Header list of 1pfn.pdb file
Complete list - v 3 2 Bytes
HEADER CYTOKINE 18-JUL-95 1PFN
TITLE PF4-M2 CHIMERIC MUTANT WITH THE FIRST 10 N-TERMINAL RESIDUES OF R-PF4
TITLE 2 REPLACED BY THE N-TERMINAL RESIDUES OF THE IL8 SEQUENCE. MODELS 16-27
TITLE 3 OF A 27-MODEL SET.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PF4-M2 CHIMERA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PLATELET FACTOR 4, PLATELET FACTOR M2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR K.H.MAYO,V.ROONGTA,E.ILYINA,R.MILIUS,S.BARKER,C.QUINLAN,G.LA ROSA,
AUTHOR 2 T.J.DALY
REVDAT 3 03-NOV-21 1PFN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PFN 1 VERSN
REVDAT 1 29-JAN-96 1PFN 0
JRNL AUTH K.H.MAYO,V.ROONGTA,E.ILYINA,R.MILIUS,S.BARKER,C.QUINLAN,
JRNL AUTH 2 G.LA ROSA,T.J.DALY
JRNL TITL NMR SOLUTION STRUCTURE OF THE 32-KDA PLATELET FACTOR 4
JRNL TITL 2 ELR-MOTIF N-TERMINAL CHIMERA: A SYMMETRIC TETRAMER.
JRNL REF BIOCHEMISTRY V. 34 11399 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7547867
JRNL DOI 10.1021/BI00036A012
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.ZHANG,L.CHEN,D.P.BANCROFT,C.K.LAI,T.E.MAIONE
REMARK 1 TITL CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4
REMARK 1 REF BIOCHEMISTRY V. 33 8361 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PFN 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_1000175645.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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: 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 5 83.00 56.04
REMARK 500 1 LYS A 6 118.46 -177.00
REMARK 500 1 GLU A 7 104.19 59.97
REMARK 500 1 LEU A 8 -75.32 -139.13
REMARK 500 1 ARG A 9 17.00 -149.66
REMARK 500 1 LYS A 14 -116.27 57.05
REMARK 500 1 THR A 16 57.77 -91.91
REMARK 500 1 ARG A 22 176.62 98.21
REMARK 500 1 HIS A 23 33.44 31.02
REMARK 500 1 THR A 25 -48.29 -134.78
REMARK 500 1 LEU A 45 -169.02 -105.91
REMARK 500 1 ILE A 51 -143.09 -105.76
REMARK 500 1 CYS A 52 143.12 -173.23
REMARK 500 1 GLN A 56 41.87 -100.20
REMARK 500 1 ALA B 5 173.43 -56.13
REMARK 500 1 GLU B 7 149.40 63.12
REMARK 500 1 LEU B 8 -79.84 176.25
REMARK 500 1 ARG B 9 58.31 -148.65
REMARK 500 1 LYS B 14 -114.88 57.51
REMARK 500 1 THR B 16 58.55 -91.70
REMARK 500 1 ARG B 22 -83.69 167.45
REMARK 500 1 LYS B 31 -169.71 -79.21
REMARK 500 1 PRO B 34 -70.17 -77.60
REMARK 500 1 ILE B 51 -146.45 -104.29
REMARK 500 1 CYS B 52 139.05 -170.97
REMARK 500 1 GLN B 56 43.42 -99.07
REMARK 500 1 LYS C 6 -156.86 -133.80
REMARK 500 1 LEU C 8 -145.96 -129.59
REMARK 500 1 LYS C 14 -115.56 55.49
REMARK 500 1 THR C 16 58.80 -92.04
REMARK 500 1 ARG C 22 -90.84 168.28
REMARK 500 1 THR C 25 -50.85 -126.21
REMARK 500 1 LYS C 31 -168.61 -78.89
REMARK 500 1 ILE C 51 -145.11 -104.84
REMARK 500 1 GLN C 56 44.05 -100.58
REMARK 500 1 ALA D 5 175.38 61.99
