Header list of 1jfn.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID TRANSPORT 21-JUN-01 1JFN
TITLE SOLUTION STRUCTURE OF HUMAN APOLIPOPROTEIN(A) KRINGLE IV TYPE 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPROTEIN A, KIV-T6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: APO(A) KIV-T6;
COMPND 5 SYNONYM: APO(A) KIV-T6; LIPOPROTEIN, LP(A); APOLIPOPROTEIN LP(A);
COMPND 6 APO(A); LP(A);
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: APOA;
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS KRINGLE DOMAIN, PROTEIN-PROTEIN RECOGNITION, LP(A), LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.MADEREGGER,W.BERMEL,A.HRZENJAK,G.M.KOSTNER,H.STERK
REVDAT 3 23-FEB-22 1JFN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1JFN 1 VERSN
REVDAT 1 28-JUN-02 1JFN 0
JRNL AUTH B.MADEREGGER,W.BERMEL,A.HRZENJAK,G.M.KOSTNER,H.STERK
JRNL TITL SOLUTION STRUCTURE OF HUMAN APOLIPOPROTEIN(A) KRINGLE IV
JRNL TITL 2 TYPE 6.
JRNL REF BIOCHEMISTRY V. 41 660 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11781107
JRNL DOI 10.1021/BI011430K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.6, X-PLOR 3.0
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUENGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JFN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013714.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 65 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM APO(A) KIV-T6 U-15N;15 MM
REMARK 210 PHOSPHATE BUFFER, 50MM NACL, PH
REMARK 210 6.5; 0.7MM APO(A) KIV-T6 U-15N,U-
REMARK 210 13C;15 MM PHOSPHATE BUFFER, 50MM
REMARK 210 NACL, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, XWINNMR 2.6, X-PLOR
REMARK 210 3.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 150
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
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 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 H TYR A 26 O THR A 100 1.50
REMARK 500 H GLN A 47 O TYR A 86 1.54
REMARK 500 O PHE A 37 H THR A 39 1.56
REMARK 500 H VAL A 41 O TYR A 96 1.59
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 HIS A 7 -85.03 -103.94
REMARK 500 1 ILE A 10 59.85 -107.70
REMARK 500 1 GLU A 11 74.06 -63.74
REMARK 500 1 GLN A 23 73.84 -160.41
REMARK 500 1 ASP A 24 -164.46 -67.17
REMARK 500 1 SER A 36 59.78 -92.91
REMARK 500 1 SER A 38 42.50 -64.22
REMARK 500 1 ARG A 44 -164.69 -70.91
REMARK 500 1 SER A 50 30.96 -79.44
REMARK 500 1 THR A 53 -66.57 -98.81
REMARK 500 1 PRO A 54 -93.90 -73.55
REMARK 500 1 ARG A 59 71.46 51.79
REMARK 500 1 ARG A 71 -143.03 74.69
REMARK 500 1 GLU A 80 -172.97 -68.36
REMARK 500 1 GLN A 101 99.78 -61.71
REMARK 500 1 CYS A 102 98.18 -38.34
REMARK 500 1 GLU A 106 178.47 -47.98
REMARK 500 1 SER A 108 -73.45 61.24
REMARK 500 1 SER A 113 -72.41 -62.83
REMARK 500 2 ARG A 2 69.44 173.76
REMARK 500 2 ILE A 3 70.82 50.01
REMARK 500 2 HIS A 4 32.16 -141.13
REMARK 500 2 HIS A 5 -153.47 -124.76
REMARK 500 2 HIS A 6 22.32 -147.32
REMARK 500 2 GLU A 11 -83.44 -75.24
REMARK 500 2 GLN A 23 -147.01 -164.57
REMARK 500 2 ASP A 24 93.82 -33.77
REMARK 500 2 TYR A 33 88.64 -60.90
REMARK 500 2 SER A 38 38.57 -71.76
REMARK 500 2 ARG A 44 -169.80 -78.94
REMARK 500 2 SER A 50 26.92 -79.59
REMARK 500 2 MET A 52 38.29 -89.48
REMARK 500 2 THR A 53 -66.81 -103.59
REMARK 500 2 PRO A 54 -95.00 -73.69
REMARK 500 2 GLN A 58 -152.62 -96.48
REMARK 500 2 ARG A 59 82.35 42.49
REMARK 500 2 THR A 70 160.36 -49.37
REMARK 500 2 ARG A 71 -131.95 47.59
REMARK 500 2 ASN A 72 34.94 -99.11
REMARK 500 2 GLU A 80 -158.20 -58.52
REMARK 500 2 SER A 82 -179.33 -174.55
REMARK 500 2 CYS A 85 164.67 178.33
REMARK 500 2 ASN A 98 85.96 -53.92
REMARK 500 2 GLN A 101 85.60 -68.12
REMARK 500 2 VAL A 104 -82.83 -139.93
REMARK 500 2 GLU A 106 106.25 170.41
REMARK 500 3 ILE A 3 93.57 44.30
