Header list of 1itf.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 22-AUG-97 1ITF
TITLE INTERFERON ALPHA-2A, NMR, 24 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON ALPHA-2A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INTERFERON, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR W.KLAUS,B.GSELL,A.M.LABHARDT,B.WIPF,H.SENN
REVDAT 3 23-FEB-22 1ITF 1 REMARK
REVDAT 2 24-FEB-09 1ITF 1 VERSN
REVDAT 1 03-DEC-97 1ITF 0
JRNL AUTH W.KLAUS,B.GSELL,A.M.LABHARDT,B.WIPF,H.SENN
JRNL TITL THE THREE-DIMENSIONAL HIGH RESOLUTION STRUCTURE OF HUMAN
JRNL TITL 2 INTERFERON ALPHA-2A DETERMINED BY HETERONUCLEAR NMR
JRNL TITL 3 SPECTROSCOPY IN SOLUTION.
JRNL REF J.MOL.BIOL. V. 274 661 1997
JRNL REFN ISSN 0022-2836
JRNL PMID 9417943
JRNL DOI 10.1006/JMBI.1997.1396
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : M. NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE FORTHCOMING PUBLICATION.
REMARK 4
REMARK 4 1ITF 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_1000174258.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HETERONUCLEAR 3D; 4D
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-500; AMX2-600; DMX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
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: 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 GLU A 113 H LEU A 117 1.56
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 2 56.89 -149.00
REMARK 500 1 THR A 6 -74.43 -133.98
REMARK 500 1 SER A 8 24.12 -157.91
REMARK 500 1 CYS A 29 53.37 -112.84
REMARK 500 1 PHE A 47 44.27 -148.09
REMARK 500 1 LYS A 49 58.32 -150.28
REMARK 500 1 THR A 106 -159.29 -125.67
REMARK 500 1 THR A 108 125.47 -38.98
REMARK 500 1 LEU A 110 -8.94 -53.22
REMARK 500 1 GLN A 158 -85.95 -109.72
REMARK 500 1 LYS A 164 70.38 -163.03
REMARK 500 2 CYS A 29 50.92 -101.88
REMARK 500 2 PHE A 47 46.08 -148.37
REMARK 500 2 LYS A 49 60.84 62.29
REMARK 500 2 ALA A 50 71.72 65.21
REMARK 500 2 GLU A 51 -48.50 -142.14
REMARK 500 2 THR A 108 43.20 -149.69
REMARK 500 2 LEU A 161 -166.65 -69.82
REMARK 500 2 ARG A 162 52.53 -91.15
REMARK 500 2 SER A 163 47.09 -94.08
REMARK 500 2 LYS A 164 41.91 -154.23
REMARK 500 3 LEU A 3 104.13 -44.39
REMARK 500 3 GLN A 5 60.55 -159.95
REMARK 500 3 THR A 6 -55.06 -149.36
REMARK 500 3 ARG A 22 106.41 -55.63
REMARK 500 3 CYS A 29 54.17 -114.86
REMARK 500 3 GLN A 48 -161.24 -70.61
REMARK 500 3 ALA A 50 36.68 -94.38
REMARK 500 3 THR A 106 29.25 -153.77
REMARK 500 3 GLU A 107 -76.24 -28.25
REMARK 500 3 THR A 108 -60.49 -169.09
REMARK 500 3 SER A 160 51.39 -100.51
REMARK 500 4 CYS A 29 56.26 -112.95
REMARK 500 4 PHE A 47 42.50 -148.40
REMARK 500 4 LYS A 49 93.05 66.15
REMARK 500 4 MET A 111 -8.22 -56.75
REMARK 500 5 THR A 6 -59.50 -123.13
REMARK 500 5 LEU A 9 18.60 -147.15
REMARK 500 5 CYS A 29 47.39 -105.15
REMARK 500 5 PHE A 47 43.81 -147.23
REMARK 500 5 LYS A 49 65.45 77.35
REMARK 500 5 GLU A 107 -65.48 -158.17
REMARK 500 5 LEU A 110 -64.18 -122.65
REMARK 500 5 SER A 160 -79.32 -105.62
REMARK 500 5 ARG A 162 58.75 -107.47
REMARK 500 6 GLN A 5 66.09 -153.14
REMARK 500 6 THR A 6 -86.42 -136.99
REMARK 500 6 SER A 8 102.48 -171.95
REMARK 500 6 LEU A 9 84.29 -172.10
REMARK 500 6 CYS A 29 51.20 -108.88
REMARK 500
REMARK 500 THIS ENTRY HAS 234 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 12 0.32 SIDE CHAIN
