Header list of 2ktx.pdb file
Complete list - 20 20 Bytes
HEADER NEUROTOXIN 27-FEB-97 2KTX TITLE COMPLETE KALIOTOXIN FROM ANDROCTONUS MAURETANICUS MAURETANICUS, NMR, TITLE 2 18 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: KALIOTOXIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ANDROCTONUS MAURETANICUS MAURETANICUS; SOURCE 3 ORGANISM_TAXID: 6860; SOURCE 4 STRAIN: MAURETANICUS KEYWDS NEUROTOXIN, POTASSIUM CHANNEL INHIBITOR EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR M.GAIRI,R.ROMI,I.FERNANDEZ,H.ROCHAT,M.-F.MARTIN-EAUCLAIRE,J.VAN AUTHOR 2 RIETSCHTOTEN,M.PONS,E.GIRALT REVDAT 3 20-DEC-17 2KTX 1 JRNL REMARK REVDAT 2 24-FEB-09 2KTX 1 VERSN REVDAT 1 16-JUN-97 2KTX 0 JRNL AUTH M.GAIRI,R.ROMI,I.FERNANDEZ,H.ROCHAT,M.F.MARTIN-EAUCLAIRE, JRNL AUTH 2 J.VAN RIETSCHOTEN,M.PONS,E.GIRALT JRNL TITL 3D STRUCTURE OF KALIOTOXIN: IS RESIDUE 34 A KEY FOR CHANNEL JRNL TITL 2 SELECTIVITY? JRNL REF J.PEPT.SCI. V. 3 314 1997 JRNL REFN ISSN 1075-2617 JRNL PMID 9262650 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.CREST,G.JACQUET,M.GOLA,H.ZERROUK,A.BENSLIMANE,H.ROCHAT, REMARK 1 AUTH 2 P.MANSUELLE,M.F.MARTIN-EAUCLAIRE REMARK 1 TITL KALIOTOXIN, A NOVEL PEPTIDYL INHIBITOR OF NEURONAL BK-TYPE REMARK 1 TITL 2 CA(2+)-ACTIVATED K+ CHANNELS CHARACTERIZED FROM ANDROCTONUS REMARK 1 TITL 3 MAURETANICUS MAURETANICUS VENOM REMARK 1 REF J.BIOL.CHEM. V. 267 1640 1992 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER REMARK 3 AUTHORS : BIOSYM REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: DGII ALSO WAS USED. REFINEMENT DETAILS REMARK 3 CAN BE FOUND IN THE JRNL CITATION ABOVE. REMARK 4 REMARK 4 2KTX 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_1000178288. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 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 : NOESY; TOCSY; DQF-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE DMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DGII, DISCOVER REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 35 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL ENERGY/DISTANCE VIOLATIONS 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: 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 H VAL A 6 H LYS A 7 1.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 1 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 1 LYS A 38 C LYS A 38 OXT 0.142 REMARK 500 2 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 2 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 3 GLU A 3 CD GLU A 3 OE2 0.119 REMARK 500 3 LYS A 38 C LYS A 38 OXT 0.140 REMARK 500 4 GLU A 3 CD GLU A 3 OE2 0.117 REMARK 500 4 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 5 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 5 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 6 GLU A 3 CD GLU A 3 OE2 0.117 REMARK 500 6 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 7 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 7 LYS A 38 C LYS A 38 OXT 0.140 REMARK 500 8 GLU A 3 CD GLU A 3 OE2 0.117 REMARK 500 8 LYS A 38 C LYS A 38 OXT 0.142 REMARK 500 9 GLU A 3 CD GLU A 3 OE2 0.117 REMARK 500 9 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 10 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 10 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 11 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 11 LYS A 38 C LYS A 38 OXT 0.142 REMARK 500 12 GLU A 3 CD GLU A 3 OE2 0.117 REMARK 500 12 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 13 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 13 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 14 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 14 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 15 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 15 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 16 GLU A 3 CD GLU A 3 OE2 0.119 REMARK 500 16 LYS A 38 C LYS A 38 OXT 0.140 REMARK 500 17 GLU A 3 CD GLU A 3 OE2 0.119 REMARK 500 17 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 18 GLU A 3 CD GLU A 3 OE2 0.118 REMARK 500 18 LYS A 38 C LYS A 38 OXT 0.141 REMARK 500 REMARK 500 REMARK: NULL 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 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES REMARK 500 2 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 2 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 3 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 3 