Header list of 1ls8.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSPORT PROTEIN 17-MAY-02 1LS8 TITLE NMR STRUCTURE OF THE UNLIGANDED BOMBYX MORI PHEROMONE-BINDING PROTEIN TITLE 2 AT PHYSIOLOGICAL PH COMPND MOL_ID: 1; COMPND 2 MOLECULE: PHEROMONE BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PBP; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOMBYX MORI; SOURCE 3 ORGANISM_COMMON: DOMESTIC SILKWORM; SOURCE 4 ORGANISM_TAXID: 7091; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS PHEROMONE BINDING PROTEIN, BMPBP, BMPBPB, SOLUTION STRUCTURE, KEYWDS 2 TRANSPORT PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR D.LEE,F.DAMBERGER,R.HORST,P.GUNTERT,W.S.LEAL,K.WUTHRICH REVDAT 3 23-FEB-22 1LS8 1 REMARK REVDAT 2 24-FEB-09 1LS8 1 VERSN REVDAT 1 20-NOV-02 1LS8 0 JRNL AUTH D.LEE,F.F.DAMBERGER,R.HORST,P.GUNTERT,L.NIKONOVA,W.S.LEAL, JRNL AUTH 2 K.WUTHRICH JRNL TITL NMR STRUCTURE OF THE UNLIGANDED BOMBYX MORI JRNL TITL 2 PHEROMONE-BINDING PROTEIN AT PHYSIOLOGICAL PH JRNL REF FEBS LETT. V. 531 314 2002 JRNL REFN ISSN 0014-5793 JRNL PMID 12417333 JRNL DOI 10.1016/S0014-5793(02)03548-2 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA, OPALP REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LS8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-MAY-02. REMARK 100 THE DEPOSITION ID IS D_1000016239. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 0.7MM BMPBP 15N,13C; 50MM REMARK 210 PHOSPHATE BUFFER; 95% H2O, 5% 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; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CANDID REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS ENERGY REMARK 210 MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 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 OD2 ASP A 32 HG1 THR A 48 1.59 REMARK 500 REMARK 500 REMARK: NULL 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 5 ARG A 46 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES REMARK 500 5 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 7 CYS A 108 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 12 CYS A 108 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 13 CYS A 108 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 16 ARG A 46 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 GLN A 2 -63.31 66.43 REMARK 500 1 LEU A 8 -8.41 -56.19 REMARK 500 1 TYR A 34 97.22 -69.72 REMARK 500 1 ASN A 35 99.02 35.52 REMARK 500 1 TRP A 37 -140.48 60.88 REMARK 500 1 LYS A 38 -170.05 57.34 REMARK 500 1 PRO A 102 -74.99 -68.58 REMARK 500 1 ALA A 128 64.13 -167.33 REMARK 500 1 SER A 130 11.97 -153.40 REMARK 500 1 ASP A 132 -172.20 51.37 REMARK 500 1 VAL A 133 76.41 37.43 REMARK 500 1 ALA A 140 89.09 50.81 REMARK 500 2 LEU A 8 -7.94 -58.72 REMARK 500 2 LEU A 10 -99.67 -107.50 REMARK 500 2 PHE A 12 -77.31 -58.92 REMARK 500 2 LYS A 14 1.68 -68.01 REMARK 500 2 LEU A 25 -157.20 -83.25 REMARK 500 2 ASN A 35 113.99 -164.71 REMARK 500 2 TRP A 37 -81.89 65.30 REMARK 500 2 ASN A 45 