Header list of 1gcf.pdb file
Complete list - r 14 2 Bytes
HEADER BINDING PROTEIN 10-APR-97 1GCF
TITLE NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION OF
TITLE 2 MURINE GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR, 12 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMAL-P;
SOURCE 8 OTHER_DETAILS: EXPRESSED AS A FUSION PROTEIN WITH MALTOSE BINDING
SOURCE 9 PROTEIN
KEYWDS BINDING PROTEIN, CYTOKINE RECEPTOR
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR K.YAMASAKI,S.NAITO,H.ANAGUCHI,T.OHKUBO,Y.OTA
REVDAT 3 14-MAR-18 1GCF 1 REMARK
REVDAT 2 24-FEB-09 1GCF 1 VERSN
REVDAT 1 22-OCT-97 1GCF 0
JRNL AUTH K.YAMASAKI,S.NAITO,H.ANAGUCHI,T.OHKUBO,Y.OTA
JRNL TITL SOLUTION STRUCTURE OF AN EXTRACELLULAR DOMAIN CONTAINING THE
JRNL TITL 2 WSXWS MOTIF OF THE GRANULOCYTE COLONY-STIMULATING FACTOR
JRNL TITL 3 RECEPTOR AND ITS INTERACTION WITH LIGAND.
JRNL REF NAT.STRUCT.BIOL. V. 4 498 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9187659
JRNL DOI 10.1038/NSB0697-498
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.ANAGUCHI,O.HIRAOKA,K.YAMASAKI,S.NAITO,Y.OTA
REMARK 1 TITL LIGAND BINDING CHARACTERISTICS OF THE CARBOXYL-TERMINAL
REMARK 1 TITL 2 DOMAIN OF THE CYTOKINE RECEPTOR HOMOLOGOUS REGION OF THE
REMARK 1 TITL 3 GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR
REMARK 1 REF J.BIOL.CHEM. V. 270 27845 1995
REMARK 1 REFN ISSN 0021-9258
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 1GCF 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_1000173516.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE 2D; 3D NMR
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : RANDOM.INP/DGSA.INP/ REFINE.INP
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL OF NOE, DIHEDRAL, AND VAN
REMARK 210 DER WAALS ENERGIES
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: 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 SER A 2 78.63 -150.53
REMARK 500 1 SER A 3 -148.41 -93.25
REMARK 500 1 PRO A 16 -93.15 -76.27
REMARK 500 1 VAL A 19 -75.55 77.99
REMARK 500 1 SER A 20 -154.44 -106.22
REMARK 500 1 PRO A 23 47.06 -80.73
REMARK 500 1 SER A 29 132.93 175.04
REMARK 500 1 PRO A 32 -94.91 -78.43
REMARK 500 1 TRP A 33 -100.06 -142.94
REMARK 500 1 LYS A 34 91.59 73.17
REMARK 500 1 PRO A 35 47.91 -80.80
REMARK 500 1 TYR A 38 -152.77 -73.14
REMARK 500 1 MET A 39 115.71 104.86
REMARK 500 1 GLU A 40 68.43 -118.56
REMARK 500 1 GLN A 41 -146.16 -71.04
