Header list of 1m9g.pdb file
Complete list - v 10 2 Bytes
HEADER PLANT PROTEIN 29-JUL-02 1M9G
TITLE SOLUTION STRUCTURE OF G16A-MNEI, A STRUCTURAL MUTANT OF SINGLE CHAIN
TITLE 2 MONELLIN MNEI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONELLIN CHAIN B AND MONELLIN CHAIN A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MNEI;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 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: PET22B+
KEYWDS 5 STRANDED BETA SHEET 1 HELIX, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.SPADACCINI,F.TRABUCCO,G.SAVIANO,D.PICONE,O.CRESCENZI,T.TANCREDI,
AUTHOR 2 P.A.TEMUSSI
REVDAT 3 10-NOV-21 1M9G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1M9G 1 VERSN
REVDAT 1 10-JUN-03 1M9G 0
JRNL AUTH R.SPADACCINI,F.TRABUCCO,G.SAVIANO,D.PICONE,O.CRESCENZI,
JRNL AUTH 2 T.TANCREDI,P.A.TEMUSSI
JRNL TITL THE MECHANISM OF INTERACTION OF SWEET PROTEINS WITH THE
JRNL TITL 2 T1R2-T1R3 RECEPTOR: EVIDENCE FROM THE SOLUTION STRUCTURE OF
JRNL TITL 3 G16A-MNEI
JRNL REF J.MOL.BIOL. V. 328 683 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12706725
JRNL DOI 10.1016/S0022-2836(03)00346-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, DYANA 1.5
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), GUENTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M9G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000016762.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 2.9
REMARK 210 IONIC STRENGTH : 18.5MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM G16A MNEI; 18.5 MM PHOSPHATE
REMARK 210 BUFFER K; 90% H2O, 10% D2O; 2MM
REMARK 210 G16A MNEI U-15N; 18.5MM
REMARK 210 PHOSPHATE BUFFER K;90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARETED_TOCSY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB; HSQC
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 : NMRVIEW 4.0.3, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES.
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 3 TYR A 59 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 6 LEU A 33 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 9 TYR A 59 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 11 TYR A 48 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
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 3 -164.62 -125.66
REMARK 500 1 PHE A 12 -66.51 -157.61
REMARK 500 1 LEU A 33 -128.83 -78.88
REMARK 500 1 PHE A 35 77.82 0.65
REMARK 500 1 ASN A 36 -88.42 -87.75
REMARK 500 1 LYS A 37 -174.93 -177.77
REMARK 500 1 ARG A 40 146.55 65.02
REMARK 500 1 PRO A 41 -172.06 -69.57
REMARK 500 1 GLU A 49 39.57 -83.05
REMARK 500 1 ASN A 50 82.14 -58.57
REMARK 500 1 ILE A 56 103.58 62.39
REMARK 500 1 SER A 68 -77.55 62.59
REMARK 500 1 ASP A 69 31.43 -170.83
REMARK 500 1 THR A 82 -100.61 -115.51
REMARK 500 1 ARG A 83 50.79 -174.67