REMARK 500 1 LYS D 6 101.45 -162.96
REMARK 500 1 GLU D 7 97.47 59.65
REMARK 500 1 LEU D 8 -65.67 -125.25
REMARK 500 1 LYS D 14 -111.91 57.08
REMARK 500 1 ARG D 22 -88.66 168.01
REMARK 500 1 THR D 25 -52.61 -126.83
REMARK 500 1 LEU D 45 -169.68 -102.98
REMARK 500 1 ILE D 51 -144.45 -105.44
REMARK 500 1 CYS D 52 141.48 -172.62
REMARK 500 1 LEU D 53 -166.12 -125.99
REMARK 500 1 GLN D 56 43.87 -101.64
REMARK 500 2 SER A 4 55.22 -91.27
REMARK 500 2 ARG A 9 92.55 -168.82
REMARK 500 2 CYS A 12 79.43 -158.94
REMARK 500
REMARK 500 THIS ENTRY HAS 538 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 9 0.31 SIDE CHAIN
REMARK 500 1 ARG A 20 0.32 SIDE CHAIN
REMARK 500 1 ARG A 22 0.29 SIDE CHAIN
REMARK 500 1 ARG A 49 0.20 SIDE CHAIN
REMARK 500 1 ARG B 9 0.29 SIDE CHAIN
REMARK 500 1 ARG B 20 0.31 SIDE CHAIN
REMARK 500 1 ARG B 22 0.32 SIDE CHAIN
REMARK 500 1 ARG B 49 0.16 SIDE CHAIN
REMARK 500 1 ARG C 9 0.26 SIDE CHAIN
REMARK 500 1 ARG C 20 0.32 SIDE CHAIN
REMARK 500 1 ARG C 22 0.31 SIDE CHAIN
REMARK 500 1 ARG C 49 0.32 SIDE CHAIN
REMARK 500 1 ARG D 9 0.17 SIDE CHAIN
REMARK 500 1 ARG D 20 0.26 SIDE CHAIN
REMARK 500 1 ARG D 22 0.32 SIDE CHAIN
REMARK 500 1 ARG D 49 0.19 SIDE CHAIN
REMARK 500 2 ARG A 9 0.22 SIDE CHAIN
REMARK 500 2 ARG A 20 0.27 SIDE CHAIN
REMARK 500 2 ARG A 22 0.29 SIDE CHAIN
REMARK 500 2 ARG A 49 0.29 SIDE CHAIN
REMARK 500 2 ARG B 9 0.28 SIDE CHAIN
REMARK 500 2 ARG B 20 0.20 SIDE CHAIN
REMARK 500 2 ARG B 22 0.32 SIDE CHAIN
REMARK 500 2 ARG B 49 0.24 SIDE CHAIN
REMARK 500 2 ARG C 9 0.23 SIDE CHAIN
REMARK 500 2 ARG C 20 0.28 SIDE CHAIN
REMARK 500 2 ARG C 22 0.30 SIDE CHAIN
REMARK 500 2 ARG C 49 0.25 SIDE CHAIN
REMARK 500 2 ARG D 9 0.30 SIDE CHAIN
REMARK 500 2 ARG D 20 0.18 SIDE CHAIN
REMARK 500 2 ARG D 22 0.22 SIDE CHAIN
REMARK 500 2 ARG D 49 0.17 SIDE CHAIN
REMARK 500 3 ARG A 9 0.21 SIDE CHAIN
REMARK 500 3 ARG A 20 0.23 SIDE CHAIN
REMARK 500 3 ARG A 22 0.25 SIDE CHAIN
REMARK 500 3 ARG A 49 0.29 SIDE CHAIN
REMARK 500 3 ARG B 9 0.23 SIDE CHAIN
REMARK 500 3 ARG B 20 0.28 SIDE CHAIN
REMARK 500 3 ARG B 22 0.30 SIDE CHAIN
REMARK 500 3 ARG B 49 0.17 SIDE CHAIN
REMARK 500 3 ARG C 9 0.30 SIDE CHAIN
REMARK 500 3 ARG C 20 0.23 SIDE CHAIN
REMARK 500 3 ARG C 22 0.30 SIDE CHAIN
REMARK 500 3 ARG C 49 0.31 SIDE CHAIN
REMARK 500 3 ARG D 9 0.16 SIDE CHAIN
REMARK 500 3 ARG D 20 0.18 SIDE CHAIN
REMARK 500 3 ARG D 22 0.28 SIDE CHAIN
REMARK 500 3 ARG D 49 0.32 SIDE CHAIN
REMARK 500 4 ARG A 9 0.28 SIDE CHAIN
REMARK 500 4 ARG A 20 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 192 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PFN A 8 70 UNP P02776 PLF4_HUMAN 39 101
DBREF 1PFN B 8 70 UNP P02776 PLF4_HUMAN 39 101
DBREF 1PFN C 8 70 UNP P02776 PLF4_HUMAN 39 101
DBREF 1PFN D 8 70 UNP P02776 PLF4_HUMAN 39 101
