Header list of 1e09.pdb file
Complete list - r 25 2 Bytes
HEADER ALLERGEN 15-MAR-00 1E09 TITLE SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRU AV 1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PRUNUS AVIUM; SOURCE 3 ORGANISM_COMMON: SWEET CHERRY; SOURCE 4 ORGANISM_TAXID: 42229; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET16B KEYWDS ALLERGEN, MAJOR CHERRY ALLERGEN, PATHOGENESIS-RELATED KEYWDS 2 PROTEIN, HETERONUCLEAR NMR, STRUCTURE EXPDTA SOLUTION NMR NUMMDL 22 AUTHOR P.NEUDECKER,J.NERKAMP,K.SCHWEIMER,H.STICHT,M.BOEHM, AUTHOR 2 S.SCHEURER,S.VIETHS,P.ROESCH REVDAT 5 24-FEB-09 1E09 1 VERSN REVDAT 4 03-MAY-05 1E09 1 ATOM REVDAT 3 08-NOV-02 1E09 1 SHEET REVDAT 2 19-AUG-02 1E09 1 JRNL REMARK REVDAT 1 15-MAR-01 1E09 0 JRNL AUTH P.NEUDECKER,K.SCHWEIMER,J.NERKAMP,S.SCHEURER, JRNL AUTH 2 S.VIETHS,H.STICHT,P.ROESCH JRNL TITL ALLERGIC CROSS-REACTIVITY MADE VISIBLE: THE JRNL TITL 2 SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN JRNL TITL 3 PRU AV 1 JRNL REF J.BIOL.CHEM. V. 276 22756 2001 JRNL REFN ISSN 0021-9258 JRNL PMID 11287426 JRNL DOI 10.1074/JBC.M101657200 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.SCHWEIMER,H.STICHT,J.NERKAMP,M.BOEHM, REMARK 1 AUTH 2 M.BREITENBACH,S.VIETHS,P.ROESCH REMARK 1 TITL NMR SPECTROSCOPY REVEALS COMMON STRUCTURAL REMARK 1 TITL 2 FEATURES OF THE BIRCH POLLEN ALLERGEN BET V 1 AND REMARK 1 TITL 3 THE CHERRY ALLERGEN PRU A 1 REMARK 1 REF APPL.MAGN.RESON. V. 17 449 1999 REMARK 1 REFN ISSN 0937-9347 REMARK 1 REMARK 1 REFERENCE 2 REMARK 1 AUTH P.NEUDECKER,K.SCHWEIMER,J.NERKAMP,M.BOEHM, REMARK 1 AUTH 2 S.SCHEURER,S.VIETHS,H.STICHT,P.ROESCH REMARK 1 TITL SEQUENCE-SPECIFIC 1H, 13C AND 15N RESONANCE REMARK 1 TITL 2 ASSIGNMENTS OF THE MAJOR CHERRY ALLERGEN PRU A 1 REMARK 1 REF J.BIOMOL.NMR V. 18 71 2000 REMARK 1 REFN ISSN 0925-2738 REMARK 1 PMID 11061231 REMARK 1 DOI 10.1023/A:1008357100592 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1E09 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-00. REMARK 100 THE PDBE ID CODE IS EBI-4742. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 10 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% H2O / 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-TOCSY, 2D-NOESY, REMARK 210 1H,15N-HSQC, HNHA, REMARK 210 3D-1H,15N-TOCSY-HSQC, REMARK 210 3D-1H,15N-NOESY-HSQC, REMARK 210 3D-1H,15N/ REMARK 210 1H,15N-HMQC-NOESY-HSQC, REMARK 210 1H,13C-CTHSQC, HNCO, REMARK 210 HNCA, HNCACB, CBCA(CO)NH, REMARK 210 H(C)CH-COSY, (H)CCH-COSY, REMARK 210 HC(C)H-TOCSY, REMARK 210 3D-1H,13C-NOESY-HSQC, REMARK 210 3D-1H,13C/ REMARK 210 1H,15N-HMQC-NOESY-HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NDEE, NMRVIEW 4.1.0, REMARK 210 X-PLOR 3.851 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE REMARK 210 NMR SPECTROSCOPY ON 13C/15N-LABELED PRU AV 1 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 H LEU A 44 - O ILE A 53 1.57 REMARK 500 O ILE A 56 - H VAL A 67 1.58 REMARK 500 H PHE A 58 - O GLY A 65 1.50 REMARK 500 O LYS A 70 - H THR A 84 1.55 REMARK 500 H LYS A 70 - O THR A 84 1.57 REMARK 500 H TYR A 81 - O THR A 102 1.57 REMARK 500 H GLU A 101 - O THR A 117 1.58 REMARK 500 H LYS A 103 - O LYS A 115 1.57 REMARK 500 O LYS A 129 - H HIS A 132 1.58 REMARK 500 O TYR A 150 - H HIS A 154 1.58 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 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 VAL A 23 -65.86 -102.13 REMARK 500 1 ASP A 25 24.41 -146.47 REMARK 500 1 SER A 73 157.05 170.39 REMARK 500 1 GLU A 96 -79.81 -132.71 REMARK 500 1 ASN A 125 63.13 66.32 REMARK 500 1 TYR A 158 33.11 34.34 REMARK 500 2 VAL A 23 -61.71 -96.85 REMARK 500 2 ASP A 25 15.22 -147.69 REMARK 500 2 LYS A 32 -30.27 -130.94 REMARK 500 2 ALA A 34 102.65 -173.11 REMARK 500 2 HIS A 40 139.86 178.73 REMARK 500 2 GLU A 96 -80.71 -144.84 REMARK 500 2 ASN A 125 60.41 68.68 REMARK 500 2 ILE A 128 173.52 -55.77 REMARK 500 2 TYR A 158 32.53 34.65 REMARK 500 3 VAL A 23 -65.25 -93.49 REMARK 500 3 ASP A 25 25.24 -149.04 REMARK 500 3 SER A 62 -173.38 -57.52 REMARK 500 3 SER A 73 161.62 172.19 REMARK 500 3 GLU A 96 -83.44 -124.98 REMARK 500 3 LYS A 134 -65.37 -104.31 REMARK 500 3 TYR A 158 31.93 34.79 REMARK 500 4 VAL A 23 -61.94 -98.18 REMARK 500 4 ASP A 25 46.92 -154.55 REMARK 500 4 ALA A 34 99.06 -160.38 REMARK 500 4 HIS A 40 132.69 -175.42 REMARK 500 4 GLU A 96 -79.57 -143.23 REMARK 500 4 ASN A 125 65.76 60.83 REMARK 500 4 TYR A 158 33.55 34.68 REMARK 500 5 VAL A 23 -65.03 -108.68 REMARK 500 5 ASP A 25 23.09 -148.47 REMARK 500 5 ALA A 34 98.52 -160.46 REMARK 500 5 HIS A 40 164.16 177.01 REMARK 500 5 SER A 62 -165.27 -62.08 REMARK 500 5 SER A 73 158.57 178.39 REMARK 500 5 GLU A 96 -79.78 -143.56 REMARK 500 5 TYR A 158 36.80 34.03 REMARK 500 6 VAL A 23 -65.39 -98.17 REMARK 500 6 ASP A 25 36.64 -148.19 REMARK 500 6 SER A 73 156.75 177.40 REMARK 500 6 GLU A 96 -81.12 -142.64 REMARK 500 6 TYR A 158 33.19 34.66 REMARK 500 7 VAL A 23 -65.74 -95.28 REMARK 500 7 ASP A 25 33.19 -148.28 REMARK 500 7 ALA A 34 97.74 -163.17 REMARK 500 7 HIS A 40 157.52 178.80 REMARK 500 7 GLU A 96 -80.91 -127.40 REMARK 500 7 ILE A 128 173.40 -57.91 REMARK 500 7 TYR A 158 31.22 35.46 REMARK 500 8 ASP A 25 30.03 -152.64 REMARK 500 8 ALA A 34 101.38 -160.84 REMARK 500 8 HIS A 40 158.68 179.44 REMARK 500 8 SER A 73 160.20 175.50 REMARK 500 8 GLU A 96 -78.79 -131.33 REMARK 500 8 TYR A 158 33.41 34.52 REMARK 500 9 VAL A 23 -65.30 -106.86 REMARK 500 9 ALA A 34 98.24 -170.59 REMARK 500 9 HIS A 40 156.54 179.02 