU LEU ARG PHE ASN GLY
SEQRES 8 A 96 PRO VAL PRO PRO PRO
HELIX 1 1 GLY A 9 GLY A 27 1 19
SHEET 1 A 5 GLU A 4 ILE A 5 0
SHEET 2 A 5 PHE A 34 GLU A 48 -1 N LYS A 43 O GLU A 4
SHEET 3 A 5 GLU A 54 ALA A 66 -1 O GLU A 54 N GLU A 48
SHEET 4 A 5 LYS A 69 ASP A 78 -1 O LYS A 69 N ALA A 66
SHEET 5 A 5 GLY A 83 ASN A 90 -1 O GLY A 83 N ASP A 78
CISPEP 1 ARG A 39 PRO A 40 1 -3.13
CISPEP 2 GLY A 91 PRO A 92 1 2.97
CISPEP 3 ARG A 39 PRO A 40 2 -5.79
CISPEP 4 GLY A 91 PRO A 92 2 2.12
CISPEP 5 ARG A 39 PRO A 40 3 -3.36
CISPEP 6 GLY A 91 PRO A 92 3 -6.75
CISPEP 7 ARG A 39 PRO A 40 4 -9.20
CISPEP 8 GLY A 91 PRO A 92 4 3.14
CISPEP 9 ARG A 39 PRO A 40 5 -4.53
CISPEP 10 GLY A 91 PRO A 92 5 -2.80
CISPEP 11 ARG A 39 PRO A 40 6 -4.54
CISPEP 12 GLY A 91 PRO A 92 6 -1.94
CISPEP 13 ARG A 39 PRO A 40 7 -8.54
CISPEP 14 GLY A 91 PRO A 92 7 -2.57
CISPEP 15 ARG A 39 PRO A 40 8 -7.57
CISPEP 16 GLY A 91 PRO A 92 8 0.10
CISPEP 17 ARG A 39 PRO A 40 9 -4.79
CISPEP 18 GLY A 91 PRO A 92 9 2.60
CISPEP 19 ARG A 39 PRO A 40 10 -9.62
CISPEP 20 GLY A 91 PRO A 92 10 2.98
CISPEP 21 ARG A 39 PRO A 40 11 -1.50
CISPEP 22 GLY A 91 PRO A 92 11 -3.52
CISPEP 23 ARG A 39 PRO A 40 12 0.74
CISPEP 24 GLY A 91 PRO A 92 12 2.14
CISPEP 25 ARG A 39 PRO A 40 13 4.76
CISPEP 26 GLY A 91 PRO A 92 13 1.83
CISPEP 27 ARG A 39 PRO A 40 14 -4.67
CISPEP 28 GLY A 91 PRO A 92 14 2.99
CISPEP 29 ARG A 39 PRO A 40 15 -5.33
CISPEP 30 GLY A 91 PRO A 92 15 1.64
CISPEP 31 ARG A 39 PRO A 40 16 0.05
CISPEP 32 GLY A 91 PRO A 92 16 -0.57
CISPEP 33 ARG A 39 PRO A 40 17 0.18
CISPEP 34 GLY A 91 PRO A 92 17 1.32
CISPEP 35 ARG A 39 PRO A 40 18 -3.26
CISPEP 36 GLY A 91 PRO A 92 18 -1.97
CISPEP 37 ARG A 39 PRO A 40 19 -1.32
CISPEP 38 GLY A 91 PRO A 92 19 2.49
CISPEP 39 ARG A 39 PRO A 40 20 -7.90
CISPEP 40 GLY A 91 PRO A 92 20 -1.99
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