SEQADV 1PFN ARG A 9 UNP P02776 GLN 40 ENGINEERED MUTATION
SEQADV 1PFN GLN A 11 UNP P02776 LEU 42 ENGINEERED MUTATION
SEQADV 1PFN ARG B 9 UNP P02776 GLN 40 ENGINEERED MUTATION
SEQADV 1PFN GLN B 11 UNP P02776 LEU 42 ENGINEERED MUTATION
SEQADV 1PFN ARG C 9 UNP P02776 GLN 40 ENGINEERED MUTATION
SEQADV 1PFN GLN C 11 UNP P02776 LEU 42 ENGINEERED MUTATION
SEQADV 1PFN ARG D 9 UNP P02776 GLN 40 ENGINEERED MUTATION
SEQADV 1PFN GLN D 11 UNP P02776 LEU 42 ENGINEERED MUTATION
SEQRES 1 A 68 MET SER ALA LYS GLU LEU ARG CYS GLN CYS VAL LYS THR
SEQRES 2 A 68 THR SER GLN VAL ARG PRO ARG HIS ILE THR SER LEU GLU
SEQRES 3 A 68 VAL ILE LYS ALA GLY PRO HIS CYS PRO THR ALA GLN LEU
SEQRES 4 A 68 ILE ALA THR LEU LYS ASN GLY ARG LYS ILE CYS LEU ASP
SEQRES 5 A 68 LEU GLN ALA PRO LEU TYR LYS LYS ILE ILE LYS LYS LEU
SEQRES 6 A 68 LEU GLU SER
SEQRES 1 B 68 MET SER ALA LYS GLU LEU ARG CYS GLN CYS VAL LYS THR
SEQRES 2 B 68 THR SER GLN VAL ARG PRO ARG HIS ILE THR SER LEU GLU
SEQRES 3 B 68 VAL ILE LYS ALA GLY PRO HIS CYS PRO THR ALA GLN LEU
SEQRES 4 B 68 ILE ALA THR LEU LYS ASN GLY ARG LYS ILE CYS LEU ASP
SEQRES 5 B 68 LEU GLN ALA PRO LEU TYR LYS LYS ILE ILE LYS LYS LEU
SEQRES 6 B 68 LEU GLU SER
SEQRES 1 C 68 MET SER ALA LYS GLU LEU ARG CYS GLN CYS VAL LYS THR
SEQRES 2 C 68 THR SER GLN VAL ARG PRO ARG HIS ILE THR SER LEU GLU
SEQRES 3 C 68 VAL ILE LYS ALA GLY PRO HIS CYS PRO THR ALA GLN LEU
SEQRES 4 C 68 ILE ALA THR LEU LYS ASN GLY ARG LYS ILE CYS LEU ASP
SEQRES 5 C 68 LEU GLN ALA PRO LEU TYR LYS LYS ILE ILE LYS LYS LEU
SEQRES 6 C 68 LEU GLU SER
SEQRES 1 D 68 MET SER ALA LYS GLU LEU ARG CYS GLN CYS VAL LYS THR
SEQRES 2 D 68 THR SER GLN VAL ARG PRO ARG HIS ILE THR SER LEU GLU
SEQRES 3 D 68 VAL ILE LYS ALA GLY PRO HIS CYS PRO THR ALA GLN LEU
SEQRES 4 D 68 ILE ALA THR LEU LYS ASN GLY ARG LYS ILE CYS LEU ASP
SEQRES 5 D 68 LEU GLN ALA PRO LEU TYR LYS LYS ILE ILE LYS LYS LEU
SEQRES 6 D 68 LEU GLU SER
HELIX 1 1 PRO A 58 LEU A 68 1 11
HELIX 2 2 PRO B 58 LEU B 68 1 11
HELIX 3 3 PRO C 58 LEU C 68 1 11
HELIX 4 4 PRO D 58 LEU D 68 1 11
SHEET 1 A 4 GLN A 40 THR A 44 0
SHEET 2 A 4 SER A 26 ILE A 30 -1 N ILE A 30 O GLN A 40
SHEET 3 A 4 SER B 26 ILE B 30 -1 N VAL B 29 O LEU A 27
SHEET 4 A 4 GLN B 40 THR B 44 -1 N THR B 44 O SER B 26
SHEET 1 B 4 GLN C 40 THR C 44 0
SHEET 2 B 4 SER C 26 ILE C 30 -1 N ILE C 30 O GLN C 40
SHEET 3 B 4 SER D 26 ILE D 30 -1 N VAL D 29 O LEU C 27
SHEET 4 B 4 GLN D 40 THR D 44 -1 N THR D 44 O SER D 26
SSBOND 1 CYS A 10 CYS A 36 1555 1555 2.02
SSBOND 2 CYS A 12 CYS A 52 1555 1555 2.01
SSBOND 3 CYS B 10 CYS B 36 1555 1555 2.02
SSBOND 4 CYS B 12 CYS B 52 1555 1555 2.03
SSBOND 5 CYS C 10 CYS C 36 1555 1555 2.03
SSBOND 6 CYS C 12 CYS C 52 1555 1555 2.01
SSBOND 7 CYS D 10 CYS D 36 1555 1555 2.02
SSBOND 8 CYS D 12 CYS D 52 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 - v 3 2 Bytes