REMARK 500 9 SER A 73 160.84 172.78 REMARK 500 9 GLU A 96 -79.78 -131.45 REMARK 500 9 TYR A 158 32.54 34.59 REMARK 500 10 VAL A 23 -66.29 -105.22 REMARK 500 10 ASP A 25 31.26 -147.96 REMARK 500 10 HIS A 40 139.78 178.80 REMARK 500 10 GLU A 96 -81.69 -140.94 REMARK 500 10 PRO A 108 73.93 -66.64 REMARK 500 10 ASN A 125 81.34 -151.41 REMARK 500 10 TYR A 158 32.73 34.24 REMARK 500 11 ASP A 25 38.80 -154.68 REMARK 500 11 LYS A 32 -30.29 -137.39 REMARK 500 11 HIS A 40 139.98 179.08 REMARK 500 11 SER A 73 157.72 178.16 REMARK 500 11 GLU A 96 -80.56 -131.54 REMARK 500 11 TYR A 158 31.96 34.99 REMARK 500 12 VAL A 23 -65.17 -104.68 REMARK 500 12 ASP A 25 33.39 -145.68 REMARK 500 12 GLU A 96 -80.84 -140.31 REMARK 500 12 TYR A 158 32.17 34.90 REMARK 500 13 VAL A 23 -67.85 -104.62 REMARK 500 13 ASP A 25 19.85 -144.15 REMARK 500 13 ALA A 37 -62.59 -101.96 REMARK 500 13 HIS A 40 141.42 -174.55 REMARK 500 13 SER A 73 161.74 171.95 REMARK 500 13 GLU A 96 -79.54 -142.03 REMARK 500 13 ASN A 125 65.96 64.91 REMARK 500 13 ALA A 157 99.62 -69.36 REMARK 500 13 TYR A 158 31.89 34.90 REMARK 500 14 VAL A 23 -66.30 -97.37 REMARK 500 14 ASP A 25 25.88 -143.79 REMARK 500 14 GLU A 96 -83.33 -137.24 REMARK 500 14 TYR A 158 32.45 34.65 REMARK 500 15 ASP A 25 15.17 -147.30 REMARK 500 15 HIS A 40 141.32 -178.77 REMARK 500 15 GLU A 96 -79.79 -140.79 REMARK 500 15 TYR A 158 32.09 34.86 REMARK 500 16 ALA A 34 103.79 -169.75 REMARK 500 16 ALA A 37 -71.97 -92.06 REMARK 500 16 GLU A 96 -80.83 -137.37 REMARK 500 16 TYR A 158 32.72 34.40 REMARK 500 17 VAL A 23 -65.82 -106.27 REMARK 500 17 ASP A 25 28.52 -144.76 REMARK 500 17 HIS A 40 153.82 177.61 REMARK 500 17 SER A 73 156.57 176.18 REMARK 500 17 GLU A 96 -77.84 -133.18 REMARK 500 17 TYR A 158 33.60 34.09 REMARK 500 18 ASP A 25 28.58 -145.36 REMARK 500 18 ALA A 34 100.13 -164.95 REMARK 500 18 SER A 73 156.58 179.07 REMARK 500 18 ASP A 93 16.10 56.29 REMARK 500 18 GLU A 96 -81.61 -127.98 REMARK 500 18 TYR A 158 32.79 34.85 REMARK 500 19 VAL A 23 -61.14 -91.20 REMARK 500 19 ASP A 25 25.97 -151.11 REMARK 500 19 GLU A 96 -78.63 -135.37 REMARK 500 19 ALA A 157 99.21 -67.22 REMARK 500 19 TYR A 158 23.45 37.55 REMARK 500 20 ALA A 21 -70.87 -56.77 REMARK 500 20 VAL A 23 -60.42 -90.27 REMARK 500 20 ASP A 25 27.77 -153.52 REMARK 500 20 LYS A 32 -30.90 -135.77 REMARK 500 20 ALA A 34 87.58 -157.64 REMARK 500 20 HIS A 40 164.77 178.71 REMARK 500 20 GLU A 96 -79.40 -137.00 REMARK 500 20 TYR A 158 21.80 38.52 REMARK 500 21 VAL A 23 -62.19 -92.82 REMARK 500 21 LEU A 24 0.23 -69.09 REMARK 500 21 ASP A 25 24.33 -150.18 REMARK 500 21 ALA A 34 95.43 -171.92 REMARK 500 21 GLU A 96 -78.84 -134.65 REMARK 500 21 ASN A 125 54.67 -104.53 REMARK 500 21 TYR A 158 32.44 34.57 REMARK 500 22 VAL