REMARK 500 1 LEU A 87 104.56 -59.98
REMARK 500 1 PHE A 90 70.96 61.70
REMARK 500 2 GLU A 3 165.89 74.67
REMARK 500 2 PHE A 12 -75.94 -151.96
REMARK 500 2 TYR A 30 -61.84 -132.24
REMARK 500 2 ARG A 32 48.37 -78.70
REMARK 500 2 LEU A 33 -128.33 45.75
REMARK 500 2 PHE A 35 71.90 32.42
REMARK 500 2 ASN A 36 -128.64 -88.88
REMARK 500 2 ASN A 50 92.09 -49.62
REMARK 500 2 TYR A 66 64.13 -101.19
REMARK 500 2 THR A 82 -93.45 -165.83
REMARK 500 2 ARG A 83 43.37 -179.22
REMARK 500 2 LEU A 87 109.02 -53.58
REMARK 500 2 PHE A 90 77.21 69.70
REMARK 500 3 GLU A 3 -179.69 67.57
REMARK 500 3 ILE A 27 -64.37 -92.38
REMARK 500 3 GLN A 29 -75.07 -94.49
REMARK 500 3 TYR A 30 -64.24 -100.64
REMARK 500 3 ARG A 32 62.70 -69.00
REMARK 500 3 LEU A 33 -125.37 45.39
REMARK 500 3 PHE A 35 72.94 17.23
REMARK 500 3 ASN A 36 -94.64 -92.86
REMARK 500 3 LYS A 37 -177.19 -176.96
REMARK 500 3 GLU A 49 38.13 -87.93
REMARK 500 3 ASN A 50 162.32 61.63
REMARK 500 3 GLU A 51 179.24 68.01
REMARK 500 3 ARG A 54 70.80 40.92
REMARK 500 3 ILE A 56 108.50 -26.00
REMARK 500 3 TYR A 66 54.06 -95.50
REMARK 500 3 THR A 82 -92.24 -113.73
REMARK 500 3 ARG A 83 50.72 -172.46
REMARK 500 3 PHE A 90 64.78 66.97
REMARK 500 4 ASP A 8 81.17 -169.62
REMARK 500 4 TYR A 30 -48.77 -138.61
REMARK 500
REMARK 500 THIS ENTRY HAS 274 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 61 0.08 SIDE CHAIN
REMARK 500 1 TYR A 66 0.11 SIDE CHAIN
REMARK 500 1 TYR A 80 0.06 SIDE CHAIN
REMARK 500 2 TYR A 30 0.10 SIDE CHAIN
REMARK 500 3 TYR A 30 0.08 SIDE CHAIN
REMARK 500 3 TYR A 80 0.08 SIDE CHAIN
REMARK 500 4 TYR A 66 0.09 SIDE CHAIN
REMARK 500 4 PHE A 90 0.10 SIDE CHAIN
REMARK 500 5 PHE A 12 0.08 SIDE CHAIN
REMARK 500 5 TYR A 48 0.20 SIDE CHAIN
REMARK 500 7 TYR A 66 0.07 SIDE CHAIN
REMARK 500 8 PHE A 12 0.13 SIDE CHAIN
REMARK 500 8 TYR A 48 0.08 SIDE CHAIN
REMARK 500 8 TYR A 59 0.07 SIDE CHAIN
REMARK 500 8 TYR A 66 0.06 SIDE CHAIN
REMARK 500 9 TYR A 59 0.10 SIDE CHAIN
REMARK 500 10 PHE A 19 0.12 SIDE CHAIN
REMARK 500 11 PHE A 12 0.09 SIDE CHAIN
REMARK 500 11 TYR A 59 0.06 SIDE CHAIN
REMARK 500 12 PHE A 19 0.21 SIDE CHAIN
REMARK 500 12 PHE A 90 0.10 SIDE CHAIN
REMARK 500 13 TYR A 48 0.14 SIDE CHAIN
REMARK 500 14 PHE A 12 0.12 SIDE CHAIN
REMARK 500 14 TYR A 66 0.12 SIDE CHAIN
REMARK 500 15 ARG A 32 0.11 SIDE CHAIN
REMARK 500 15 TYR A 59 0.07 SIDE CHAIN
REMARK 500 15 PHE A 90 0.12 SIDE CHAIN
REMARK 500 16 TYR A 61 0.11 SIDE CHAIN
REMARK 500 17 PHE A 12 0.10 SIDE CHAIN
REMARK 500 17 TYR A 30 0.14 SIDE CHAIN
REMARK 500 18 PHE A 12 0.11 SIDE CHAIN
REMARK 500 18 TYR A 30 0.12 SIDE CHAIN
REMARK 500 18 TYR A 59 0.10 SIDE CHAIN
REMARK 500 18 TYR A 61 0.08 SIDE CHAIN
REMARK 500 19 PHE A 12 0.10 SIDE CHAIN
REMARK 500 19 TYR A 48 0.14 SIDE CHAIN
REMARK 500 19 ARG A 85 0.12 SIDE CHAIN
REMARK 500 20 TYR A 61 0.09 SIDE CHAIN
REMARK 500 20 TYR A 66 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M9G A 2 49 UNP P02882 MONB_DIOCU 1 48