REMARK 500 1 LEU A 51 -157.07 -155.18
REMARK 500 1 TRP A 56 125.02 65.85
REMARK 500 1 PHE A 60 -153.91 -132.35
REMARK 500 1 GLN A 68 71.87 -155.09
REMARK 500 1 HIS A 75 100.17 -165.31
REMARK 500 1 GLN A 76 -33.71 -179.82
REMARK 500 1 GLN A 83 -169.30 -121.53
REMARK 500 1 ILE A 87 -173.30 -173.89
REMARK 500 1 PHE A 94 -48.92 -142.42
REMARK 500 1 SER A 96 176.49 49.75
REMARK 500 1 PRO A 106 -159.63 -78.59
REMARK 500 1 THR A 107 156.21 -39.04
REMARK 500 2 SER A 3 -149.17 -61.06
REMARK 500 2 GLU A 5 74.89 83.26
REMARK 500 2 PRO A 16 -93.98 -77.57
REMARK 500 2 VAL A 19 -73.45 72.68
REMARK 500 2 SER A 20 -148.96 -57.40
REMARK 500 2 PRO A 23 40.39 -79.47
REMARK 500 2 SER A 29 121.77 169.83
REMARK 500 2 LYS A 31 135.27 179.35
REMARK 500 2 PRO A 32 -157.21 -83.63
REMARK 500 2 TRP A 33 54.43 -164.11
REMARK 500 2 SER A 36 -168.43 -73.71
REMARK 500 2 TYR A 38 -153.09 -102.74
REMARK 500 2 MET A 39 176.01 51.81
REMARK 500 2 GLN A 41 -96.91 -38.17
REMARK 500 2 GLU A 42 140.51 169.41
REMARK 500 2 LEU A 51 -159.67 -157.24
REMARK 500 2 LYS A 52 -80.63 -46.59
REMARK 500 2 TRP A 56 133.80 64.48
REMARK 500 2 PHE A 60 -164.94 -111.73
REMARK 500 2 SER A 65 113.43 -169.82
REMARK 500 2 LEU A 74 42.29 -90.47
REMARK 500 2 HIS A 75 74.13 -64.40
REMARK 500 2 GLN A 76 -20.82 176.53
REMARK 500
REMARK 500 THIS ENTRY HAS 347 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 46 0.30 SIDE CHAIN
REMARK 500 1 ARG A 88 0.23 SIDE CHAIN
REMARK 500 1 ARG A 105 0.20 SIDE CHAIN
REMARK 500 2 ARG A 46 0.31 SIDE CHAIN
REMARK 500 2 ARG A 85 0.14 SIDE CHAIN
REMARK 500 2 ARG A 88 0.29 SIDE CHAIN
REMARK 500 2 ARG A 105 0.29 SIDE CHAIN
REMARK 500 3 ARG A 46 0.31 SIDE CHAIN
REMARK 500 3 ARG A 85 0.19 SIDE CHAIN
REMARK 500 3 ARG A 88 0.16 SIDE CHAIN
REMARK 500 3 ARG A 105 0.20 SIDE CHAIN
REMARK 500 4 ARG A 46 0.19 SIDE CHAIN
REMARK 500 4 ARG A 85 0.27 SIDE CHAIN
REMARK 500 4 ARG A 88 0.12 SIDE CHAIN
REMARK 500 4 ARG A 105 0.21 SIDE CHAIN
REMARK 500 5 ARG A 46 0.22 SIDE CHAIN
REMARK 500 5 ARG A 85 0.22 SIDE CHAIN
REMARK 500 5 ARG A 88 0.26 SIDE CHAIN
REMARK 500 5 ARG A 105 0.22 SIDE CHAIN
REMARK 500 6 ARG A 46 0.13 SIDE CHAIN
REMARK 500 6 ARG A 85 0.09 SIDE CHAIN
REMARK 500 6 ARG A 88 0.25 SIDE CHAIN
REMARK 500 6 ARG A 105 0.26 SIDE CHAIN
REMARK 500 7 ARG A 46 0.26 SIDE CHAIN
REMARK 500 7 ARG A 85 0.28 SIDE CHAIN
REMARK 500 7 ARG A 88 0.30 SIDE CHAIN
REMARK 500 7 ARG A 105 0.30 SIDE CHAIN
REMARK 500 8 ARG A 46 0.27 SIDE CHAIN
