Header list of 1b6f.pdb file
Complete list - v 3 2 Bytes
HEADER PLANT PROTEIN 13-JAN-99 1B6F TITLE BIRCH POLLEN ALLERGEN BET V 1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (MAJOR POLLEN ALLERGEN BET V 1-A); COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BETULA PENDULA; SOURCE 3 ORGANISM_COMMON: EUROPEAN WHITE BIRCH; SOURCE 4 ORGANISM_TAXID: 3505; SOURCE 5 CELL: POLLEN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21/DE3; SOURCE 9 OTHER_DETAILS: SYNTHETIC GENE KEYWDS MAJOR BIRCH POLLEN ALLERGEN, PATHOGENESIS-RELATED PROTEIN, PLANT KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 23 AUTHOR K.SCHWEIMER,H.STICHT,M.BOEHM,P.ROESCH REVDAT 3 03-NOV-21 1B6F 1 REMARK SEQADV REVDAT 2 24-FEB-09 1B6F 1 VERSN REVDAT 1 17-JAN-00 1B6F 0 JRNL AUTH K.SCHWEIMER,H.STICHT,M.BOEHM,P.ROESCH JRNL TITL NMR SPECTROSCOPY REVEALS COMMON STRUCTURAL FEATURES OF THE JRNL TITL 2 BIRCH POLLEN ALLERGEN BET V 1 AND THE CHERRY ALLERGEN PRU A JRNL TITL 3 1 JRNL REF APPL.MAGN.RESON. V. 17 449 1999 JRNL REFN ISSN 0937-9347 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.BOEHM,P.ROESCH REMARK 1 TITL EXPRESSION IN ESCHERICHIA COLI, PURIFICATION, AND REMARK 1 TITL 2 SPECTROSCOPIC CHARACTERIZATION OF TWO MUTANT BET V 1 REMARK 1 TITL 3 PROTEINS REMARK 1 REF BIOL.CHEM. V. 378 687 1997 REMARK 1 REFN ISSN 1431-6730 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.FABER,A.LINDEMANN,H.STICHT,A.EJCHART,A.KUNGL,M.SUSANI, REMARK 1 AUTH 2 R.W.FRANK,D.KRAFT,M.BREITENBACH,P.ROESCH REMARK 1 TITL SECONDARY STRUCTURE AND TERTIARY FOLD OF THE BIRCH POLLEN REMARK 1 TITL 2 ALLERGEN BET V 1 IN SOLUTION REMARK 1 REF J.BIOL.CHEM. V. 271 19243 1996 REMARK 1 REFN ISSN 0021-9258 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: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION ABOVE REMARK 4 REMARK 4 1B6F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-99. REMARK 100 THE DEPOSITION ID IS D_1000007232. 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 : 10 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCO; 3D HNCA; 3D CBCA(CO)NH; REMARK 210 3D HNCACB; 3D HCCH-COSY; 3D HCCH- REMARK 210 TOCSY; 3D-13C-NOESYHSQC; 3D-15N- REMARK 210 NOESYHSQC; 3D-15N-TOCSYHSQC; 3D REMARK 210 HNHA; 2D-NOESY(D2O); 2D- REMARK 210 TOCSY(D2O) REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NDEE, X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 60 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND LEAST REMARK 210 RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: REMARK 210 THE STRUCTURE WAS DETERMINED USING MULTIDIMENSIONAL HETERONUCLEAR REMARK 210 NMR REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED BET V 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 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: 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 ALA A 