Header list of 1b45.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 05-JAN-99 1B45 TITLE ALPHA-CNIA CONOTOXIN FROM CONUS CONSORS, NMR, 43 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-CNIA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CONUS CONSORS; SOURCE 3 ORGANISM_TAXID: 101297 KEYWDS ALPHA-CONOTOXIN, CONUS CONSORS, NICOTINIC ACETYLCHOLINE RECEPTOR, KEYWDS 2 TOXIN EXPDTA SOLUTION NMR NUMMDL 43 AUTHOR P.FAVREAU,I.KRIMM,F.LE GALL,M.J.BOBENRIETH,H.LAMTHANH,F.BOUET, AUTHOR 2 D.SERVENT,J.MOLGO,A.MENEZ,Y.LETOURNEUX,J.M.LANCELIN REVDAT 3 16-FEB-22 1B45 1 REMARK LINK REVDAT 2 24-FEB-09 1B45 1 VERSN REVDAT 1 09-JUL-99 1B45 0 JRNL AUTH P.FAVREAU,I.KRIMM,F.LE GALL,M.J.BOBENRIETH,H.LAMTHANH, JRNL AUTH 2 F.BOUET,D.SERVENT,J.MOLGO,A.MENEZ,Y.LETOURNEUX,J.M.LANCELIN JRNL TITL BIOCHEMICAL CHARACTERIZATION AND NUCLEAR MAGNETIC RESONANCE JRNL TITL 2 STRUCTURE OF NOVEL ALPHA-CONOTOXINS ISOLATED FROM THE VENOM JRNL TITL 3 OF CONUS CONSORS. JRNL REF BIOCHEMISTRY V. 38 6317 1999 JRNL REFN ISSN 0006-2960 JRNL PMID 10320362 JRNL DOI 10.1021/BI982817Z REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 80 STRUCTURES WERE GENERATED REMARK 3 STARTING FROM RANDOM COORDINATES BY A HIGH TEMPERATURE SIMULATED REMARK 3 ANNEALING PROTOCOL AT 1000K (NILGES ET AL., 1988), USING THE REMARK 3 PARALLHDG.PRO FORCE FIELD OF X-PLOR THAT DO NO TAKE INTO ACCOUNT REMARK 3 THE ATTRACTIVE TERM OF THE VAN DER WALLS' INTERACTIONS NOR THE REMARK 3 ELECTROSTATIC INTERACTIONS. THE STRUCTURES THAT AGREED WITH THE REMARK 3 FORCE FIELD AND EXPERIMENTAL RESTRAINTS (NO NOE VIOLATION GRATER REMARK 3 THAN 0.2 A) WERE FURTHER REFINED, USING THE FULL CHARMM22 FORCE REMARK 3 FIELD OF X-PLOR. AN APPROXIMATE SOLVENT ELECTROSTATIC SCREENING REMARK 3 EFFECT WAS INTRODUCED BY USING A DISTANCE-DEPENDENT DIELECTRIC REMARK 3 CONSTANT AND BY REDUCING THE ELECTRIC CHARGES OF THE FORMALLY REMARK 3 CHARGED AMINO ACID SIDE CHAINS (ARG, LYS AND HIS) AND THE N- REMARK 3 TERMINUS TO 20% OF THEIR NOMINAL CHARGES DEFINED IN THE CHARMM22 REMARK 3 FORCE FIELD. AFTER 1500 STEPS OF CONJUGATE GRADIENT ENERGY REMARK 3 MINIMIZATION, THE DYNAMIC WAS INITIATED AT 750 K, EQUILIBRATED REMARK 3 FOR 0.5 PS WITH 1 FS INTEGRATION STEPS, THEN COUPLED TO A HEAT REMARK 3 BATH AT 750 K AND THE MOLECULE WAS ALLOWED TO EVOLVE FOR 10 PS REMARK 3 BEFORE BEING COOLED SLOWLY TO 300 K ON A PERIOD OF 5.4 PS AND REMARK 3 ALLOWED TO EVOLVE AGAIN AT THIS TEMPERATURE FOR 15 PS. AT THE REMARK 3 END, STRUCTURES WERE ENERGY MINIMIZED BY 1500 STEPS OF THE REMARK 3 CONJUGATE GRADIENT ALGORITHM. THE FORCE CONSTANT USED FOR THE REMARK 3 NOE POTENTIAL IN BOTH STEPS WAS 50 KCAL MOL-1 A-2. REMARK 4 REMARK 4 1B45 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_1000171467. