Header list of 2czp.pdb file
Complete list - 9 20 Bytes
HEADER TOXIN 14-JUL-05 2CZP TITLE STRUCTURAL ANALYSIS OF MEMBRANE-BOUND MASTOPARAN-X BY SOLID-STATE NMR COMPND MOL_ID: 1; COMPND 2 MOLECULE: MASTOPARAN X; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: MP-X; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VESPA SIMILLIMA XANTHOPTERA; SOURCE 3 ORGANISM_COMMON: JAPANESE YELLOW HORNET; SOURCE 4 ORGANISM_TAXID: 7448; SOURCE 5 STRAIN: XANTHOPTERA; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUBK19 KEYWDS MASTOPARAN X, MP-X, MEMBRANE BOUND, MAST CELL DEGRANULATION, VENOM, KEYWDS 2 AMIDATION, TOXIN EXPDTA SOLID-STATE NMR NUMMDL 10 AUTHOR Y.TODOKORO,T.FUJIWARA,I.YUMEN,K.FUKUSHIMA,S.-W.KANG,J.-S.PARK, AUTHOR 2 T.KOHNO,K.WAKAMATSU,H.AKUTSU REVDAT 4 09-MAR-22 2CZP 1 REMARK LINK REVDAT 3 24-FEB-09 2CZP 1 VERSN REVDAT 2 08-AUG-06 2CZP 1 JRNL REVDAT 1 04-JUL-06 2CZP 0 JRNL AUTH Y.TODOKORO,I.YUMEN,K.FUKUSHIMA,S.-W.KANG,J.-S.PARK,T.KOHNO, JRNL AUTH 2 K.WAKAMATSU,H.AKUTSU,T.FUJIWARA JRNL TITL STRUCTURE OF TIGHTLY MEMBRANE-BOUND MASTOPARAN-X, A JRNL TITL 2 G-PROTEIN-ACTIVATING PEPTIDE, DETERMINED BY SOLID-STATE NMR. JRNL REF BIOPHYS.J. V. 91 1368 2006 JRNL REFN ISSN 0006-3495 JRNL PMID 16714348 JRNL DOI 10.1529/BIOPHYSJ.106.082735 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : FELIX 2000, CYANA 1.0.6 REMARK 3 AUTHORS : ACCELRYS INC. (FELIX), GUENTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 31 RESTRAINTS, 5 DISTANCE RESTRAINTS DERIVED BY RR AND REDOR REMARK 3 EXPERIMENTS AND 26 DIHEDRAL ANGLE RESTRAINTS PREDICTED BY TALOS. REMARK 4 REMARK 4 2CZP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000024806. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 253; 283 REMARK 210 PH : 7.4; 7.4 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2MG OR 5MG UNIFORMLY 13C, 15N REMARK 210 LABELED MP-X BOUND TO MEMBRANE: REMARK 210 MOLAR RATIO MP-X:MEMBRANE=1:20; REMARK 210 2MG SELECTIVELY 13C LABELED MP-X REMARK 210 BOUND TO MEMBRANE: MOLAR RATIO REMARK 210 MP-X:MEMBRANE=1:20; 2MG REMARK 210 SELECTIVELY 13C, 15N LABELED MP- REMARK 210 X BOUND TO MEMBRANE: MOLAR RATIO REMARK 210 MP-X:MEMBRANE=1:20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_N-CA-CO; 3D_NI-COI+1-CAI+1; REMARK 210 2D_RFDR; 2D_SPCZ5; 2D_(CACB)I+1- REMARK 210 (COCA)I; 2D_NI-(COCA)I+1; 2D_N- REMARK 210 CA; 2D_NI-(COCACB)I+1; RR; REDOR REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : CMX REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 1.0.6, TALOS REMARK 210 2003.027.13.05 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE REMARK 210 1H/13C/15N AND DOUBLE-RESONANCE 1H/13C PROBES WITH 4MM AND 3.2MM REMARK 210 SPINNER MODULES. REMARK 217 REMARK 217 SOLID STATE NMR STUDY REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 217 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 LYS A 11 HN1 NH2 A 15 1.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 15 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A13 RELATED DB: PDB REMARK 900 G PROTEIN-BOUND CONFORMATION OF MASTOPARAN-X REMARK 900 RELATED ID: 1D7N RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE ANALYSIS OF THE MASTOPARAN WITH DETERGENTS REMARK 900 RELATED ID: 6214 RELATED DB: BMRB REMARK 900 SIGNAL ASSIGNMENTS AND CHEMICAL-SHIFT STRUCTURAL ANALYSIS OF REMARK 900 UNIFORMLY 13C, 15N-LABELED PEPTIDE, MASTOPARAN-X, BY REMARK 900 MULTIDIMENSIONAL SOLID-STATE NMR UNDER MAGIC-ANGLE SPINNING DBREF 2CZP A 1 14 UNP P01515 MAST_VESXA 1 14 SEQRES 1 A 15 ILE ASN TRP LYS GLY ILE ALA ALA MET ALA LYS LYS LEU SEQRES 2 A 15 LEU NH2 HET NH2 A 15 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 ASN A 2 LEU A 14 1 13 LINK C LEU A 14 N NH2 A 15 1555 1555 1.33 SITE 1 AC1 2 LYS A 11 LEU A 14 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 - 9 20 Bytes