Header list of 1cto.pdb file
Complete list - 14 20 Bytes
HEADER BINDING PROTEIN 25-SEP-96 1CTO TITLE NMR STRUCTURE OF THE C-TERMINAL DOMAIN OF THE LIGAND-BINDING REGION OF TITLE 2 MURINE GRANULOCYTE COLONY-STIMULATING FACTOR RECEPTOR, MINIMIZED TITLE 3 AVERAGE STRUCTURE 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 AUTHOR K.YAMASAKI,S.NAITO,H.ANAGUCHI,T.OHKUBO,Y.OTA REVDAT 3 14-MAR-18 1CTO 1 REMARK REVDAT 2 24-FEB-09 1CTO 1 VERSN REVDAT 1 22-OCT-97 1CTO 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 1CTO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000172525. 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 : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE 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 SER A 2 -144.20 52.77 REMARK 500 SER A 3 -171.00 -53.40 REMARK 500 GLU A 5 102.89 56.16 REMARK 500 ASP A 13 95.57 -69.29 REMARK 500 VAL A 18 44.27 -108.47 REMARK 500 VAL A 19 -87.45 64.22 REMARK 500 SER A 20 -93.03 -85.77 REMARK 500 HIS A 21 49.75 161.01 REMARK 500 SER A 29 128.64 170.61 REMARK 500 LYS A 31 136.94 -179.30 REMARK 500 PRO A 32 -162.16 -77.80 REMARK 500 LYS A 34 165.01 43.73 REMARK 500 SER A 36 -156.57 36.56 REMARK 500 GLU A 37 -92.61 -133.02 REMARK 500 TYR A 38 -129.22 -83.44 REMARK 500 MET A 39 -140.68 176.30 REMARK 500 GLU A 40 54.36 71.90 REMARK 500 GLU A 42 134.45 112.47 REMARK 500 TYR A 47 116.42 -163.11 REMARK 500 LEU A 51 -155.92 -160.94 REMARK 500 ALA A 54 159.16 163.83 REMARK 500 TRP A 56 119.08 63.18 REMARK 500 PHE A 60 -166.65 -110.48 REMARK 500 CYS A 72 128.62 -170.30 REMARK 500 GLN A 76 -36.84 179.77 REMARK 500 ILE A 87 -142.52 -158.68 REMARK 500 LEU A 91 62.94 -175.65 REMARK 500 SER A 96 172.04 52.57 REMARK 500 TRP A 98 96.22 -49.09 REMARK 500 LEU A 102 -174.52 -170.10 REMARK 500 PRO A 106 -159.27 -77.67 REMARK 500 THR A 107 150.06 -40.19 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 ARG A 46 0.31 SIDE CHAIN REMARK 500 ARG A 85 0.20 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1CTO A 1 109 UNP P40223 CSF3R_MOUSE 211 333 SEQADV 1CTO A UNP P40223 GLU 214 DELETION SEQADV 1CTO A UNP P40223 SER 215 DELETION SEQADV 1CTO A UNP P40223 PRO 216 DELETION SEQADV 1CTO A UNP P40223 LYS 217 DELETION SEQADV 1CTO A UNP P40223 LEU 218 DELETION SEQADV 1CTO A UNP P40223 CYS 219 DELETION SEQADV 1CTO A UNP P40223 LEU 220 DELETION SEQADV 1CTO A UNP P40223 ASP 221 DELETION SEQADV 1CTO A UNP P40223 PRO 222 DELETION SEQADV 1CTO A UNP P40223 MET 223 DELETION SEQADV 1CTO A UNP P40223 ASP 224 DELETION SEQADV 1CTO A UNP P40223 VAL 225 DELETION SEQADV 1CTO A UNP P40223 VAL 226 DELETION SEQADV 1CTO 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
Complete list - 14 20 Bytes