Header list of 1i16.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 20-MAY-98 1I16 TITLE STRUCTURE OF INTERLEUKIN 16: IMPLICATIONS FOR FUNCTION, NMR, 20 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN 16; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: LCF; 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 CELL: CD8+ T CELLS; SOURCE 7 CELLULAR_LOCATION: EXTRACELLULAR; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET16B KEYWDS CYTOKINE, LYMPHOCYTE CHEMOATTRACTANT FACTOR, PDZ DOMAIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.MUEHLHAHN,M.ZWECKSTETTER,J.GEORGESCU,C.CIOSTO,C.RENNER, AUTHOR 2 M.LANZENDOERFER,K.LANG,D.AMBROSIUS,M.BAIER,R.KURTH,T.A.HOLAK REVDAT 3 23-FEB-22 1I16 1 REMARK REVDAT 2 24-FEB-09 1I16 1 VERSN REVDAT 1 25-MAY-99 1I16 0 JRNL AUTH P.MUHLHAHN,M.ZWECKSTETTER,J.GEORGESCU,C.CIOSTO,C.RENNER, JRNL AUTH 2 M.LANZENDORFER,K.LANG,D.AMBROSIUS,M.BAIER,R.KURTH,T.A.HOLAK JRNL TITL STRUCTURE OF INTERLEUKIN 16 RESEMBLES A PDZ DOMAIN WITH AN JRNL TITL 2 OCCLUDED PEPTIDE BINDING SITE. JRNL REF NAT.STRUCT.BIOL. V. 5 682 1998 JRNL REFN ISSN 1072-8368 JRNL PMID 9699630 JRNL DOI 10.1038/1376 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: NULL REMARK 4 REMARK 4 1I16 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_1000174079. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 50 MM NACL REMARK 210 PRESSURE : NORMAL REMARK 210 SAMPLE CONTENTS : WATER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CCNMR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION, LEAST REMARK 210 TOTAL ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY ON 13C-, 15N- LABELED INTERLEUKIN 16. 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 O ILE A 102 H LEU A 105 1.45 REMARK 500 H LEU A 35 O VAL A 110 1.45 REMARK 500 H GLU A 47 O THR A 60 1.45 REMARK 500 O VAL A 33 H ILE A 112 1.47 REMARK 500 OE1 GLN A 84 H THR A 88 1.54 REMARK 500 O GLY A 43 H PHE A 65 1.57 REMARK 500 O GLU A 47 H THR A 60 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 ASP A 3 -168.93 -117.70 REMARK 500 1 LEU A 4 -176.30 -58.93 REMARK 500 1 SER A 6 -158.74 -164.70 REMARK 500 1 THR A 8 -165.32 -175.68 REMARK 500 1 SER A 10 90.69 -55.12 REMARK 500 1 ALA A 14 -71.44 -118.04 REMARK 500 1 SER A 15 169.62 54.49 REMARK 500 1 SER A 18 -74.75 69.90 REMARK 500 1 VAL A 22 84.09 64.24 REMARK 500 1 GLU A 23 156.22 -43.65 REMARK 500 1 SER A 24 -172.51 -67.45 REMARK 500 1 GLU A 27 92.52 52.89 REMARK 500 1 MET A 38 -32.23 -151.05 REMARK 500 1 LEU A 42 25.61 40.02 REMARK 500 1 SER A 52 44.97 -176.30 REMARK 500 1 ASP A 56 120.27 165.26 REMARK 500 1 LEU A 59 152.78 -43.25 REMARK 500 1 ALA A 68 -164.94 -177.85 REMARK 500 1 GLN A 72 71.84 -178.96 REMARK 500 1 SER A 73 -170.71 55.96 REMARK 500 1 TRP A 99 -9.50 -58.44 REMARK 500 1 SER A 118 175.41 80.91 REMARK 500 1 LEU A 119 -176.26 -55.25 REMARK 500 1 GLN A 120 46.96 74.70 REMARK 500 1 GLU A 123 38.01 -165.10 REMARK 500 1 THR A 125 87.60 45.34 REMARK 500 1 ALA A 127 49.34 -98.58 REMARK 500 2 ASP A 3 -72.14 -65.93 REMARK 500 2 SER A 6 82.13 51.12 REMARK 500 2 SER A 7 -165.81 -75.61 REMARK 500 2 THR A 8 139.83 61.18 REMARK 500 2 ALA A 17 106.11 -47.61 REMARK 500 2 SER A 18 -73.46 -121.32 REMARK 500 2 ASP A 19 75.63 -67.83 REMARK 500 2 SER A 21 81.19 54.92 REMARK 500 2 VAL A 22 98.46 -54.24 REMARK 500 2 GLU A 23 155.18 64.00 REMARK 500 2 SER A 24 55.94 -161.02 REMARK 500 2 ALA A 26 -173.29 46.74 REMARK 500 2 GLU A 27 97.20 65.94 REMARK 500 2 ALA A 28 145.33 