130 H LYS A 134 1.46 REMARK 500 H ASP A 72 O ASN A 82 1.57 REMARK 500 H PHE A 3 O TYR A 120 1.58 REMARK 500 O LEU A 151 HD1 HIS A 154 1.58 REMARK 500 HD22 ASN A 43 O GLY A 46 1.59 REMARK 500 H ILE A 44 O ILE A 53 1.60 REMARK 500 H THR A 7 O ILE A 116 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 ALA A 34 75.87 -159.77 REMARK 500 1 ALA A 37 -69.16 -107.28 REMARK 500 1 PHE A 62 175.33 -59.06 REMARK 500 1 LYS A 65 -44.64 -142.09 REMARK 500 1 TYR A 66 -170.05 -65.42 REMARK 500 1 LYS A 68 -61.76 -90.14 REMARK 500 1 ASP A 69 124.36 59.20 REMARK 500 1 ASP A 72 -71.40 -99.95 REMARK 500 1 ILE A 86 -68.47 -126.96 REMARK 500 1 ASP A 93 -84.14 -120.80 REMARK 500 1 THR A 94 14.12 -150.83 REMARK 500 1 GLU A 131 -70.36 -39.83 REMARK 500 1 TYR A 150 -70.52 -52.35 REMARK 500 1 SER A 155 83.58 -150.17 REMARK 500 2 TYR A 5 56.63 -152.29 REMARK 500 2 ILE A 23 -58.08 -120.15 REMARK 500 2 PRO A 31 46.11 -76.70 REMARK 500 2 LYS A 32 -54.87 -154.32 REMARK 500 2 ALA A 37 -72.65 -100.51 REMARK 500 2 GLU A 60 -178.70 50.09 REMARK 500 2 LYS A 65 -79.45 -55.18 REMARK 500 2 ASP A 72 -73.23 -100.44 REMARK 500 2 ILE A 86 -66.80 -120.98 REMARK 500 2 THR A 94 24.91 49.23 REMARK 500 2 TYR A 150 -70.87 -45.54 REMARK 500 3 TYR A 5 61.31 -158.29 REMARK 500 3 ALA A 34 75.39 -159.03 REMARK 500 3 ALA A 37 -72.26 -102.50 REMARK 500 3 LYS A 65 -81.80 -122.34 REMARK 500 3 LYS A 68 -64.75 -99.30 REMARK 500 3 ASP A 69 129.33 59.08 REMARK 500 3 ASP A 72 -75.25 -104.69 REMARK 500 3 ILE A 86 -74.33 -123.43 REMARK 500 3 ASP A 93 -49.09 -146.23 REMARK 500 3 THR A 94 12.45 -145.08 REMARK 500 3 ASP A 125 -81.39 -68.50 REMARK 500 3 HIS A 126 -178.08 -64.33 REMARK 500 3 TYR A 150 -71.50 -47.71 REMARK 500 3 TYR A 158 -63.28 -96.90 REMARK 500 4 LYS A 32 -67.20 -93.42 REMARK 500 4 ALA A 34 56.33 -146.80 REMARK 500 4 PRO A 59 -169.90 -70.55 REMARK 500 4 LYS A 65 -38.71 -144.07 REMARK 500 4 LYS A 68 -65.02 -93.46 REMARK 500 4 ASP A 69 120.76 60.60 REMARK 500 4 ASP A 72 -72.34 -101.20 REMARK 500 4 ILE A 86 -76.33 -122.61 REMARK 500 4 ASP A 93 -82.63 -114.30 REMARK 500 4 ALA A 157 178.18 68.38 REMARK 500 4 TYR A 158 -49.57 -173.73 REMARK 500 REMARK 500 THIS ENTRY HAS 333 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 ARG A 17 0.12 SIDE CHAIN REMARK 500 1 ARG A 70 0.20 SIDE CHAIN REMARK 500 1 ARG A 145 0.30 SIDE CHAIN REMARK 500 2 ARG A 17 0.32 SIDE CHAIN REMARK 500 2 ARG A 70 0.24 SIDE CHAIN REMARK 500 2 ARG A 145 0.32 SIDE CHAIN REMARK 500 3 ARG A 17 0.11 SIDE CHAIN REMARK 500 3 ARG A 70 0.26 SIDE CHAIN REMARK 500 3 ARG A 145 0.32 SIDE CHAIN REMARK 500 4 ARG A 17 0.28 SIDE CHAIN REMARK 500 4 ARG A 70 0.32 SIDE CHAIN REMARK 500 4 ARG A 145 0.29 SIDE CHAIN REMARK 500 5 ARG A 17 0.11 SIDE CHAIN REMARK 500 5 ARG A 70 0.12 SIDE CHAIN REMARK 500 5 ARG A 145 0.28 SIDE CHAIN REMARK 500 6 ARG A 17 0.27 SIDE CHAIN REMARK 500 6 ARG A 