REMARK 500 3 HIS A 4 164.16 59.39
REMARK 500 3 HIS A 5 48.40 -163.85
REMARK 500 3 HIS A 6 87.28 54.74
REMARK 500
REMARK 500 THIS ENTRY HAS 405 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 2 0.20 SIDE CHAIN
REMARK 500 1 ARG A 13 0.25 SIDE CHAIN
REMARK 500 1 ARG A 34 0.27 SIDE CHAIN
REMARK 500 1 ARG A 44 0.31 SIDE CHAIN
REMARK 500 1 ARG A 59 0.21 SIDE CHAIN
REMARK 500 1 ARG A 71 0.30 SIDE CHAIN
REMARK 500 1 ARG A 75 0.20 SIDE CHAIN
REMARK 500 1 ARG A 93 0.19 SIDE CHAIN
REMARK 500 2 ARG A 2 0.13 SIDE CHAIN
REMARK 500 2 ARG A 13 0.30 SIDE CHAIN
REMARK 500 2 ARG A 34 0.23 SIDE CHAIN
REMARK 500 2 ARG A 44 0.31 SIDE CHAIN
REMARK 500 2 ARG A 59 0.23 SIDE CHAIN
REMARK 500 2 ARG A 75 0.24 SIDE CHAIN
REMARK 500 3 ARG A 2 0.32 SIDE CHAIN
REMARK 500 3 ARG A 13 0.32 SIDE CHAIN
REMARK 500 3 ARG A 34 0.12 SIDE CHAIN
REMARK 500 3 ARG A 44 0.20 SIDE CHAIN
REMARK 500 3 ARG A 59 0.28 SIDE CHAIN
REMARK 500 3 ARG A 71 0.29 SIDE CHAIN
REMARK 500 3 ARG A 75 0.32 SIDE CHAIN
REMARK 500 3 ARG A 93 0.32 SIDE CHAIN
REMARK 500 4 ARG A 2 0.32 SIDE CHAIN
REMARK 500 4 ARG A 13 0.31 SIDE CHAIN
REMARK 500 4 ARG A 34 0.23 SIDE CHAIN
REMARK 500 4 ARG A 44 0.24 SIDE CHAIN
REMARK 500 4 ARG A 59 0.14 SIDE CHAIN
REMARK 500 4 ARG A 71 0.24 SIDE CHAIN
REMARK 500 4 ARG A 75 0.23 SIDE CHAIN
REMARK 500 4 ARG A 93 0.28 SIDE CHAIN
REMARK 500 5 ARG A 2 0.19 SIDE CHAIN
REMARK 500 5 ARG A 34 0.26 SIDE CHAIN
REMARK 500 5 ARG A 44 0.13 SIDE CHAIN
REMARK 500 5 ARG A 59 0.29 SIDE CHAIN
REMARK 500 5 ARG A 71 0.30 SIDE CHAIN
REMARK 500 5 ARG A 75 0.31 SIDE CHAIN
REMARK 500 5 ARG A 93 0.31 SIDE CHAIN
REMARK 500 6 ARG A 2 0.31 SIDE CHAIN
REMARK 500 6 ARG A 13 0.32 SIDE CHAIN
REMARK 500 6 ARG A 34 0.27 SIDE CHAIN
REMARK 500 6 ARG A 44 0.23 SIDE CHAIN
REMARK 500 6 ARG A 59 0.30 SIDE CHAIN
REMARK 500 6 ARG A 71 0.08 SIDE CHAIN
REMARK 500 6 ARG A 75 0.23 SIDE CHAIN
REMARK 500 6 ARG A 93 0.08 SIDE CHAIN
REMARK 500 7 ARG A 2 0.30 SIDE CHAIN
REMARK 500 7 ARG A 13 0.31 SIDE CHAIN
REMARK 500 7 ARG A 34 0.30 SIDE CHAIN
REMARK 500 7 ARG A 44 0.32 SIDE CHAIN
REMARK 500 7 ARG A 59 0.16 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 113 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JFN A 14 119 UNP P08519 APOA_HUMAN 3665 3770
SEQADV 1JFN ALA A 1 UNP P08519 EXPRESSION TAG
SEQADV 1JFN ARG A 2 UNP P08519 EXPRESSION TAG
SEQADV 1JFN ILE A 3 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 4 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 5 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 6 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 7 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 8 UNP P08519 EXPRESSION TAG
SEQADV 1JFN HIS A 9 UNP P08519 EXPRESSION TAG
SEQADV 1JFN ILE A 10 UNP P08519 EXPRESSION TAG
SEQADV 1JFN GLU A 11 UNP P08519 EXPRESSION TAG
SEQADV 1JFN GLY A 12 UNP P08519 EXPRESSION TAG
SEQADV 1JFN ARG A 13 UNP P08519 EXPRESSION TAG
SEQRES 1 A 119 ALA ARG ILE HIS HIS HIS HIS HIS HIS ILE GLU GLY ARG
SEQRES 2 A 119 ALA PRO THR GLU GLN SER PRO GLY VAL GLN ASP CYS TYR
SEQRES 3 A 119 HIS GLY ASP GLY GLN SER TYR ARG GLY SER PHE SER THR
SEQRES 4 A 119 THR VAL THR GLY ARG THR CYS GLN SER TRP SER SER MET
SEQRES 5 A 119 THR PRO HIS TRP HIS GLN ARG THR THR GLU TYR TYR PRO
SEQRES 6 A 119 ASN GLY GLY LEU THR ARG ASN TYR CYS ARG ASN PRO ASP
SEQRES 7 A 119 ALA GLU ILE SER PRO TRP CYS TYR THR MET ASP PRO ASN
SEQRES 8 A 119 VAL ARG TRP GLU TYR CYS ASN LEU THR GLN CYS PRO VAL
SEQRES 9 A 119 THR GLU SER SER VAL LEU ALA THR SER THR ALA VAL SER
SEQRES 10 A 119 GLU GLN
HELIX 1 1 THR A 60 TYR A 64 5 5
SHEET 1 A 2 TRP A 84 TYR A 86 0
SHEET 2 A 2 TRP A 94 TYR A 96 -1 O GLU A 95 N CYS A 85
SSBOND 1 CYS A 25 CYS A 102 1555 1555 2.03
SSBOND 2 CYS A 46 CYS A 85 1555 1555 2.02
SSBOND 3 CYS A 74 CYS A 97 1555 1555 2.02
CRYST1 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