DBREF 1M9G A 53 97 UNP P02881 MONA_DIOCU 1 45
SEQADV 1M9G MET A 1 UNP P02882 INITIATING METHIONINE
SEQADV 1M9G ALA A 17 UNP P02882 GLY 16 ENGINEERED MUTATION
SEQADV 1M9G ASN A 50 UNP P02882 LINKER
SEQADV 1M9G GLU A 51 UNP P02882 LINKER
SEQADV 1M9G GLY A 52 UNP P02882 LINKER
SEQRES 1 A 97 MET GLY GLU TRP GLU ILE ILE ASP ILE GLY PRO PHE THR
SEQRES 2 A 97 GLN ASN LEU ALA LYS PHE ALA VAL ASP GLU GLU ASN LYS
SEQRES 3 A 97 ILE GLY GLN TYR GLY ARG LEU THR PHE ASN LYS VAL ILE
SEQRES 4 A 97 ARG PRO CYS MET LYS LYS THR ILE TYR GLU ASN GLU GLY
SEQRES 5 A 97 PHE ARG GLU ILE LYS GLY TYR GLU TYR GLN LEU TYR VAL
SEQRES 6 A 97 TYR ALA SER ASP LYS LEU PHE ARG ALA ASP ILE SER GLU
SEQRES 7 A 97 ASP TYR LYS THR ARG GLY ARG LYS LEU LEU ARG PHE ASN
SEQRES 8 A 97 GLY PRO VAL PRO PRO PRO
HELIX 1 1 PHE A 12 GLY A 28 1 17
SHEET 1 A 4 LYS A 86 VAL A 94 0
SHEET 2 A 4 LYS A 70 SER A 77 -1 N SER A 77 O LYS A 86
SHEET 3 A 4 GLY A 58 ALA A 67 -1 N LEU A 63 O ALA A 74
SHEET 4 A 4 LYS A 37 VAL A 38 -1 N LYS A 37 O TYR A 66
SHEET 1 B 5 LYS A 86 VAL A 94 0
SHEET 2 B 5 LYS A 70 SER A 77 -1 N SER A 77 O LYS A 86
SHEET 3 B 5 GLY A 58 ALA A 67 -1 N LEU A 63 O ALA A 74
SHEET 4 B 5 MET A 43 ILE A 47 -1 N LYS A 45 O GLU A 60
SHEET 5 B 5 GLU A 5 ILE A 6 -1 N GLU A 5 O LYS A 44
CISPEP 1 ARG A 40 PRO A 41 1 -10.59
CISPEP 2 GLY A 92 PRO A 93 1 -2.02
CISPEP 3 ARG A 40 PRO A 41 2 -5.69
CISPEP 4 GLY A 92 PRO A 93 2 -1.91
CISPEP 5 ARG A 40 PRO A 41 3 -6.82
CISPEP 6 GLY A 92 PRO A 93 3 -6.11
CISPEP 7 ARG A 40 PRO A 41 4 -3.08
CISPEP 8 GLY A 92 PRO A 93 4 -6.05
CISPEP 9 ARG A 40 PRO A 41 5 -5.96
CISPEP 10 GLY A 92 PRO A 93 5 -3.79
CISPEP 11 ARG A 40 PRO A 41 6 -10.81
CISPEP 12 GLY A 92 PRO A 93 6 -1.32
CISPEP 13 ARG A 40 PRO A 41 7 -5.87
CISPEP 14 GLY A 92 PRO A 93 7 -1.91
CISPEP 15 ARG A 40 PRO A 41 8 -3.31
CISPEP 16 GLY A 92 PRO A 93 8 -2.52
CISPEP 17 ARG A 40 PRO A 41 9 -0.54
CISPEP 18 GLY A 92 PRO A 93 9 -1.50
CISPEP 19 ARG A 40 PRO A 41 10 -10.71
CISPEP 20 GLY A 92 PRO A 93 10 -1.80
CISPEP 21 ARG A 40 PRO A 41 11 -6.23
CISPEP 22 GLY A 92 PRO A 93 11 -2.06
CISPEP 23 ARG A 40 PRO A 41 12 4.07
CISPEP 24 GLY A 92 PRO A 93 12 -3.46
CISPEP 25 ARG A 40 PRO A 41 13 -6.48
CISPEP 26 GLY A 92 PRO A 93 13 -3.94
CISPEP 27 ARG A 40 PRO A 41 14 -6.60
CISPEP 28 GLY A 92 PRO A 93 14 -3.13
CISPEP 29 ARG A 40 PRO A 41 15 -5.88
CISPEP 30 GLY A 92 PRO A 93 15 -3.28
CISPEP 31 ARG A 40 PRO A 41 16 -5.47
CISPEP 32 GLY A 92 PRO A 93 16 -2.11
CISPEP 33 ARG A 40 PRO A 41 17 -2.21
CISPEP 34 GLY A 92 PRO A 93 17 -1.12
CISPEP 35 ARG A 40 PRO A 41 18 -5.91
CISPEP 36 GLY A 92 PRO A 93 18 -2.95
CISPEP 37 ARG A 40 PRO A 41 19 -9.99
CISPEP 38 GLY A 92 PRO A 93 19 -3.59
CISPEP 39 ARG A 40 PRO A 41 20 -7.39
CISPEP 40 GLY A 92 PRO A 93 20 -1.66
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 10 2 Bytes