Header list of 1txm.pdb file
Complete list - r 2 2 Bytes
HEADER NEUROTOXIN 19-NOV-96 1TXM TITLE SCORPION TOXIN (MAUROTOXIN) FROM SCORPIO MAURUS, NMR, 35 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: MAUROTOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SCORPIO MAURUS; SOURCE 3 ORGANISM_TAXID: 53956; SOURCE 4 ORGAN: TELSON KEYWDS NEUROTOXIN, TOXIN, SCORPION, POTASSIUM CHANNEL BLOCKER, ALPHA BETA KEYWDS 2 SCORPION TOXIN FOLD EXPDTA SOLUTION NMR NUMMDL 35 AUTHOR E.BLANC,J.-M.SABATIER,R.KHARRAT,S.MEUNIER,M.EL AYEB,J.VAN AUTHOR 2 RIETSCHOTEN,H.DARBON REVDAT 3 02-MAR-22 1TXM 1 REMARK LINK REVDAT 2 24-FEB-09 1TXM 1 VERSN REVDAT 1 05-JUN-97 1TXM 0 JRNL AUTH E.BLANC,J.M.SABATIER,R.KHARRAT,S.MEUNIER,M.EL AYEB, JRNL AUTH 2 J.VAN RIETSCHOTEN,H.DARBON JRNL TITL SOLUTION STRUCTURE OF MAUROTOXIN, A SCORPION TOXIN FROM JRNL TITL 2 SCORPIO MAURUS, WITH HIGH AFFINITY FOR VOLTAGE-GATED JRNL TITL 3 POTASSIUM CHANNELS. JRNL REF PROTEINS V. 29 321 1997 JRNL REFN ISSN 0887-3585 JRNL PMID 9365987 JRNL DOI 10.1002/(SICI)1097-0134(199711)29:3<321::AID-PROT6>3.3.CO;2- JRNL DOI 2 K REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DISTANCE GEOMETRY USING DIANA, FOLLOWED REMARK 3 BY AN ENERGY MINIMIZATION USING X-PLOR. REMARK 4 REMARK 4 1TXM 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_1000176878. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 3.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX 500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DIANA, XPLOR REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 35 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 1 CYS A 29 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 2 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 3 CYS A 13 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 4 CYS A 13 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 5 CYS A 13 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 5 CYS A 29 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 6 CYS A 13 CA - CB - SG ANGL. DEV. = 7.7 DEGREES REMARK 500 7 CYS A 13 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 8 CYS A 9 CA - CB - SG ANGL. DEV. = 13.5 DEGREES REMARK 500 8 CYS A 13 CA - CB - SG ANGL. DEV. = 7.9 DEGREES REMARK 500 8 TYR A 32 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 9 CYS A 13 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 9 CYS A 29 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 9 CYS A 31 CA - CB - SG ANGL. DEV. = 10.6 DEGREES REMARK 500 10 CYS A 13 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 10 CYS A 34 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 11 CYS A 13 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 11 CYS A 29 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 11 CYS A 31 CA - CB - SG ANGL. DEV. = 9.1 DEGREES REMARK 500 11 CYS A 34 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 12 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 