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 4 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 4 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 5 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 5 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 6 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 6 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 7 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 7 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 8 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 8 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 9 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 9 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES REMARK 500 10 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 10 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES REMARK 500 11 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 11 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES REMARK 500 12 ASP A 20 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 12 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 12 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 13 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 13 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES REMARK 500 14 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 14 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 15 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 15 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES REMARK 500 16 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 16 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 17 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 17 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 18 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 18 HIS A 34 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 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 2 79.23 63.91 REMARK 500 1 GLU A 3 91.73 54.18 REMARK 500 1 VAL A 6 -9.86 -143.27 REMARK 500 1 LYS A 7 99.88 58.36 REMARK 500 1 SER A 9 10.68 -143.44 REMARK 500 1 ARG A 24 -117.03 -86.45 REMARK 500 1 LYS A 27 115.71 -165.77 REMARK 500 2 ASN A 5 58.44 -92.83 REMARK 500 2 ARG A 24 -122.91 -76.44 REMARK 500 3 SER A 9 18.44 -144.02 REMARK 500 3 ARG A 24 -118.28 -81.42 REMARK 500 4 ARG A 24 -115.66 -95.09 REMARK 500 5 VAL A 2 52.64 -103.33 REMARK 500 5 ALA A 21 44.60 -150.81 REMARK 500 5 ARG A 24 -125.27 -80.40 REMARK 500 6 ARG A 24 -117.88 -89.55 REMARK 500 7 VAL A 2 64.84 63.86 REMARK 500 7 GLU A 3 119.91 66.07 REMARK 500 7 ARG A 24 -115.36 -78.13 REMARK 500 7 CYS A 35 -151.80 -142.57 REMARK 500 8 ARG A 24 -119.60 -75.92 REMARK 500 9 ALA A 21 25.35 -147.53 REMARK 500 9 ARG A 24 -114.21 -83.79 REMARK 500 10 SER A 9 11.92 -142.54 REMARK 500 10 ALA A 21 38.22 -150.93 REMARK 500 10 ARG A 24 -122.53 -84.90 REMARK 500 11 ALA A 21 35.70 -151.01 REMARK 500 11 ARG A 24 -124.87 -94.35 REMARK 500 12 ALA A 21 43.27 -150.76 REMARK 500 12 ARG A 24 -125.07 -76.46 REMARK 500 13 VAL A 2 75.87 62.06 REMARK 500 13 GLU A 3 102.41 59.31 REMARK 500 13 ASN A 5 32.32 -96.47 REMARK 500 13 PHE A 25 133.93 57.51 REMARK 500 14 SER A 9 12.20 -141.63 REMARK 500 14 ALA A 21 41.55 -152.30 REMARK 500 14 ARG A 24 -120.11 -80.58 REMARK 500 15 VAL A 2 77.37 61.13 REMARK 500 15 GLU A 3 80.05 59.80 REMARK 500 15 LEU A 15 -70.75 -42.48 REMARK 500 15 ARG A 24 -117.87 -74.57 REMARK 500 15 CYS A 35 -155.21 -76.17 REMARK 500 16 ARG A 24 -114.34 -85.71 REMARK 500 16 CYS A 35 -159.24 -141.64 REMARK 500 17 ARG A 24 -122.80 -84.77 REMARK 500 18 SER A 9 16.49 -143.87 REMARK 500 18 SER A 11 -49.40 -166.61 REMARK 500 18 ARG A 24 -119.70 -86.81 REMARK 500 REMARK 500 REMARK: NULL DBREF 2KTX A 1 38 UNP P24662 SCK1_ANDMA 1 38 SEQRES 1 A 38 GLY VAL GLU ILE ASN VAL LYS CYS SER GLY SER PRO GLN SEQRES 2 A 38 CYS LEU LYS PRO CYS LYS ASP ALA GLY MET ARG PHE GLY SEQRES 3 A 38 LYS CYS MET ASN ARG LYS CYS HIS CYS THR PRO LYS HELIX 1 1 SER A 11 ALA A 21 1 11 SHEET 1 A 3 GLY A 26 MET A 29 0 SHEET 2 A 3 LYS A 32 CYS A 35 -1 N HIS A 34 O LYS A 27 SHEET 3 A 3 VAL A 2 ILE A 4 -1 N ILE A 4 O CYS A 33 SHEET 1 B 3 GLY A 26 MET A 29 0 SHEET 2 B 3 LYS A 32 CYS A 35 -1 N HIS A 34 O LYS A 27 SHEET 3 B 3 VAL A 6 CYS A 8 -1 O VAL A 6 N CYS A 33 SSBOND 1 CYS A 8 CYS A 28 1555 1555 1.99 SSBOND 2 CYS A 14 CYS A 33 1555 1555 1.99 SSBOND 3 CYS A 18 CYS A 35 1555 1555 2.01 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 - 20 20 Bytes