REMARK 500 8 ARG A 85 0.25 SIDE CHAIN
REMARK 500 8 ARG A 88 0.27 SIDE CHAIN
REMARK 500 8 ARG A 105 0.22 SIDE CHAIN
REMARK 500 9 ARG A 46 0.26 SIDE CHAIN
REMARK 500 9 ARG A 85 0.32 SIDE CHAIN
REMARK 500 9 ARG A 88 0.24 SIDE CHAIN
REMARK 500 9 ARG A 105 0.31 SIDE CHAIN
REMARK 500 10 ARG A 46 0.32 SIDE CHAIN
REMARK 500 10 ARG A 85 0.25 SIDE CHAIN
REMARK 500 10 ARG A 88 0.29 SIDE CHAIN
REMARK 500 10 ARG A 105 0.22 SIDE CHAIN
REMARK 500 11 ARG A 46 0.24 SIDE CHAIN
REMARK 500 11 ARG A 85 0.10 SIDE CHAIN
REMARK 500 11 ARG A 88 0.21 SIDE CHAIN
REMARK 500 11 ARG A 105 0.30 SIDE CHAIN
REMARK 500 12 ARG A 46 0.14 SIDE CHAIN
REMARK 500 12 ARG A 88 0.30 SIDE CHAIN
REMARK 500 12 ARG A 105 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GCF A 1 109 UNP P40223 CSF3R_MOUSE 211 333
SEQADV 1GCF A UNP P40223 GLU 214 DELETION
SEQADV 1GCF A UNP P40223 SER 215 DELETION
SEQADV 1GCF A UNP P40223 PRO 216 DELETION
SEQADV 1GCF A UNP P40223 LYS 217 DELETION
SEQADV 1GCF A UNP P40223 LEU 218 DELETION
SEQADV 1GCF A UNP P40223 CYS 219 DELETION
SEQADV 1GCF A UNP P40223 LEU 220 DELETION
SEQADV 1GCF A UNP P40223 ASP 221 DELETION
SEQADV 1GCF A UNP P40223 PRO 222 DELETION
SEQADV 1GCF A UNP P40223 MET 223 DELETION
SEQADV 1GCF A UNP P40223 ASP 224 DELETION
SEQADV 1GCF A UNP P40223 VAL 225 DELETION
SEQADV 1GCF A UNP P40223 VAL 226 DELETION
SEQADV 1GCF A UNP P40223 LYS 227 DELETION
SEQRES 1 A 109 GLY SER SER LEU GLU PRO PRO MET LEU GLN ALA LEU ASP
SEQRES 2 A 109 ILE GLY PRO ASP VAL VAL SER HIS GLN PRO GLY CYS LEU
SEQRES 3 A 109 TRP LEU SER TRP LYS PRO TRP LYS PRO SER GLU TYR MET
SEQRES 4 A 109 GLU GLN GLU CYS GLU LEU ARG TYR GLN PRO GLN LEU LYS
SEQRES 5 A 109 GLY ALA ASN TRP THR LEU VAL PHE HIS LEU PRO SER SER
SEQRES 6 A 109 LYS ASP GLN PHE GLU LEU CYS GLY LEU HIS GLN ALA PRO
SEQRES 7 A 109 VAL TYR THR LEU GLN MET ARG CYS ILE ARG SER SER LEU
SEQRES 8 A 109 PRO GLY PHE TRP SER PRO TRP SER PRO GLY LEU GLN LEU
SEQRES 9 A 109 ARG PRO THR MET LYS
SHEET 1 1 3 MET A 8 ALA A 11 0
SHEET 2 1 3 CYS A 25 LYS A 31 -1 H SER A 29 O GLN A 10
SHEET 3 1 3 PHE A 69 CYS A 72 -1 H LEU A 71 O LEU A 26
SHEET 1 2 4 TRP A 56 PHE A 60 0
SHEET 2 2 4 CYS A 43 PRO A 49 -1 H LEU A 45 O VAL A 59
SHEET 3 2 4 VAL A 79 CYS A 86 -1 H ARG A 85 O GLU A 44
SHEET 4 2 4 LEU A 102 ARG A 105 -1 H LEU A 102 O LEU A 82
SSBOND 1 CYS A 25 CYS A 72 1555 1555 2.02
SSBOND 2 CYS A 43 CYS A 86 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 - r 14 2 Bytes