Header list of 1bmw.pdb file
Complete list - b 16 2 Bytes
HEADER ALLERGEN 27-JUL-98 1BMW TITLE A FIBRONECTIN TYPE III FOLD IN PLANT ALLERGENS: THE SOLUTION STRUCTURE TITLE 2 OF PHL PII FROM TIMOTHY GRASS POLLEN, NMR, 38 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLLEN ALLERGEN PHL P2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PHL P II; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PHLEUM PRATENSE; SOURCE 3 ORGANISM_COMMON: TIMOTHY GRASS; SOURCE 4 ORGANISM_TAXID: 15957; SOURCE 5 CELL_LINE: BL21; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMW 172 KEYWDS ALLERGEN, ALLERGY, IMMUNOGLOBULINS, IMMUNOLOGY EXPDTA SOLUTION NMR NUMMDL 38 AUTHOR S.DE MARINO,M.A.C.MORELLI,F.FRATERNALI,E.TAMBORINO,S.VRTALA, AUTHOR 2 C.DOLECEK,P.AROSIO,R.VALENTA,A.PASTORE REVDAT 5 16-FEB-22 1BMW 1 REMARK REVDAT 4 24-FEB-09 1BMW 1 VERSN REVDAT 3 19-APR-05 1BMW 1 AUTHOR JRNL REVDAT 2 16-FEB-99 1BMW 1 SOURCE COMPND REMARK TITLE REVDAT 2 2 1 KEYWDS HEADER REVDAT 1 13-JAN-99 1BMW 0 JRNL AUTH S.DE MARINO,M.A.MORELLI,F.FRATERNALI,E.TAMBORINO,S.VRTALA, JRNL AUTH 2 C.DOLOCEK,P.AROSIO,R.VALENTA,A.PASTORE JRNL TITL AN IMMUNOGLOBULIN-LIKE FOLD IN A MAJOR PLANT ALLERGEN: THE JRNL TITL 2 SOLUTION STRUCTURE OF PHL P 2 FROM TIMOTHY GRASS POLLEN. JRNL REF STRUCTURE FOLD.DES. V. 7 943 1999 JRNL REFN ISSN 0969-2126 JRNL PMID 10467147 JRNL DOI 10.1016/S0969-2126(99)80121-X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ALSO USED ARIA, AUTHOR NILGES, REMARK 3 SIMULATED ANNEALING PROTOCOL WHICH PROGRESSIVELY INCLUDES, BY AN REMARK 3 ITERATIVE PROCEDURE, DISTANCE RESTRAINTS DIRECTLY ASSIGNED ON REMARK 3 THE BASIS OF CHEMICAL SHIFT AND NOE INTENSITY LISTS. REMARK 4 REMARK 4 1BMW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000171922. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE BUFFER REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AMX600 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : ARIA REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 38 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR NMR REMARK 210 SPECTROSCOPY 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 1-38 REMARK 465 RES C SSSEQI REMARK 465 GLU A 95 REMARK 465 GLU A 96 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 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 THR A 7 104.85 -165.75 REMARK 500 1 VAL A 8 91.84 -55.21 REMARK 500 1 ASN A 13 -86.61 -145.47 REMARK 500 1 LEU A 20 51.56 -98.69 REMARK 500 1 VAL A 21 107.65 -53.57 REMARK 500 1 LYS A 22 120.75 -174.46 REMARK 500 1 GLU A 24 147.94 60.44 REMARK 500 1 ASP A 26 -173.43 -57.54 REMARK 500 1 ARG A 34 -156.04 -125.98 REMARK 500 1 GLU A 35 -88.54 -161.57 REMARK 500 1 HIS A 36 -46.72 -160.76 REMARK 500 1 SER A 38 -76.03 -73.60 REMARK 500 1 ASP A 39 55.95 -173.32 REMARK 500 1 GLU A 40 176.29 67.83 REMARK 500 1 MET A 44 -171.33 -55.23 REMARK 500 1 LYS A 46 76.17 -64.56 REMARK 500 1 ARG A 67 68.36 -170.86 REMARK 500 1 PHE A 68 177.81 -51.80 REMARK 500 1 THR A 70 136.83 -27.98 REMARK 500 1 ASN A 76 126.94 173.25 REMARK 500 1 VAL A 81 -73.82 -59.77 REMARK 500 1 PRO A 83 -168.10 -73.83 REMARK 500 1 LYS A 85 57.70 -96.42 REMARK 500 1 ILE A 88 100.97 -50.47 REMARK 500 1 ALA A 93 178.02 176.25 REMARK 500 2 VAL A 4 171.07 -55.06 REMARK 500 2 VAL A 8 91.38 -58.07 REMARK 500 2 GLU A 9 176.30 -51.00 REMARK 500 2 LYS A 22 -65.27 -162.87 REMARK 500 2 TYR A 23 -171.78 45.60 REMARK 500 2 ALA A 29 -58.58 -132.16 REMARK 500 2 VAL A 31 131.33 164.30 REMARK 500 2 GLU A 35 -85.22 -132.27 REMARK 500 