13 CYS A 29 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 14 CYS A 13 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 14 CYS A 29 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 15 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 16 CYS A 13 CA - CB - SG ANGL. DEV. = 9.1 DEGREES REMARK 500 17 CYS A 9 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 17 CYS A 13 CA - CB - SG ANGL. DEV. = 8.6 DEGREES REMARK 500 17 CYS A 31 CA - CB - SG ANGL. DEV. = 7.5 DEGREES REMARK 500 17 CYS A 34 CA - CB - SG ANGL. DEV. = 9.7 DEGREES REMARK 500 18 CYS A 13 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 19 CYS A 13 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 20 CYS A 13 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 20 CYS A 29 CA - CB - SG ANGL. DEV. = 6.7 DEGREES REMARK 500 21 CYS A 13 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 21 CYS A 31 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 21 CYS A 34 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 22 CYS A 9 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 22 CYS A 13 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 22 CYS A 31 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 22 CYS A 34 CA - CB - SG ANGL. DEV. = 9.3 DEGREES REMARK 500 23 CYS A 13 CA - CB - SG ANGL. DEV. = 7.3 DEGREES REMARK 500 23 CYS A 29 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 24 CYS A 13 CA - CB - SG ANGL. DEV. = 8.7 DEGREES REMARK 500 24 CYS A 31 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 24 TYR A 32 N - CA - CB ANGL. DEV. = -12.9 DEGREES REMARK 500 24 CYS A 34 CA - CB - SG ANGL. DEV. = 8.3 DEGREES REMARK 500 25 CYS A 9 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 25 CYS A 13 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 75 ANGLE DEVIATIONS. 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 SER A 2 125.59 -38.87 REMARK 500 1 THR A 17 -51.69 -128.50 REMARK 500 1 TYR A 32 -77.71 -112.67 REMARK 500 2 SER A 2 121.06 -39.09 REMARK 500 2 THR A 17 -53.89 -124.08 REMARK 500 2 PRO A 20 -63.21 -90.35 REMARK 500 2 TYR A 32 -83.19 -109.48 REMARK 500 3 SER A 2 120.96 -39.37 REMARK 500 3 CYS A 3 -169.59 -120.76 REMARK 500 3 THR A 17 -51.34 -130.67 REMARK 500 3 PRO A 20 -71.63 -58.43 REMARK 500 3 TYR A 32 -89.37 -104.84 REMARK 500 4 SER A 2 117.07 -39.28 REMARK 500 4 THR A 17 -53.27 -127.76 REMARK 500 4 ASN A 26 11.48 -69.65 REMARK 500 4 TYR A 32 -79.49 -99.50 REMARK 500 5 SER A 2 122.89 -39.19 REMARK 500 5 THR A 17 -53.36 -132.03 REMARK 500 5 TYR A 32 -79.95 -106.54 REMARK 500 6 SER A 2 126.95 -39.25 REMARK 500 6 THR A 17 -52.32 -129.58 REMARK 500 6 TYR A 32 -77.19 -110.38 REMARK 500 7 SER A 2 100.48 -39.01 REMARK 500 7 THR A 17 -52.06 -129.79 REMARK 500 7 ASN A 26 38.30 -79.92 REMARK 500 7 LYS A 27 -51.08 -138.03 REMARK 500 7 TYR A 32 -79.46 -107.44 REMARK 500 8 SER A 2 127.32 -39.08 REMARK 500 8 THR A 17 -51.21 -132.62 REMARK 500 8 ASN A 26 6.93 -69.54 REMARK 