Header list of 1ls4.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID TRANSPORT 16-MAY-02 1LS4 TITLE NMR STRUCTURE OF APOLIPOPHORIN-III FROM LOCUSTA MIGRATORIA COMPND MOL_ID: 1; COMPND 2 MOLECULE: APOLIPOPHORIN-III; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: APOLP-III; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: LOCUSTA MIGRATORIA; SOURCE 3 ORGANISM_COMMON: MIGRATORY LOCUST; SOURCE 4 ORGANISM_TAXID: 7004; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL-21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: LAPOIII-PET22B KEYWDS HELIX-BUNDLE, EXCHANGEABLE APOLIPOPROTEIN, LIPID TRANSPORT EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR D.FAN,J.WANG REVDAT 3 23-FEB-22 1LS4 1 REMARK REVDAT 2 24-FEB-09 1LS4 1 VERSN REVDAT 1 17-JUN-03 1LS4 0 JRNL AUTH D.FAN,Y.ZHENG,D.YANG,J.WANG JRNL TITL NMR SOLUTION STRUCTURE AND DYNAMICS OF AN EXCHANGEABLE JRNL TITL 2 APOLIPOPROTEIN,LOCUSTA MIGRATORIA APOLIPOPHORIN III. JRNL REF J.BIOL.CHEM. V. 278 21212 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12621043 JRNL DOI 10.1074/JBC.M208486200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LS4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-02. REMARK 100 THE DEPOSITION ID IS D_1000016235. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.4 REMARK 210 IONIC STRENGTH : 200 MM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1 MM APOLIPOPHORIN-III, 15N/13C REMARK 210 UNIFORMLY LABELED, 200 MM REMARK 210 PHOSPHATE BUFFER, 0.5 MM SODIUM REMARK 210 AZIDE 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 REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE 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 1-21 REMARK 465 RES C SSSEQI REMARK 465 MET A -15 REMARK 465 ASN A -14 REMARK 465 THR A -13 REMARK 465 LEU A -12 REMARK 465 LEU A -11 REMARK 465 ALA A -10 REMARK 465 VAL A -9 REMARK 465 LEU A -8 REMARK 465 MET A -7 REMARK 465 LEU A -6 REMARK 465 ALA A -5 REMARK 465 VAL A -4 REMARK 465 ALA A -3 REMARK 465 ALA A -2 REMARK 465 GLN A -1 REMARK 465 ALA A 0 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 LEU A 41 HG1 THR A 45 1.59 REMARK 500 O ILE A 55 H THR A 59 1.60 REMARK 500 O VAL A 133 H LEU A 137 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 4 72.64 59.65 REMARK 500 1 ALA A 5 -64.42 71.34 REMARK 500 1 ASN A 9 -44.55 -159.81 REMARK 500 1 PRO A 35 -73.50 -79.55 REMARK 500 1 PRO A 37 47.61 -81.41 REMARK 500 1 ASP A 38 -62.18 -174.59 REMARK 500 1 LYS A 68 -43.80 -135.43 REMARK 500 1 HIS A 69 -42.46 -169.31 REMARK 500 1 LEU A 95 59.95 -113.07 REMARK 500 1 GLN A 98 -34.00 169.67 REMARK 500 1 ALA A 126 -62.20 78.43 REMARK 500 1 ALA A 163 94.10 60.15 REMARK 500 2 ASP A 3 60.87 -106.71 REMARK 500 2 ASN A 9 -45.40 -144.09 REMARK 500 2 PRO A 35 39.73 -78.72 REMARK 500 2 THR A 36 169.16 54.10 REMARK 500 2 PRO A 37 49.72 -79.12 REMARK 500 2 ASP A 38 -41.20 -169.84 REMARK 500 2 LYS A 68 -41.58 -146.08 REMARK 500 2 HIS A 69 -49.67 175.19 REMARK 500 2 ASP A 90 60.83 -150.20 REMARK 500 2 SER A 94 92.75 44.40 REMARK 500 2 ASN A 96 -39.99 -172.53 REMARK 500 2 LEU A 97 -45.41 173.51 REMARK 500 2 ALA A 126 -62.94 82.98 REMARK 500 3 ASP A 3 -38.20 -133.13 REMARK 500 3 ALA A 4 -91.12 50.81 REMARK 500 3 ASN A 9 -31.83 178.19 REMARK 500 3 PRO A 35 -77.25 -77.38 REMARK 500 3 THR A 36 169.70 179.45 REMARK 500 3 ASP A 38 -53.66 166.10 REMARK 500 3 HIS A 69 53.86 -144.76 REMARK 500 3 ASP A 90 58.77 -148.06 REMARK 500 3 LEU A 95 28.85 44.14 REMARK 500 3 GLN A 98 -36.55 163.23 REMARK 500 3 ALA A 126 -63.14 84.16 REMARK 500 4 ALA A 4 -54.85 -128.16 REMARK 500 4 ASN