REMARK 500 1 ARG A 13 0.31 SIDE CHAIN
REMARK 500 1 ARG A 22 0.29 SIDE CHAIN
REMARK 500 1 ARG A 120 0.29 SIDE CHAIN
REMARK 500 1 ARG A 125 0.31 SIDE CHAIN
REMARK 500 1 ARG A 144 0.24 SIDE CHAIN
REMARK 500 1 ARG A 149 0.29 SIDE CHAIN
REMARK 500 1 ARG A 162 0.31 SIDE CHAIN
REMARK 500 2 ARG A 12 0.27 SIDE CHAIN
REMARK 500 2 ARG A 13 0.10 SIDE CHAIN
REMARK 500 2 ARG A 22 0.30 SIDE CHAIN
REMARK 500 2 ARG A 33 0.26 SIDE CHAIN
REMARK 500 2 ARG A 120 0.26 SIDE CHAIN
REMARK 500 2 ARG A 125 0.31 SIDE CHAIN
REMARK 500 2 ARG A 144 0.29 SIDE CHAIN
REMARK 500 2 ARG A 149 0.31 SIDE CHAIN
REMARK 500 2 ARG A 162 0.23 SIDE CHAIN
REMARK 500 3 ARG A 12 0.30 SIDE CHAIN
REMARK 500 3 ARG A 13 0.31 SIDE CHAIN
REMARK 500 3 ARG A 22 0.30 SIDE CHAIN
REMARK 500 3 ARG A 33 0.29 SIDE CHAIN
REMARK 500 3 ARG A 120 0.28 SIDE CHAIN
REMARK 500 3 ARG A 144 0.31 SIDE CHAIN
REMARK 500 3 ARG A 149 0.29 SIDE CHAIN
REMARK 500 3 ARG A 162 0.29 SIDE CHAIN
REMARK 500 4 ARG A 12 0.30 SIDE CHAIN
REMARK 500 4 ARG A 13 0.24 SIDE CHAIN
REMARK 500 4 ARG A 22 0.29 SIDE CHAIN
REMARK 500 4 ARG A 33 0.30 SIDE CHAIN
REMARK 500 4 ARG A 120 0.23 SIDE CHAIN
REMARK 500 4 ARG A 125 0.31 SIDE CHAIN
REMARK 500 4 ARG A 144 0.31 SIDE CHAIN
REMARK 500 4 ARG A 149 0.31 SIDE CHAIN
REMARK 500 4 ARG A 162 0.27 SIDE CHAIN
REMARK 500 5 ARG A 12 0.28 SIDE CHAIN
REMARK 500 5 ARG A 13 0.29 SIDE CHAIN
REMARK 500 5 ARG A 22 0.32 SIDE CHAIN
REMARK 500 5 ARG A 33 0.31 SIDE CHAIN
REMARK 500 5 ARG A 120 0.28 SIDE CHAIN
REMARK 500 5 ARG A 125 0.31 SIDE CHAIN
REMARK 500 5 ARG A 144 0.25 SIDE CHAIN
REMARK 500 5 ARG A 149 0.30 SIDE CHAIN
REMARK 500 5 ARG A 162 0.31 SIDE CHAIN
REMARK 500 6 ARG A 12 0.29 SIDE CHAIN
REMARK 500 6 ARG A 13 0.31 SIDE CHAIN
REMARK 500 6 ARG A 22 0.29 SIDE CHAIN
REMARK 500 6 ARG A 33 0.31 SIDE CHAIN
REMARK 500 6 ARG A 120 0.24 SIDE CHAIN
REMARK 500 6 ARG A 125 0.30 SIDE CHAIN
REMARK 500 6 ARG A 144 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 214 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ITF A 1 165 UNP P01563 IFNA2_HUMAN 24 188
SEQRES 1 A 165 CYS ASP LEU PRO GLN THR HIS SER LEU GLY SER ARG ARG
SEQRES 2 A 165 THR LEU MET LEU LEU ALA GLN MET ARG LYS ILE SER LEU
SEQRES 3 A 165 PHE SER CYS LEU LYS ASP ARG HIS ASP PHE GLY PHE PRO
SEQRES 4 A 165 GLN GLU GLU PHE GLY ASN GLN PHE GLN LYS ALA GLU THR
SEQRES 5 A 165 ILE PRO VAL LEU HIS GLU MET ILE GLN GLN ILE PHE ASN
SEQRES 6 A 165 LEU PHE SER THR LYS ASP SER SER ALA ALA TRP ASP GLU
SEQRES 7 A 165 THR LEU LEU ASP LYS PHE TYR THR GLU LEU TYR GLN GLN
SEQRES 8 A 165 LEU ASN ASP LEU GLU ALA CYS VAL ILE GLN GLY VAL GLY
SEQRES 9 A 165 VAL THR GLU THR PRO LEU MET LYS GLU ASP SER ILE LEU
SEQRES 10 A 165 ALA VAL ARG LYS TYR PHE GLN ARG ILE THR LEU TYR LEU
SEQRES 11 A 165 LYS GLU LYS LYS TYR SER PRO CYS ALA TRP GLU VAL VAL
SEQRES 12 A 165 ARG ALA GLU ILE MET ARG SER PHE SER LEU SER THR ASN
SEQRES 13 A 165 LEU GLN GLU SER LEU ARG SER LYS GLU
HELIX 1 1 GLY A 10 MET A 21 1 12
HELIX 2 2 GLN A 40 PHE A 43 5 4
HELIX 3 3 ILE A 53 SER A 68 1 16
HELIX 4 4 LYS A 70 ALA A 75 1 6
HELIX 5 5 GLU A 78 ILE A 100 1 23
HELIX 6 6 LEU A 110 GLU A 132 5 23
HELIX 7 7 PRO A 137 LEU A 157 1 21
SSBOND 1 CYS A 1 CYS A 98 1555 1555 2.02
SSBOND 2 CYS A 29 CYS A 138 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