Header list of 1lmm.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 02-MAY-02 1LMM TITLE SOLUTION STRUCTURE OF PSMALMOTOXIN 1, THE FIRST CHARACTERIZED SPECIFIC TITLE 2 BLOCKER OF ASIC1A NA+ CHANNEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: PSALMOTOXIN 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PCTX1; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSALMOPOEUS CAMBRIDGEI; SOURCE 3 ORGANISM_COMMON: TRINIDAD CHEVRON TARANTULA; SOURCE 4 ORGANISM_TAXID: 179874; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ICK, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR P.ESCOUBAS,C.BERNARD,M.LAZDUNSKI,H.DARBON REVDAT 3 23-FEB-22 1LMM 1 REMARK REVDAT 2 24-FEB-09 1LMM 1 VERSN REVDAT 1 25-NOV-03 1LMM 0 JRNL AUTH P.ESCOUBAS,C.BERNARD,G.LAMBEAU,M.LAZDUNSKI,H.DARBON JRNL TITL RECOMBINANT PRODUCTION AND SOLUTION STRUCTURE OF PCTX1, THE JRNL TITL 2 SPECIFIC PEPTIDE INHIBITOR OF ASIC1A PROTON-GATED CATION JRNL TITL 3 CHANNELS JRNL REF PROTEIN SCI. V. 12 1332 2003 JRNL REFN ISSN 0961-8368 JRNL PMID 12824480 JRNL DOI 10.1110/PS.0307003 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1 REMARK 3 AUTHORS : BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1LMM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-02. REMARK 100 THE DEPOSITION ID IS D_1000016087. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 283; 300 REMARK 210 PH : 3.6; 3.6 REMARK 210 IONIC STRENGTH : NULL; NULL REMARK 210 PRESSURE : AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 2.9 MM REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3, DIANA REMARK 210 2.8 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 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: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 2 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 6 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 10 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 12 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 13 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 19 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES 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 VAL A 11 159.64 -41.19 REMARK 500 1 ASN A 12 83.36 75.20 REMARK 500 1 ARG A 13 -16.71 83.21 REMARK 500 1 HIS A 14 87.10 51.61 REMARK 500 1 CYS A 17 150.45 -42.91 REMARK 500 1 CYS A 18 -96.35 -70.13 REMARK 500 1 GLU A 19 -154.53 -61.89 REMARK 500 1 ARG A 26 -159.69 -74.64 REMARK 500 1 SER A 29 177.53 -57.53 REMARK 500 1 PHE A 30 -167.14 -66.04 REMARK 500 1 LYS A 36 -78.28 -54.15 REMARK 500 1 PRO A 38 -88.93 -92.67 REMARK 500 1 LYS A 39 -78.60 -70.27 REMARK 500 2 VAL A 11 86.10 -53.58 REMARK 500 2 ASN A 12 81.11 175.41 REMARK 500 2 HIS A 14 71.19 45.98 REMARK 500 2 CYS A 17 151.83 -47.25 REMARK 500 2 CYS A 18 -97.22 -67.81 REMARK 500 2 GLU A 19 -155.03 -62.87 REMARK 500 2 ARG A 28 -68.11 -100.78 REMARK 500 2 PHE A 30 -152.67 -70.25 REMARK 500 2 LYS A 36 -76.19 -48.73 REMARK 500 2 PRO A 38 71.42 -65.23 REMARK 500 3 ASP A 2 86.27 -60.34 REMARK 500 3 LYS A 6 -170.18 -59.88 REMARK 500 3 ASN A 12 18.92 59.50 REMARK 500 3 CYS A 18 -93.11 -69.96 REMARK 500 3 GLU A 19 -159.60 -61.41 REMARK 500 3 SER A 29 171.25 -58.88 REMARK 500 3 PHE A 30 -157.39 -68.60 REMARK 500 4 VAL A 11 82.02 -58.97 REMARK 500 4 ASN A 12 75.16 177.46 REMARK 500 4 HIS A 14 84.10 48.28 REMARK 500 4 CYS A 18 -94.71 -55.35 REMARK 500 4 GLU A 19 -154.94 -66.64 REMARK 500 4 ARG A 27 -73.05 -70.49 REMARK 500 4 PHE A 30 -147.11 -63.06 REMARK 500 4 PRO A 38 -70.14 -75.38 REMARK 500 5 CYS A 3 -95.47 -70.16 REMARK 500 5 VAL A 11 82.35 -60.47 REMARK 500 5 ASN A 12 81.50 177.59 REMARK 500 5 HIS A 14 83.63 46.23 REMARK 500 5 CYS A 18 -88.57 -70.24 REMARK 500 5 GLU A 19 66.47 -67.88 REMARK 500 5 ARG A 28 -82.15 -95.98 REMARK 500 5 PHE A 30 -153.66 -70.25 REMARK 500 5 VAL A 34 138.16 -170.33 REMARK 500 5 LYS A 36 -89.51 -48.15 REMARK 500 5 LYS A 39 82.65 -63.61 REMARK 500 6 VAL A 11 70.26 -67.60 REMARK 500 REMARK 500 THIS ENTRY HAS 204 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1LMM A 1 40 UNP P60514 TXP1_PSACA 1 40 SEQRES 1 A 40 GLU ASP CYS ILE PRO LYS TRP LYS GLY CYS VAL ASN ARG SEQRES 2 A 40 HIS GLY ASP CYS CYS GLU GLY LEU GLU CYS TRP LYS ARG SEQRES 3 A 40 ARG ARG SER PHE GLU VAL CYS VAL PRO LYS THR PRO LYS SEQRES 4 A 40 THR SHEET 1 A 2 GLU A 22 LYS A 25 0 SHEET 2 A 2 GLU A 31 VAL A 34 -1 O VAL A 34 N GLU A 22 SSBOND 1 CYS A 3 CYS A 18 1555 1555 2.03 SSBOND 2 CYS A 10 CYS A 23 1555 1555 2.03 SSBOND 3 CYS A 17 CYS A 33 1555 1555 2.03 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