2 HIS A 36 39.76 171.71 REMARK 500 2 GLU A 40 -179.19 169.19 REMARK 500 2 ALA A 43 137.86 60.07 REMARK 500 2 MET A 44 -167.13 -62.51 REMARK 500 2 LYS A 46 64.66 -69.25 REMARK 500 2 GLU A 57 31.56 -144.45 REMARK 500 2 ARG A 67 73.18 -152.42 REMARK 500 2 LEU A 69 57.58 -146.88 REMARK 500 2 THR A 70 135.95 -25.84 REMARK 500 2 MET A 74 -176.69 -178.58 REMARK 500 2 ASN A 76 137.17 171.81 REMARK 500 2 LYS A 85 73.72 -113.93 REMARK 500 2 ALA A 90 146.23 -170.75 REMARK 500 2 TYR A 92 -87.55 -108.12 REMARK 500 2 ALA A 93 -179.97 50.42 REMARK 500 3 LEU A 17 85.61 -167.07 REMARK 500 3 LEU A 20 57.68 -142.40 REMARK 500 REMARK 500 THIS ENTRY HAS 813 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 34 0.30 SIDE CHAIN REMARK 500 1 ARG A 67 0.23 SIDE CHAIN REMARK 500 2 ARG A 34 0.23 SIDE CHAIN REMARK 500 2 ARG A 67 0.19 SIDE CHAIN REMARK 500 3 ARG A 34 0.13 SIDE CHAIN REMARK 500 3 ARG A 67 0.17 SIDE CHAIN REMARK 500 4 ARG A 34 0.29 SIDE CHAIN REMARK 500 4 ARG A 67 0.21 SIDE CHAIN REMARK 500 5 ARG A 34 0.21 SIDE CHAIN REMARK 500 5 ARG A 67 0.31 SIDE CHAIN REMARK 500 6 ARG A 34 0.27 SIDE CHAIN REMARK 500 6 ARG A 67 0.29 SIDE CHAIN REMARK 500 7 ARG A 34 0.28 SIDE CHAIN REMARK 500 7 ARG A 67 0.30 SIDE CHAIN REMARK 500 8 ARG A 34 0.27 SIDE CHAIN REMARK 500 9 ARG A 34 0.29 SIDE CHAIN REMARK 500 9 ARG A 67 0.26 SIDE CHAIN REMARK 500 10 ARG A 34 0.30 SIDE CHAIN REMARK 500 10 ARG A 67 0.30 SIDE CHAIN REMARK 500 11 ARG A 34 0.29 SIDE CHAIN REMARK 500 11 ARG A 67 0.24 SIDE CHAIN REMARK 500 12 ARG A 34 0.28 SIDE CHAIN REMARK 500 12 ARG A 67 0.27 SIDE CHAIN REMARK 500 13 ARG A 34 0.17 SIDE CHAIN REMARK 500 13 ARG A 67 0.28 SIDE CHAIN REMARK 500 14 ARG A 34 0.28 SIDE CHAIN REMARK 500 14 ARG A 67 0.22 SIDE CHAIN REMARK 500 15 ARG A 34 0.30 SIDE CHAIN REMARK 500 15 ARG A 67 0.26 SIDE CHAIN REMARK 500 16 ARG A 34 0.21 SIDE CHAIN REMARK 500 16 ARG A 67 0.20 SIDE CHAIN REMARK 500 17 ARG A 34 0.26 SIDE CHAIN REMARK 500 17 ARG A 67 0.24 SIDE CHAIN REMARK 500 18 ARG A 34 0.09 SIDE CHAIN REMARK 500 18 ARG A 67 0.26 SIDE CHAIN REMARK 500 19 ARG A 34 0.22 SIDE CHAIN REMARK 500 19 ARG A 67 0.28 SIDE CHAIN REMARK 500 20 ARG A 34 0.31 SIDE CHAIN REMARK 500 21 ARG A 34 0.31 SIDE CHAIN REMARK 500 21 ARG A 67 0.14 SIDE CHAIN REMARK 500 22 ARG A 34 0.11 SIDE CHAIN REMARK 500 22 ARG A 67 0.10 SIDE CHAIN REMARK 500 23 ARG A 34 0.29 SIDE CHAIN REMARK 500 23 ARG A 67 0.15 SIDE CHAIN REMARK 500 24 ARG A 34 0.12 SIDE CHAIN REMARK 500 24 ARG A 67 0.12 SIDE CHAIN REMARK 500 25 ARG A 34 0.30 SIDE CHAIN REMARK 500 25 ARG A 67 0.24 SIDE CHAIN REMARK 500 26 ARG A 34 0.28 SIDE CHAIN REMARK 500 26 ARG A 67 0.15 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 72 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1BMW A 1 96 UNP P43214 MPAP2_PHLPR 27 122 SEQRES 1 A 96 VAL PRO LYS VAL THR PHE THR VAL GLU LYS GLY SER ASN SEQRES 2 A 96 GLU LYS HIS LEU ALA VAL LEU VAL LYS TYR GLU GLY ASP SEQRES 3 A 96 THR MET ALA GLU VAL GLU LEU ARG GLU HIS GLY SER ASP SEQRES 4 A 96 GLU TRP VAL ALA MET THR LYS GLY GLU GLY GLY VAL TRP SEQRES 5 A 96 THR PHE ASP SER GLU GLU PRO LEU GLN GLY PRO PHE ASN SEQRES 6 A 96 PHE ARG PHE LEU THR GLU LYS GLY MET LYS ASN VAL PHE SEQRES 7 A 96 ASP ASP VAL VAL PRO GLU LYS TYR THR ILE GLY ALA THR SEQRES 8 A 96 TYR ALA PRO GLU GLU SHEET 1 A 2 VAL A 31 LEU A 33 0 SHEET 2 A 2 PHE A 66 PHE A 68 -1 N ARG A 67 O GLU A 32 SHEET 1 B 2 LEU A 17 VAL A 19 0 SHEET 2 B 2 TRP A 52 PHE A 54 -1 N PHE A 54 O LEU A 17 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 - b 16 2 Bytes