70 0.24 SIDE CHAIN REMARK 500 6 ARG A 145 0.26 SIDE CHAIN REMARK 500 7 ARG A 17 0.32 SIDE CHAIN REMARK 500 7 ARG A 70 0.29 SIDE CHAIN REMARK 500 7 ARG A 145 0.15 SIDE CHAIN REMARK 500 8 ARG A 17 0.29 SIDE CHAIN REMARK 500 8 ARG A 70 0.27 SIDE CHAIN REMARK 500 8 ARG A 145 0.28 SIDE CHAIN REMARK 500 9 ARG A 17 0.23 SIDE CHAIN REMARK 500 9 ARG A 70 0.20 SIDE CHAIN REMARK 500 9 ARG A 145 0.31 SIDE CHAIN REMARK 500 10 ARG A 17 0.12 SIDE CHAIN REMARK 500 10 ARG A 70 0.32 SIDE CHAIN REMARK 500 10 ARG A 145 0.29 SIDE CHAIN REMARK 500 11 ARG A 17 0.32 SIDE CHAIN REMARK 500 11 ARG A 145 0.17 SIDE CHAIN REMARK 500 12 ARG A 17 0.31 SIDE CHAIN REMARK 500 12 ARG A 70 0.32 SIDE CHAIN REMARK 500 12 ARG A 145 0.17 SIDE CHAIN REMARK 500 13 ARG A 17 0.22 SIDE CHAIN REMARK 500 13 ARG A 70 0.23 SIDE CHAIN REMARK 500 13 ARG A 145 0.31 SIDE CHAIN REMARK 500 14 ARG A 17 0.25 SIDE CHAIN REMARK 500 14 ARG A 70 0.25 SIDE CHAIN REMARK 500 14 ARG A 145 0.29 SIDE CHAIN REMARK 500 15 ARG A 17 0.22 SIDE CHAIN REMARK 500 15 ARG A 70 0.31 SIDE CHAIN REMARK 500 15 ARG A 145 0.25 SIDE CHAIN REMARK 500 16 ARG A 17 0.31 SIDE CHAIN REMARK 500 16 ARG A 70 0.17 SIDE CHAIN REMARK 500 16 ARG A 145 0.18 SIDE CHAIN REMARK 500 17 ARG A 17 0.18 SIDE CHAIN REMARK 500 17 ARG A 70 0.32 SIDE CHAIN REMARK 500 17 ARG A 145 0.18 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 68 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1B6F A 1 159 UNP P15494 BEV1A_BETVE 1 159 SEQADV 1B6F LEU A 139 UNP P15494 MET 139 ENGINEERED MUTATION SEQRES 1 A 159 GLY VAL PHE ASN TYR GLU THR GLU THR THR SER VAL ILE SEQRES 2 A 159 PRO ALA ALA ARG LEU PHE LYS ALA PHE ILE LEU ASP GLY SEQRES 3 A 159 ASP ASN LEU PHE PRO LYS VAL ALA PRO GLN ALA ILE SER SEQRES 4 A 159 SER VAL GLU ASN ILE GLU GLY ASN GLY GLY PRO GLY THR SEQRES 5 A 159 ILE LYS LYS ILE SER PHE PRO GLU GLY PHE PRO PHE LYS SEQRES 6 A 159 TYR VAL LYS ASP ARG VAL ASP GLU VAL ASP HIS THR ASN SEQRES 7 A 159 PHE LYS TYR ASN TYR SER VAL ILE GLU GLY GLY PRO ILE SEQRES 8 A 159 GLY ASP THR LEU GLU LYS ILE SER ASN GLU ILE LYS ILE SEQRES 9 A 159 VAL ALA THR PRO ASP GLY GLY SER ILE LEU LYS ILE SER SEQRES 10 A 159 ASN LYS TYR HIS THR LYS GLY ASP HIS GLU VAL LYS ALA SEQRES 11 A 159 GLU GLN VAL LYS ALA SER LYS GLU LEU GLY GLU THR LEU SEQRES 12 A 159 LEU ARG ALA VAL GLU SER TYR LEU LEU ALA HIS SER ASP SEQRES 13 A 159 ALA TYR ASN HELIX 1 1 ALA A 15 PHE A 22 1 8 HELIX 2 2 GLY A 26 VAL A 33 1 8 HELIX 3 3 ALA A 130 ALA A 153 1 24 SHEET 1 A 3 THR A 7 SER A 11 0 SHEET 2 A 3 GLY A 111 HIS A 121 -1 N ILE A 116 O THR A 7 SHEET 3 A 3 LYS A 97 THR A 107 -1 N THR A 107 O GLY A 111 SHEET 1 B 2 VAL A 41 GLU A 45 0 SHEET 2 B 2 ILE A 53 ILE A 56 -1 N LYS A 55 O GLU A 42 SHEET 1 C 2 ARG A 70 ASP A 75 0 SHEET 2 C 2 LYS A 80 SER A 84 -1 N SER A 84 O ARG A 70 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 3 2 Bytes