HEADER UNKNOWN FUNCTION 20-FEB-12 2LPX
TITLE SOLUTION STRUCTURE OF STRAWBERRY ALLERGEN FRA A 1E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR STRAWBERRY ALLERGEN FRA A 1-E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FRAGARIA X ANANASSA;
SOURCE 3 ORGANISM_COMMON: STRAWBERRY;
SOURCE 4 ORGANISM_TAXID: 3747;
SOURCE 5 GENE: FRAA1E.2, FRAA1E.1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PQE70
KEYWDS BET V 1 HOMOLOGOUS PROTEIN, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.SEUTTER VON LOETZEN,O.HARTL-SPIEGELHAUER,K.SCHWEIMER,W.SCHWAB,
AUTHOR 2 P.ROESCH
REVDAT 3 14-JUN-23 2LPX 1 REMARK DBREF SEQADV
REVDAT 2 14-NOV-12 2LPX 1 JRNL
REVDAT 1 07-MAR-12 2LPX 0
JRNL AUTH C.SEUTTER VON LOETZEN,K.SCHWEIMER,W.SCHWAB,P.ROSCH,
JRNL AUTH 2 O.HARTL-SPIEGELHAUER
JRNL TITL SOLUTION STRUCTURE OF THE STRAWBERRY ALLERGEN FRA A 1.
JRNL REF BIOSCI.REP. V. 32 567 2012
JRNL REFN ISSN 0144-8463
JRNL PMID 22913709
JRNL DOI 10.1042/BSR20120058
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.6, X-PLOR NIH
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), SCHWIETERS, KUSZEWSKI,
REMARK 3 TJANDRA AND CLORE (X-PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000102685.
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 : 700 UM [U-99% 13C; U-99% 15N]
REMARK 210 PROTEIN, 150 MM SODIUM CHLORIDE,
REMARK 210 20 MM HEPES, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 2D 1H-13C HSQC
REMARK 210 AROMATIC; 3D HNCO; 3D HNCA; 3D
REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HBHA(CO)NH; 3D C(CO)NH; 3D HCCH-
REMARK 210 TOCSY; 3D CCH-TOCSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY ALIPHATIC;
REMARK 210 3D 1H-13C NOESY AROMATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW, X-PLOR NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 161
REMARK 465 SER A 162
REMARK 465 ARG A 163
REMARK 465 SER A 164
REMARK 465 HIS A 165
REMARK 465 HIS A 166
REMARK 465 HIS A 167
REMARK 465 HIS A 168
REMARK 465 HIS A 169
REMARK 465 HIS A 170
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 ASP A 26 H LEU A 30 1.56
REMARK 500 H LYS A 69 O GLU A 88 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 ILE A 14 139.34 67.40
REMARK 500 1 CYS A 41 139.08 178.62
REMARK 500 1 SER A 74 149.08 -170.02
REMARK 500 1 ILE A 87 -71.68 -89.84
REMARK 500 1 SER A 93 176.90 65.04
REMARK 500 1 HIS A 155 79.23 52.82
REMARK 500 2 ILE A 14 140.63 62.48
REMARK 500 2 CYS A 41 134.87 178.12
REMARK 500 2 ILE A 87 -70.14 -89.80
REMARK 500 2 SER A 93 -177.10 59.72
REMARK 500 3 ILE A 14 140.70 66.49
REMARK 500 3 VAL A 24 -68.97 -123.98
REMARK 500 3 CYS A 41 132.37 178.41
REMARK 500 3 ILE A 87 -75.87 -94.31
REMARK 500 3 SER A 93 173.35 62.86
REMARK 500 4 ILE A 14 141.77 61.74
REMARK 500 4 CYS A 41 130.90 177.71
REMARK 500 4 SER A 93 169.50 59.52
REMARK 500 4 GLU A 128 139.89 61.29
REMARK 500 5 ILE A 14 135.77 69.60
REMARK 500 5 CYS A 41 141.34 178.15
REMARK 500 5 ILE A 87 -74.59 -94.69
REMARK 500 5 SER A 93 -177.56 55.65
REMARK 500 6 ILE A 14 140.24 67.79
REMARK 500 6 ALA A 35 75.06 -157.86