80.55 REMARK 500 2 MET A 38 32.26 -151.06 REMARK 500 2 SER A 39 -78.41 -150.54 REMARK 500 2 LEU A 42 -2.22 63.73 REMARK 500 2 LYS A 50 172.63 -47.62 REMARK 500 2 LEU A 53 -40.03 80.86 REMARK 500 2 ASP A 56 176.84 57.38 REMARK 500 2 LYS A 66 75.82 49.62 REMARK 500 2 ALA A 68 137.71 -171.54 REMARK 500 2 ALA A 69 144.67 -176.16 REMARK 500 REMARK 500 THIS ENTRY HAS 654 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 63 0.22 SIDE CHAIN REMARK 500 1 ARG A 95 0.28 SIDE CHAIN REMARK 500 1 ARG A 115 0.28 SIDE CHAIN REMARK 500 1 ARG A 116 0.22 SIDE CHAIN REMARK 500 2 ARG A 63 0.32 SIDE CHAIN REMARK 500 2 ARG A 95 0.14 SIDE CHAIN REMARK 500 2 ARG A 115 0.24 SIDE CHAIN REMARK 500 2 ARG A 116 0.29 SIDE CHAIN REMARK 500 3 ARG A 63 0.25 SIDE CHAIN REMARK 500 3 ARG A 115 0.30 SIDE CHAIN REMARK 500 3 ARG A 116 0.17 SIDE CHAIN REMARK 500 4 ARG A 63 0.29 SIDE CHAIN REMARK 500 4 ARG A 95 0.19 SIDE CHAIN REMARK 500 4 ARG A 115 0.16 SIDE CHAIN REMARK 500 4 ARG A 116 0.32 SIDE CHAIN REMARK 500 5 ARG A 63 0.13 SIDE CHAIN REMARK 500 5 ARG A 95 0.11 SIDE CHAIN REMARK 500 5 ARG A 115 0.32 SIDE CHAIN REMARK 500 5 ARG A 116 0.31 SIDE CHAIN REMARK 500 6 ARG A 63 0.31 SIDE CHAIN REMARK 500 6 ARG A 95 0.16 SIDE CHAIN REMARK 500 6 ARG A 115 0.25 SIDE CHAIN REMARK 500 6 ARG A 116 0.14 SIDE CHAIN REMARK 500 7 ARG A 63 0.25 SIDE CHAIN REMARK 500 7 ARG A 95 0.32 SIDE CHAIN REMARK 500 7 ARG A 115 0.29 SIDE CHAIN REMARK 500 7 ARG A 116 0.31 SIDE CHAIN REMARK 500 8 ARG A 63 0.30 SIDE CHAIN REMARK 500 8 ARG A 95 0.23 SIDE CHAIN REMARK 500 8 ARG A 116 0.32 SIDE CHAIN REMARK 500 9 ARG A 63 0.24 SIDE CHAIN REMARK 500 9 ARG A 95 0.32 SIDE CHAIN REMARK 500 9 ARG A 115 0.24 SIDE CHAIN REMARK 500 9 ARG A 116 0.32 SIDE CHAIN REMARK 500 10 ARG A 63 0.23 SIDE CHAIN REMARK 500 10 ARG A 95 0.23 SIDE CHAIN REMARK 500 10 ARG A 115 0.24 SIDE CHAIN REMARK 500 10 ARG A 116 0.26 SIDE CHAIN REMARK 500 11 ARG A 63 0.13 SIDE CHAIN REMARK 500 11 ARG A 95 0.08 SIDE CHAIN REMARK 500 11 ARG A 115 0.32 SIDE CHAIN REMARK 500 11 ARG A 116 0.20 SIDE CHAIN REMARK 500 12 ARG A 63 0.10 SIDE CHAIN REMARK 500 12 ARG A 95 0.32 SIDE CHAIN REMARK 500 12 ARG A 115 0.16 SIDE CHAIN REMARK 500 12 ARG A 116 0.25 SIDE CHAIN REMARK 500 13 ARG A 63 0.32 SIDE CHAIN REMARK 500 13 ARG A 95 0.30 SIDE CHAIN REMARK 500 13 ARG A 115 0.15 SIDE CHAIN REMARK 500 13 ARG A 116 0.24 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 77 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1I16 A 1 130 UNP Q14005 IL16_HUMAN 502 631 SEQRES 1 A 130 MET PRO ASP LEU ASN SER SER THR ASP SER ALA ALA SER SEQRES 2 A 130 ALA SER ALA ALA SER ASP VAL SER VAL GLU SER THR ALA SEQRES 3 A 130 GLU ALA THR VAL CYS THR VAL THR LEU GLU LYS MET SER SEQRES 4 A 130 ALA GLY LEU GLY PHE SER LEU GLU GLY GLY LYS GLY SER SEQRES 5 A 130 LEU HIS GLY ASP LYS PRO LEU THR ILE ASN ARG ILE PHE SEQRES 6 A 130 LYS GLY ALA ALA SER GLU GLN SER GLU THR VAL GLN PRO SEQRES 7 A 130 GLY ASP GLU ILE LEU GLN LEU GLY GLY THR ALA MET GLN SEQRES 8 A 130 GLY LEU THR ARG PHE GLU ALA TRP ASN ILE ILE LYS ALA SEQRES 9 A 130 LEU PRO ASP GLY PRO VAL THR ILE VAL ILE ARG ARG LYS SEQRES 10 A 130 SER LEU GLN SER LYS GLU THR THR ALA ALA GLY ASP SER HELIX 1 1 MET A 90 GLY A 92 5 3 HELIX 2 2 ARG A 95 LYS A 103 1 9 SHEET 1 A 2 ALA A 28 GLU A 36 0 SHEET 2 A 2 PRO A 109 LYS A 117 -1 N ARG A 116 O THR A 29 SHEET 1 B 2 PHE A 44 GLU A 47 0 SHEET 2 B 2 THR A 60 ILE A 64 -1 N ARG A 63 O SER A 45 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