109.55 -51.39 REMARK 500 2 PRO A 64 43.93 -64.71 REMARK 500 2 GLU A 65 -64.53 -146.15 REMARK 500 2 PRO A 102 -175.20 -66.51 REMARK 500 2 TRP A 127 38.13 -90.17 REMARK 500 2 SER A 130 -47.96 70.88 REMARK 500 2 VAL A 133 26.51 -149.64 REMARK 500 2 ALA A 134 -83.87 81.08 REMARK 500 2 LEU A 139 57.83 -100.25 REMARK 500 2 ALA A 140 110.52 -169.17 REMARK 500 3 ASN A 35 83.41 51.77 REMARK 500 3 LYS A 38 119.43 65.98 REMARK 500 3 GLU A 39 -9.34 -56.59 REMARK 500 3 ILE A 43 100.12 -39.94 REMARK 500 3 MET A 61 -64.85 -97.93 REMARK 500 3 PRO A 64 42.28 -90.32 REMARK 500 3 GLU A 65 -43.65 -139.19 REMARK 500 3 PRO A 102 -73.91 -70.84 REMARK 500 3 ALA A 128 89.26 -163.77 REMARK 500 3 SER A 130 -60.78 -155.67 REMARK 500 3 ALA A 134 -64.85 166.54 REMARK 500 3 GLU A 137 -175.60 54.51 REMARK 500 3 LEU A 139 48.70 -77.95 REMARK 500 3 ALA A 140 71.06 58.33 REMARK 500 4 SER A 9 44.15 -80.54 REMARK 500 4 THR A 24 79.85 56.10 REMARK 500 4 PHE A 36 -100.59 -108.86 REMARK 500 4 TRP A 37 -167.22 48.10 REMARK 500 4 LYS A 38 104.46 51.07 REMARK 500 4 GLU A 39 -15.54 -47.68 REMARK 500 4 TYR A 41 95.39 -54.29 REMARK 500 REMARK 500 THIS ENTRY HAS 296 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 LYS A 38 GLU A 39 4 149.25 REMARK 500 ASP A 105 ASP A 106 6 -148.68 REMARK 500 SER A 130 MET A 131 10 -130.22 REMARK 500 GLY A 136 GLU A 137 16 144.33 REMARK 500 GLY A 136 GLU A 137 19 143.94 REMARK 500 MET A 131 ASP A 132 20 -140.04 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 46 0.15 SIDE CHAIN REMARK 500 2 ARG A 46 0.08 SIDE CHAIN REMARK 500 3 ARG A 46 0.10 SIDE CHAIN REMARK 500 4 ARG A 46 0.09 SIDE CHAIN REMARK 500 8 TYR A 34 0.08 SIDE CHAIN REMARK 500 9 ARG A 46 0.09 SIDE CHAIN REMARK 500 13 TYR A 41 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED DBREF 1LS8 A 1 142 UNP P34174 PBP_BOMMO 23 164 SEQRES 1 A 142 SER GLN GLU VAL MET LYS ASN LEU SER LEU ASN PHE GLY SEQRES 2 A 142 LYS ALA LEU ASP GLU CYS LYS LYS GLU MET THR LEU THR SEQRES 3 A 142 ASP ALA ILE ASN GLU ASP PHE TYR ASN PHE TRP LYS GLU SEQRES 4 A 142 GLY TYR GLU ILE LYS ASN ARG GLU THR GLY CYS ALA ILE SEQRES 5 A 142 MET CYS LEU SER THR LYS LEU ASN MET LEU ASP PRO GLU SEQRES 6 A 142 GLY ASN LEU HIS HIS GLY ASN ALA MET GLU PHE ALA LYS SEQRES 7 A 142 LYS HIS GLY ALA ASP GLU THR MET ALA GLN GLN LEU ILE SEQRES 8 A 142 ASP ILE VAL HIS GLY CYS GLU LYS SER THR PRO ALA ASN SEQRES 9 A 142 ASP ASP LYS CYS ILE TRP THR LEU GLY VAL ALA THR CYS SEQRES 10 A 142 PHE LYS ALA GLU ILE HIS LYS LEU ASN TRP ALA PRO SER SEQRES 11 A 142 MET ASP VAL ALA VAL GLY GLU ILE LEU ALA GLU VAL HELIX 1 1 GLU A 3 LEU A 8 1 6 HELIX 2 2 LEU A 16 GLU A 22 1 7 HELIX 3 3 ILE A 29 ASP A 32 1 4 HELIX 4 4 ARG A 46 LEU A 59 1 14 HELIX 5 5 HIS A 70 LYS A 79 1 10 HELIX 6 6 GLU A 84 SER A 100 1 17 HELIX 7 7 LYS A 107 LYS A 124 1 18 SSBOND 1 CYS A 19 CYS A 54 1555 1555 2.05 SSBOND 2 CYS A 50 CYS A 108 1555 1555 2.03 SSBOND 3 CYS A 97 CYS A 117 1555 1555 2.02 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 23 2 Bytes