Header list of 1uc6.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 08-APR-03 1UC6 TITLE SOLUTION STRUCTURE OF THE CARBOXYL TERMINAL DOMAIN OF THE CILIARY TITLE 2 NEUROTROPHIC FACTOR RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: CILIARY NEUROTROPHIC FACTOR RECEPTOR ALPHA; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: CARBOXYL TERMINAL DOMAIN; COMPND 5 SYNONYM: CNTF RECEPTOR; COMPND 6 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 BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1 KEYWDS CYTOKINE, CILIARY NEUROTROPHIC FACTOR, LEUKEMIA INHIBITORY FACTOR, KEYWDS 2 CYTOKINE RECEPTOR, FIBRONECTIN TYPE III DOMAIN-LIKE TOPOLOGY, SEVEN KEYWDS 3 BETA-STRANDS, TWO ANTI-PARALLEL BETA-SHEETS, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 21 MDLTYP MINIMIZED AVERAGE AUTHOR D.MAN,W.HE,K.H.SZE,G.KE,D.K.SMITH,N.Y.IP,G.ZHU REVDAT 3 02-MAR-22 1UC6 1 REMARK SEQADV REVDAT 2 24-FEB-09 1UC6 1 VERSN REVDAT 1 10-AUG-04 1UC6 0 JRNL AUTH D.MAN,W.HE,K.H.SZE,K.GONG,D.K.SMITH,G.ZHU,N.Y.IP JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE CILIARY JRNL TITL 2 NEUROTROPHIC FACTOR (CNTF) RECEPTOR AND LIGAND FREE JRNL TITL 3 ASSOCIATIONS AMONG COMPONENTS OF THE CNTF RECEPTOR COMPLEX JRNL REF J.BIOL.CHEM. V. 278 23285 2003 JRNL REFN ISSN 0021-9258 JRNL PMID 12707266 JRNL DOI 10.1074/JBC.M301976200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1 REMARK 3 AUTHORS : VARIAN (VNMR), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: FOLLOWING IDENTIFICATION OF THE GLOBAL REMARK 3 FOLD FROM MANUAL INSPECTION OF THE NUCLEAR OVERHAUSER EFFECT REMARK 3 SPECTROSCOPY DATA, AMBIGUOUS NOE RESTRAINTS WERE RESOLVED USING REMARK 3 THE ITERATIVE ARIA METHOD (NILGES ET AL., 1997) AND THE REMARK 3 STRUCTURE WAS DETERMINED BY SIMULATED ANNEALING USING THE CNS REMARK 3 PACKAGE. REMARK 4 REMARK 4 1UC6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-03. REMARK 100 THE DEPOSITION ID IS D_1000005666. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 100MM NACL, 10MM SODIUM REMARK 210 PHOSPHATE, 0.1MM EDTA REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM CNTFR-BC U-15N; 100MM NACL, REMARK 210 10MM SODIUM PHOSPHATE, 0.1MM REMARK 210 EDTA; 1.3MM CNTFR-BC U-15N,13C; REMARK 210 100MM NACL, 10MM SODIUM REMARK 210 PHOSPHATE, 0.1MM EDTA REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNHA; NJ-HMQC REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.0, PIPP 1.0, SPARKY REMARK 210 1.06, ARIA 1.1, CNS 1.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: FOR DETERMINATION OF HYDROGEN BONDS, AMIDE PROTONS REMARK 210 EXCHANGING SLOWLY WITH DEUTERONS WERE IDENTIFIED BY TIME COURSE REMARK 210 1H-15N HSQC EXPERIMENTS ON A FREEZE-DRIED 15N-LABELLED SAMPLE OF REMARK 210 BC DISSOLVED IN D2O BUFFER. 