REMARK 500 6 CYS A 41 129.71 -176.94
REMARK 500 6 ILE A 87 -76.86 -91.98
REMARK 500 6 SER A 93 157.20 58.03
REMARK 500 6 LYS A 98 93.22 -179.11
REMARK 500 6 HIS A 122 -167.11 -125.45
REMARK 500 7 ILE A 14 142.48 65.41
REMARK 500 7 CYS A 41 129.77 177.79
REMARK 500 7 SER A 63 25.43 46.32
REMARK 500 7 SER A 74 154.38 178.10
REMARK 500 7 ILE A 87 -75.46 -80.69
REMARK 500 7 SER A 93 177.18 60.13
REMARK 500 8 ILE A 14 142.11 70.20
REMARK 500 8 ALA A 35 72.20 -155.87
REMARK 500 8 CYS A 41 129.72 177.91
REMARK 500 8 SER A 93 -170.58 46.37
REMARK 500 8 GLU A 128 143.79 63.79
REMARK 500 8 HIS A 155 60.09 60.10
REMARK 500 9 ILE A 14 141.06 68.71
REMARK 500 9 CYS A 41 142.03 178.10
REMARK 500 9 SER A 74 141.42 -170.30
REMARK 500 9 SER A 93 178.19 61.47
REMARK 500 9 GLU A 128 128.85 61.60
REMARK 500 9 TYR A 159 -63.38 66.94
REMARK 500 10 ILE A 14 141.88 68.60
REMARK 500 10 CYS A 41 131.16 178.51
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18281 RELATED DB: BMRB
DBREF 2LPX A 1 160 UNP Q256S2 Q256S2_FRAAN 1 160
SEQADV 2LPX GLY A 161 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX SER A 162 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX ARG A 163 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX SER A 164 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 165 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 166 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 167 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 168 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 169 UNP Q256S2 EXPRESSION TAG
SEQADV 2LPX HIS A 170 UNP Q256S2 EXPRESSION TAG
SEQRES 1 A 170 MET GLY VAL TYR THR TYR GLU ASN GLU PHE THR SER ASP
SEQRES 2 A 170 ILE PRO ALA PRO LYS LEU PHE LYS ALA PHE VAL LEU ASP
SEQRES 3 A 170 ALA ASP ASN LEU ILE PRO LYS ILE ALA PRO GLN ALA VAL
SEQRES 4 A 170 LYS CYS ALA GLU ILE LEU GLU GLY ASP GLY GLY PRO GLY
SEQRES 5 A 170 THR ILE LYS LYS ILE THR PHE GLY GLU GLY SER HIS TYR
SEQRES 6 A 170 GLY TYR VAL LYS HIS LYS ILE HIS SER ILE ASP LYS VAL
SEQRES 7 A 170 ASN HIS THR TYR SER TYR SER LEU ILE GLU GLY ASP ALA
SEQRES 8 A 170 LEU SER GLU ASN ILE GLU LYS ILE ASP TYR GLU THR LYS
SEQRES 9 A 170 LEU VAL SER ALA PRO HIS GLY GLY THR ILE ILE LYS THR
SEQRES 10 A 170 THR SER LYS TYR HIS THR LYS GLY ASP VAL GLU ILE LYS
SEQRES 11 A 170 GLU GLU HIS VAL LYS ALA GLY LYS GLU LYS ALA ALA HIS
SEQRES 12 A 170 LEU PHE LYS LEU ILE GLU GLY TYR LEU LYS ASP HIS PRO
SEQRES 13 A 170 SER GLU TYR ASN GLY SER ARG SER HIS HIS HIS HIS HIS
SEQRES 14 A 170 HIS
HELIX 1 1 PRO A 15 LEU A 25 1 11
HELIX 2 2 ASP A 26 ALA A 35 1 10
HELIX 3 3 LYS A 130 HIS A 155 1 26
SHEET 1 A 7 TYR A 6 SER A 12 0
SHEET 2 A 7 THR A 113 THR A 123 -1 O ILE A 115 N PHE A 10
SHEET 3 A 7 ILE A 96 SER A 107 -1 N VAL A 106 O ILE A 114
SHEET 4 A 7 THR A 81 LEU A 86 -1 N TYR A 84 O TYR A 101
SHEET 5 A 7 TYR A 67 ASP A 76 -1 N LYS A 71 O SER A 85
SHEET 6 A 7 ILE A 54 THR A 58 -1 N LYS A 55 O HIS A 70
SHEET 7 A 7 CYS A 41 GLU A 46 -1 N GLU A 43 O LYS A 56
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
(ATOM LINES ARE NOT SHOWN.)
END