A 23 -64.97 -96.14 REMARK 500 22 LEU A 29 -62.16 -106.11 REMARK 500 22 SER A 62 -162.40 48.70 REMARK 500 22 SER A 73 157.43 168.28 REMARK 500 22 GLU A 96 -78.20 -138.53 REMARK 500 22 TYR A 158 21.46 38.99 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 2 ARG A 17 0.20 SIDE CHAIN REMARK 500 4 ARG A 17 0.23 SIDE CHAIN REMARK 500 6 ARG A 17 0.23 SIDE CHAIN REMARK 500 8 ARG A 17 0.20 SIDE CHAIN REMARK 500 9 ARG A 17 0.24 SIDE CHAIN REMARK 500 10 ARG A 17 0.26 SIDE CHAIN REMARK 500 11 ARG A 17 0.31 SIDE CHAIN REMARK 500 12 ARG A 17 0.19 SIDE CHAIN REMARK 500 13 ARG A 17 0.21 SIDE CHAIN REMARK 500 14 ARG A 17 0.27 SIDE CHAIN REMARK 500 15 ARG A 17 0.08 SIDE CHAIN REMARK 500 16 ARG A 17 0.28 SIDE CHAIN REMARK 500 17 ARG A 17 0.21 SIDE CHAIN REMARK 500 18 ARG A 17 0.20 SIDE CHAIN REMARK 500 19 ARG A 17 0.26 SIDE CHAIN REMARK 500 20 ARG A 17 0.16 SIDE CHAIN REMARK 500 21 ARG A 17 0.12 SIDE CHAIN REMARK 500 22 ARG A 17 0.26 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED. REMARK 900 REMARK 900 RELATED ID: 1BTV RELATED DB: PDB REMARK 900 STRUCTURE OF BET V 1, NMR, 20 STRUCTURES REMARK 900 RELATED ID: 1B6F RELATED DB: PDB REMARK 900 BIRCH POLLEN ALLERGEN BET V 1 REMARK 900 RELATED ID: 1BV1 RELATED DB: PDB REMARK 900 BIRCH POLLEN ALLERGEN BET V 1 DBREF 1E09 A 1 159 UNP O24248 O24248 2 160 SEQRES 1 A 159 GLY VAL PHE THR TYR GLU SER GLU PHE THR SER GLU ILE SEQRES 2 A 159 PRO PRO PRO ARG LEU PHE LYS ALA PHE VAL LEU ASP ALA SEQRES 3 A 159 ASP ASN LEU VAL PRO LYS ILE ALA PRO GLN ALA ILE LYS SEQRES 4 A 159 HIS SER GLU ILE LEU GLU GLY ASP GLY GLY PRO GLY THR SEQRES 5 A 159 ILE LYS LYS ILE THR PHE GLY GLU GLY SER GLN TYR GLY SEQRES 6 A 159 TYR VAL LYS HIS LYS ILE ASP SER ILE ASP LYS GLU ASN SEQRES 7 A 159 TYR SER TYR SER TYR THR LEU ILE GLU GLY ASP ALA LEU SEQRES 8 A 159 GLY ASP THR LEU GLU LYS ILE SER TYR GLU THR LYS LEU SEQRES 9 A 159 VAL ALA SER PRO SER GLY GLY SER ILE ILE LYS SER THR SEQRES 10 A 159 SER HIS TYR HIS THR LYS GLY ASN VAL GLU ILE LYS GLU SEQRES 11 A 159 GLU HIS VAL LYS ALA GLY LYS GLU LYS ALA SER ASN LEU SEQRES 12 A 159 PHE LYS LEU ILE GLU THR TYR LEU LYS GLY HIS PRO ASP SEQRES 13 A 159 ALA TYR ASN HELIX 1 1 PRO A 15 PHE A 22 1 8 HELIX 2 2 ALA A 26 ILE A 33 1 8 HELIX 4 4 GLU A 130 GLY A 153 1 24 SHEET 1 A 5 VAL A 2 SER A 11 0 SHEET 2 A 5 SER A 112 THR A 122 -1 N SER A 118 O TYR A 5 SHEET 3 A 5 LYS A 97 LEU A 104 -1 N GLU A 101 O THR A 117 SHEET 4 A 5 SER A 80 LEU A 85 -1 N TYR A 83 O TYR A 100 SHEET 5 A 5 SER A 73 ASP A 75 -1 N ASP A 75 O SER A 80 SHEET 1 B 3 SER A 41 ILE A 43 0 SHEET 2 B 3 ILE A 53 PHE A 58 -1 N LYS A 55 O GLU A 42 SHEET 3 B 3 GLY A 65 ILE A 71 -1 N VAL A 67 O ILE 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
Complete list - r 25 2 Bytes