500 8 TYR A 32 -74.33 -113.37 REMARK 500 9 SER A 2 117.02 -38.98 REMARK 500 9 THR A 17 -44.68 -142.70 REMARK 500 9 TYR A 32 -88.23 -110.55 REMARK 500 10 THR A 17 -52.30 -134.61 REMARK 500 10 PRO A 20 -71.10 -56.00 REMARK 500 10 ASN A 26 21.54 -73.61 REMARK 500 10 TYR A 32 -74.66 -98.99 REMARK 500 11 SER A 2 131.59 -39.14 REMARK 500 11 THR A 17 -52.72 -128.58 REMARK 500 11 PRO A 20 -68.42 -97.77 REMARK 500 11 ASN A 21 74.46 -119.13 REMARK 500 11 TYR A 32 -69.11 -92.14 REMARK 500 12 SER A 2 118.72 -38.89 REMARK 500 12 THR A 17 -54.99 -121.78 REMARK 500 12 ASN A 26 6.30 -69.88 REMARK 500 12 TYR A 32 -85.56 -110.17 REMARK 500 13 SER A 2 125.12 -39.13 REMARK 500 13 THR A 17 -51.65 -129.86 REMARK 500 13 TYR A 32 -77.83 -111.61 REMARK 500 REMARK 500 THIS ENTRY HAS 143 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 14 0.31 SIDE CHAIN REMARK 500 2 ARG A 14 0.31 SIDE CHAIN REMARK 500 3 ARG A 14 0.32 SIDE CHAIN REMARK 500 4 ARG A 14 0.31 SIDE CHAIN REMARK 500 5 ARG A 14 0.31 SIDE CHAIN REMARK 500 6 ARG A 14 0.31 SIDE CHAIN REMARK 500 7 ARG A 14 0.32 SIDE CHAIN REMARK 500 8 ARG A 14 0.31 SIDE CHAIN REMARK 500 9 ARG A 14 0.31 SIDE CHAIN REMARK 500 10 ARG A 14 0.31 SIDE CHAIN REMARK 500 11 ARG A 14 0.31 SIDE CHAIN REMARK 500 12 ARG A 14 0.32 SIDE CHAIN REMARK 500 13 ARG A 14 0.31 SIDE CHAIN REMARK 500 14 ARG A 14 0.31 SIDE CHAIN REMARK 500 15 ARG A 14 0.31 SIDE CHAIN REMARK 500 16 ARG A 14 0.31 SIDE CHAIN REMARK 500 17 ARG A 14 0.31 SIDE CHAIN REMARK 500 18 ARG A 14 0.31 SIDE CHAIN REMARK 500 19 ARG A 14 0.31 SIDE CHAIN REMARK 500 20 ARG A 14 0.31 SIDE CHAIN REMARK 500 21 ARG A 14 0.31 SIDE CHAIN REMARK 500 22 ARG A 14 0.31 SIDE CHAIN REMARK 500 23 ARG A 14 0.31 SIDE CHAIN REMARK 500 24 ARG A 14 0.31 SIDE CHAIN REMARK 500 25 ARG A 14 0.31 SIDE CHAIN REMARK 500 26 ARG A 14 0.31 SIDE CHAIN REMARK 500 27 ARG A 14 0.31 SIDE CHAIN REMARK 500 28 ARG A 14 0.32 SIDE CHAIN REMARK 500 29 ARG A 14 0.32 SIDE CHAIN REMARK 500 30 ARG A 14 0.29 SIDE CHAIN REMARK 500 31 ARG A 14 0.31 SIDE CHAIN REMARK 500 32 ARG A 14 0.31 SIDE CHAIN REMARK 500 33 ARG A 14 0.31 SIDE CHAIN REMARK 500 34 ARG A 14 0.31 SIDE CHAIN REMARK 500 35 ARG A 14 0.31 SIDE CHAIN 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 35 DBREF 1TXM A 1 34 UNP P80719 SCXM_SCOMA 1 34 SEQRES 1 A 35 VAL SER CYS THR GLY SER LYS ASP CYS TYR ALA PRO CYS SEQRES 2 A 35 ARG LYS GLN THR GLY CYS PRO ASN ALA LYS CYS ILE ASN SEQRES 3 A 35 LYS SER CYS LYS CYS TYR GLY CYS NH2 HET NH2 A 35 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 H1 SER A 6 GLN A 16 1ALPHA KINK AT POSITION 10 11 SHEET 1 A 2 LYS A 23 CYS A 24 0 SHEET 2 A 2 CYS A 29 LYS A 30 -1 N LYS A 30 O LYS A 23 SSBOND 1 CYS A 3 CYS A 24 1555 1555 2.02 SSBOND 2 CYS A 9 CYS A 29 1555 1555 2.02 SSBOND 3 CYS A 13 CYS A 19 1555 1555 2.02 SSBOND 4 CYS A 31 CYS A 34 1555 1555 2.02 LINK C CYS A 34 N NH2 A 35 1555 1555 1.31 SITE 1 AC1 2 GLY A 33 CYS A 34 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