A 9 -44.19 -163.32 REMARK 500 4 PRO A 35 -79.65 -78.34 REMARK 500 4 PRO A 37 43.90 -79.57 REMARK 500 4 ASP A 38 -62.25 -170.44 REMARK 500 4 LYS A 68 -44.19 -135.58 REMARK 500 4 HIS A 69 -48.98 177.07 REMARK 500 4 GLN A 98 -52.80 163.98 REMARK 500 4 ALA A 126 -63.16 82.79 REMARK 500 4 ALA A 163 -76.66 164.07 REMARK 500 5 PRO A 2 -87.00 -77.99 REMARK 500 5 ASN A 9 -60.37 179.40 REMARK 500 5 PRO A 35 -77.35 -76.74 REMARK 500 5 ASP A 38 -46.61 -136.77 REMARK 500 REMARK 500 THIS ENTRY HAS 242 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 1 0.21 SIDE CHAIN REMARK 500 1 ARG A 82 0.31 SIDE CHAIN REMARK 500 2 ARG A 1 0.29 SIDE CHAIN REMARK 500 2 ARG A 82 0.30 SIDE CHAIN REMARK 500 3 ARG A 1 0.28 SIDE CHAIN REMARK 500 3 ARG A 82 0.20 SIDE CHAIN REMARK 500 4 ARG A 1 0.29 SIDE CHAIN REMARK 500 4 ARG A 82 0.19 SIDE CHAIN REMARK 500 5 ARG A 1 0.23 SIDE CHAIN REMARK 500 5 ARG A 82 0.32 SIDE CHAIN REMARK 500 6 ARG A 1 0.32 SIDE CHAIN REMARK 500 6 ARG A 82 0.31 SIDE CHAIN REMARK 500 7 ARG A 1 0.17 SIDE CHAIN REMARK 500 7 ARG A 82 0.20 SIDE CHAIN REMARK 500 8 ARG A 1 0.28 SIDE CHAIN REMARK 500 8 ARG A 82 0.29 SIDE CHAIN REMARK 500 9 ARG A 1 0.25 SIDE CHAIN REMARK 500 9 ARG A 82 0.29 SIDE CHAIN REMARK 500 10 ARG A 1 0.10 SIDE CHAIN REMARK 500 10 ARG A 82 0.23 SIDE CHAIN REMARK 500 11 ARG A 1 0.11 SIDE CHAIN REMARK 500 11 ARG A 82 0.30 SIDE CHAIN REMARK 500 12 ARG A 1 0.30 SIDE CHAIN REMARK 500 12 ARG A 82 0.27 SIDE CHAIN REMARK 500 13 ARG A 1 0.16 SIDE CHAIN REMARK 500 13 ARG A 82 0.32 SIDE CHAIN REMARK 500 14 ARG A 1 0.29 SIDE CHAIN REMARK 500 14 ARG A 82 0.30 SIDE CHAIN REMARK 500 15 ARG A 1 0.24 SIDE CHAIN REMARK 500 15 ARG A 82 0.25 SIDE CHAIN REMARK 500 16 ARG A 1 0.29 SIDE CHAIN REMARK 500 16 ARG A 82 0.18 SIDE CHAIN REMARK 500 17 ARG A 1 0.31 SIDE CHAIN REMARK 500 17 ARG A 82 0.22 SIDE CHAIN REMARK 500 18 ARG A 1 0.15 SIDE CHAIN REMARK 500 19 ARG A 1 0.26 SIDE CHAIN REMARK 500 19 ARG A 82 0.32 SIDE CHAIN REMARK 500 20 ARG A 1 0.16 SIDE CHAIN REMARK 500 21 ARG A 1 0.31 SIDE CHAIN REMARK 500 21 ARG A 82 0.21 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AEP RELATED DB: PDB REMARK 900 THE X-RAY CRYSTAL STRUCTURE OF APOLIPOPHORIN-III FROM LOCUSTA REMARK 900 MIGRATORIA (A ISOFORM OF 162-RESIDUES) REMARK 900 RELATED ID: 1EQ1 RELATED DB: PDB REMARK 900 THE NMR STRUCTURE OF ANOTHER APOLIPOPHORIN-III FROM MANDUCA SEXTA DBREF 1LS4 A -15 164 UNP P10762 APL3_LOCMI 1 180 SEQRES 1 A 180 MET ASN THR LEU LEU ALA VAL LEU MET LEU ALA VAL ALA SEQRES 2 A 180 ALA GLN ALA ARG PRO ASP ALA ALA GLY HIS VAL ASN ILE SEQRES 3 A 180 ALA GLU ALA VAL GLN GLN LEU ASN HIS THR ILE VAL ASN SEQRES 4 A 180 ALA ALA HIS GLU LEU HIS GLU THR LEU GLY LEU PRO THR SEQRES 5 A 180 PRO ASP GLU ALA LEU ASN LEU LEU THR GLU GLN ALA ASN SEQRES 6 A 180 ALA PHE LYS THR LYS ILE ALA GLU VAL THR THR SER LEU SEQRES 7 A 180 LYS GLN GLU ALA GLU LYS HIS GLN GLY SER VAL ALA GLU SEQRES 8 A 180 GLN LEU ASN ALA PHE ALA ARG ASN LEU ASN ASN SER ILE SEQRES 9 A 180 HIS ASP ALA ALA THR SER LEU ASN LEU GLN ASP GLN LEU SEQRES 10 A 180 ASN SER LEU GLN SER ALA LEU THR ASN VAL GLY HIS GLN SEQRES 11 A 180 TRP GLN ASP ILE ALA THR LYS THR GLN ALA SER ALA GLN SEQRES 12 A 180 GLU ALA TRP ALA PRO VAL GLN SER ALA LEU GLN GLU ALA SEQRES 13 A 180 ALA GLU LYS THR LYS GLU ALA ALA ALA ASN LEU GLN ASN SEQRES 14 A 180 SER ILE GLN SER ALA VAL GLN LYS PRO ALA ASN HELIX 1 1 ASN A 9 LEU A 34 1 26 HELIX 2 2 ALA A 40 ALA A 66 1 27 HELIX 3 3 GLN A 70 ASP A 90 1 21 HELIX 4 4 GLN A 98 ALA A 126 1 29 HELIX 5 5 ALA A 129 LYS A 161 1 33 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