Header list of 2a0a.pdb file
Complete list - v 6 2 Bytes
HEADER ALLERGEN 16-JUN-05 2A0A
TITLE SOLUTION STRUCTURE OF DER F 13, GROUP 13 ALLERGEN FROM HOUSE DUST
TITLE 2 MITES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DER F 13;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DERMATOPHAGOIDES FARINAE;
SOURCE 3 ORGANISM_COMMON: AMERICAN HOUSE DUST MITE;
SOURCE 4 ORGANISM_TAXID: 6954;
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: PET-M
KEYWDS BETA BARREL, HELIX, ALLERGEN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.L.CHAN,Y.K.MOK
REVDAT 3 06-NOV-19 2A0A 1 JRNL REMARK
REVDAT 2 24-FEB-09 2A0A 1 VERSN
REVDAT 1 11-APR-06 2A0A 0
JRNL AUTH S.L.CHAN,S.T.ONG,S.Y.ONG,F.T.CHEW,Y.K.MOK
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE-BASED EPITOPE MAPPING
JRNL TITL 2 AND MODULATION OF DUST MITE GROUP 13 ALLERGEN AS A
JRNL TITL 3 HYPOALLERGEN.
JRNL REF J IMMUNOL. V. 176 4852 2006
JRNL REFN ISSN 0022-1767
JRNL PMID 16585580
JRNL DOI 10.4049/JIMMUNOL.176.8.4852
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 7.0
REMARK 3 AUTHORS : D. A. PEARLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2A0A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033331.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DER F 13, U-15N, 13C; 50MM
REMARK 210 ACETATE BUFFER PH 4.5; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 1.0.5
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
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: 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 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 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 11 47.44 -145.92
REMARK 500 1 LYS A 12 -57.48 -154.08
REMARK 500 1 LYS A 15 13.16 56.58
REMARK 500 1 THR A 35 -152.21 -147.08
REMARK 500 1 ASN A 46 40.49 -74.52
REMARK 500 1 ASP A 47 -48.35 -153.09
REMARK 500 1 SER A 55 -142.27 -95.56
REMARK 500 1 PHE A 57 24.76 49.26
REMARK 500 1 LYS A 58 108.37 -164.34
REMARK 500 1 ALA A 75 -152.13 51.41
REMARK 500 1 ASP A 89 25.19 -170.48
REMARK 500 1 ASN A 90 -39.61 -156.19
REMARK 500 1 LYS A 100 -45.29 -155.79
REMARK 500 1 GLU A 101 84.27 167.98
REMARK 500 1 PHE A 108 84.15 -67.91
REMARK 500 1 CYS A 119 -157.36 -115.80
REMARK 500 2 SER A 3 38.17 -169.36
REMARK 500 2 LYS A 12 -41.94 66.06
REMARK 500 2 SER A 13 77.04 38.20
REMARK 500 2 LYS A 15 7.86 56.21
REMARK 500 2 THR A 35 -155.43 -125.92
REMARK 500 2 GLU A 45 79.14 -101.26
REMARK 500 2 ASN A 46 -62.60 61.24
REMARK 500 2 PHE A 51 75.91 -100.43
REMARK 500 2 LEU A 54 30.51 -91.54
REMARK 500 2 SER A 55 -136.99 -116.42
REMARK 500 2 PHE A 57 -39.84 62.00
REMARK 500 2 LYS A 65 -120.42 -120.98
REMARK 500 2 ARG A 74 -80.65 -150.26
REMARK 500 2 ASP A 76 18.99 44.89
REMARK 500 2 ASN A 90 -45.78 -149.98
REMARK 500 2 PHE A 97 28.29 -79.64
REMARK 500 2 ASP A 99 -33.51 -133.48
REMARK 500 2 LYS A 100 -50.34 -139.79
REMARK 500 2 GLU A 101 79.55 171.28
REMARK 500 2 SER A 118 109.64 -160.67
REMARK 500 2 CYS A 119 -163.70 -105.45
REMARK 500 2 ASP A 120 -49.38 -25.06
REMARK 500 3 LYS A 12 -43.29 66.36
REMARK 500 3 SER A 13 74.72 39.51
REMARK 500 3 LYS A 15 9.65 57.14
REMARK 500 3 THR A 35 -159.30 -132.64
REMARK 500 3 GLU A 45 34.22 -81.21
REMARK 500 3 ASN A 46 17.70 54.16
REMARK 500 3 ASP A 47 -56.03 -173.28
REMARK 500 3 PHE A 51 72.20 -101.88
REMARK 500 3 SER A 55 -130.73 -104.09
REMARK 500 3 PHE A 57 -34.39 60.95
REMARK 500 3 ALA A 75 -129.95 48.96
REMARK 500 3 ASP A 76 31.42 -69.51
REMARK 500
REMARK 500 THIS ENTRY HAS 188 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 7 ARG A 106 0.08 SIDE CHAIN
REMARK 500 10 TYR A 8 0.08 SIDE CHAIN
REMARK 500 10 TYR A 128 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2A0A A 1 131 UNP Q1M2P5 Q1M2P5_DERFA 1 131
SEQRES 1 A 131 MET ALA SER ILE GLU GLY LYS TYR LYS LEU GLU LYS SER
SEQRES 2 A 131 GLU LYS PHE ASP GLU PHE LEU ASP LYS LEU GLY VAL GLY
SEQRES 3 A 131 PHE MET VAL LYS THR ALA ALA LYS THR LEU LYS PRO THR
SEQRES 4 A 131 PHE GLU VAL ALA ILE GLU ASN ASP GLN TYR ILE PHE ARG
SEQRES 5 A 131 SER LEU SER THR PHE LYS ASN THR GLU ALA LYS PHE LYS
SEQRES 6 A 131 LEU GLY GLU GLU PHE GLU GLU ASP ARG ALA ASP GLY LYS
SEQRES 7 A 131 ARG VAL LYS THR VAL ILE GLN LYS GLU GLY ASP ASN LYS
SEQRES 8 A 131 PHE VAL GLN THR GLN PHE GLY ASP LYS GLU VAL LYS ILE
SEQRES 9 A 131 ILE ARG GLU PHE ASN GLY ASP GLU VAL VAL VAL THR ALA
SEQRES 10 A 131 SER CYS ASP GLY VAL THR SER VAL ARG THR TYR LYS ARG
SEQRES 11 A 131 ILE
HELIX 1 1 LYS A 15 GLY A 24 1 10
HELIX 2 2 GLY A 26 THR A 31 1 6
HELIX 3 3 ALA A 32 THR A 35 5 4
SHEET 1 A10 THR A 60 PHE A 64 0
SHEET 2 A10 TYR A 49 SER A 53 -1 N SER A 53 O THR A 60
SHEET 3 A10 THR A 39 ILE A 44 -1 N GLU A 41 O ARG A 52
SHEET 4 A10 GLY A 6 LEU A 10 -1 N TYR A 8 O PHE A 40
SHEET 5 A10 THR A 123 ILE A 131 -1 O ILE A 131 N LYS A 7
SHEET 6 A10 GLU A 112 SER A 118 -1 N VAL A 113 O TYR A 128
SHEET 7 A10 VAL A 102 PHE A 108 -1 N LYS A 103 O SER A 118
SHEET 8 A10 LYS A 91 GLN A 96 -1 N GLN A 94 O ILE A 104
SHEET 9 A10 LYS A 78 GLU A 87 -1 N GLN A 85 O VAL A 93
SHEET 10 A10 PHE A 70 ARG A 74 -1 N ARG A 74 O LYS A 78
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 6 2 Bytes