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 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 LEU A 3 82.70 51.40 REMARK 500 1 SER A 5 33.85 -79.25 REMARK 500 1 PRO A 23 32.84 -78.44 REMARK 500 1 ARG A 24 -4.03 -160.52 REMARK 500 1 PRO A 37 -95.98 -76.30 REMARK 500 1 PRO A 43 100.08 -57.17 REMARK 500 1 ASN A 65 36.80 -158.41 REMARK 500 1 GLU A 90 -78.40 -69.48 REMARK 500 1 THR A 93 65.75 -114.72 REMARK 500 1 SER A 98 -90.58 -110.53 REMARK 500 1 TRP A 106 109.30 -46.37 REMARK 500 2 LYS A 7 114.79 130.25 REMARK 500 2 PRO A 37 -105.88 -76.41 REMARK 500 2 LEU A 55 -40.43 -138.34 REMARK 500 2 ASN A 65 71.63 -157.59 REMARK 500 2 TRP A 97 101.48 -51.98 REMARK 500 2 SER A 98 -78.61 -91.21 REMARK 500 2 PRO A 105 -164.58 -68.33 REMARK 500 3 PRO A 11 139.78 -38.78 REMARK 500 3 PRO A 23 49.33 -76.37 REMARK 500 3 ARG A 24 -19.48 -170.92 REMARK 500 3 PRO A 37 -151.47 -73.00 REMARK 500 3 PRO A 39 44.45 -74.89 REMARK 500 3 LEU A 44 100.39 53.03 REMARK 500 3 SER A 98 -104.50 -90.64 REMARK 500 4 PRO A 2 39.19 -89.41 REMARK 500 4 LEU A 53 48.98 -76.24 REMARK 500 4 ILE A 54 -25.92 -148.69 REMARK 500 4 ASN A 65 103.26 -163.14 REMARK 500 4 LYS A 87 148.52 -173.40 REMARK 500 4 SER A 98 -87.59 -90.43 REMARK 500 4 PRO A 105 -145.64 -67.52 REMARK 500 5 PRO A 2 48.66 -83.86 REMARK 500 5 ARG A 24 0.64 -151.31 REMARK 500 5 PRO A 37 -85.85 -54.90 REMARK 500 5 GLU A 40 -50.49 -124.22 REMARK 500 5 SER A 41 32.71 -96.04 REMARK 500 5 LEU A 55 -51.32 -133.40 REMARK 500 5 SER A 98 -81.71 -90.49 REMARK 500 6 LYS A 7 83.89 49.08 REMARK 500 6 PRO A 10 -74.61 -48.62 REMARK 500 6 PRO A 37 -81.66 -77.12 REMARK 500 6 PRO A 43 99.35 -65.30 REMARK 500 6 ASN A 65 51.56 -148.44 REMARK 500 6 ILE A 91 34.98 -144.50 REMARK 500 6 TRP A 97 103.95 -59.62 REMARK 500 6 SER A 98 -86.50 -91.13 REMARK 500 7 PRO A 37 -102.13 -68.24 REMARK 500 7 ILE A 54 -28.54 -153.52 REMARK 500 7 ASN A 65 62.32 -165.80 REMARK 500 REMARK 500 THIS ENTRY HAS 167 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1UC6 A 6 109 UNP P26992 CNTFR_HUMAN 202 305 SEQADV 1UC6 GLY A 1 UNP P26992 EXPRESSION TAG SEQADV 1UC6 PRO A 2 UNP P26992 EXPRESSION TAG SEQADV 1UC6 LEU A 3 UNP P26992 EXPRESSION TAG SEQADV 1UC6 GLY A 4 UNP P26992 EXPRESSION TAG SEQADV 1UC6 SER A 5 UNP P26992 EXPRESSION TAG SEQADV 1UC6 ASN A 65 UNP P26992 ASP 261 CONFLICT SEQRES 1 A 109 GLY PRO LEU GLY SER VAL LYS PRO ASP PRO PRO GLU ASN SEQRES 2 A 109 VAL VAL ALA ARG PRO VAL PRO SER ASN PRO ARG ARG LEU SEQRES 3 A 109 GLU VAL THR TRP GLN THR PRO SER THR TRP PRO ASP PRO SEQRES 4 A 109 GLU SER PHE PRO LEU LYS PHE PHE LEU ARG TYR ARG PRO SEQRES 5 A 109 LEU ILE LEU ASP GLN TRP GLN HIS VAL GLU LEU SER ASN SEQRES 6 A 109 GLY THR ALA HIS THR ILE THR ASP ALA TYR ALA GLY LYS SEQRES 7 A 109 GLU TYR ILE ILE GLN VAL ALA ALA LYS ASP ASN GLU ILE SEQRES 8 A 109 GLY THR TRP SER ASP TRP SER VAL ALA ALA HIS ALA THR SEQRES 9 A 109 PRO TRP THR GLU GLU SHEET 1 A 3 GLU A 12 PRO A 18 0 SHEET 2 A 3 LEU A 26 GLN A 31 -1 O THR A 29 N VAL A 15 SHEET 3 A 3 ALA A 68 ILE A 71 -1 O HIS A 69 N VAL A 28 SHEET 1 B 4 VAL A 61 LEU A 63 0 SHEET 2 B 4 PHE A 46 PRO A 52 -1 N PHE A 46 O LEU A 63 SHEET 3 B 4 TYR A 80 ALA A 85 -1 O GLN A 83 N ARG A 49 SHEET 4 B 4 VAL A 99 ALA A 103 -1 O ALA A 103 N TYR A 80 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 2 2 Bytes