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 4.1 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90%WATER/ 10%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE DRX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : HIGH TEMPERATURE SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 43 REMARK 210 CONFORMERS, SELECTION CRITERIA : POTENTIAL ENERGIES 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 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 4 CYS A 3 N - CA - C ANGL. DEV. = -16.5 DEGREES REMARK 500 8 TYR A 11 N - CA - C ANGL. DEV. = -19.2 DEGREES REMARK 500 9 TYR A 11 N - CA - C ANGL. DEV. = -21.0 DEGREES REMARK 500 9 TYR A 12 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 9 TYR A 12 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES REMARK 500 12 TYR A 11 N - CA - C ANGL. DEV. = -20.7 DEGREES REMARK 500 13 GLY A 9 N - CA - C ANGL. DEV. = -15.7 DEGREES REMARK 500 14 GLY A 9 N - CA - C ANGL. DEV. = -15.4 DEGREES REMARK 500 14 TYR A 11 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 19 GLY A 9 N - CA - C ANGL. DEV. = -16.2 DEGREES REMARK 500 20 GLY A 9 N - CA - C ANGL. DEV. = -16.0 DEGREES REMARK 500 22 GLY A 9 N - CA - C ANGL. DEV. = -17.3 DEGREES REMARK 500 22 TYR A 11 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 23 GLY A 9 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 24 GLY A 9 N - CA - C ANGL. DEV. = -17.4 DEGREES REMARK 500 28 TYR A 11 N - CA - C ANGL. DEV. = -18.7 DEGREES REMARK 500 31 CYS A 8 N - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 32 GLY A 9 N - CA - C ANGL. DEV. = -16.7 DEGREES REMARK 500 32 TYR A 11 N - CA - C ANGL. DEV. = -19.7 DEGREES REMARK 500 33 GLY A 9 N - CA - C ANGL. DEV. = -15.8 DEGREES REMARK 500 35 CYS A 8 N - CA - C ANGL. DEV. = -16.5 DEGREES REMARK 500 36 TYR A 11 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 37 TYR A 11 N - CA - C ANGL. DEV. = -19.8 DEGREES REMARK 500 38 TYR A 11 N - CA - C ANGL. DEV. = -19.8 DEGREES REMARK 500 40 GLY A 9 N - CA - C ANGL. DEV. = -15.1 DEGREES REMARK 500 40 TYR A 11 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 43 TYR A 11 N - CA - C ANGL. DEV. = -18.2 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 CYS A 4 55.71 -154.59 REMARK 500 2 SER A 13 104.45 -168.03 REMARK 500 3 LYS A 10 37.73 -89.41 REMARK 500 3 SER A 13 -138.74 -145.20 REMARK 500 4 CYS A 4 51.37 -145.92 REMARK 500 5 CYS A 4 73.22 -160.07 REMARK 500 7 CYS A 4 61.42 -159.96 REMARK 500 8 TYR A 12 -179.47 -173.22 REMARK 500 9 ALA A 7 48.07 -86.80 REMARK 500 9 CYS A 8 -85.07 -120.62 REMARK 500 9 LYS A 10 42.43 -102.26 REMARK 500 10 SER A 13 -139.81 -147.27 REMARK 500 12 CYS A 8 -82.51 -126.20 REMARK 500 13 CYS A 4 83.60 -163.48 REMARK 500 13 ALA A 7 70.89 -102.30 REMARK 500 13 CYS A 8 -67.96 -107.45 REMARK 500 13 LYS A 10 35.51 -83.85 REMARK 500 14 CYS A 8 -73.04 -121.88 REMARK 500 15 CYS A 4 81.68 -156.56 REMARK 500 15 TYR A 11 65.43 -112.50 REMARK 500 16 CYS A 8 -67.18 -140.64 REMARK 500 18 CYS A 4 26.59 -140.20 REMARK 500 18 ALA A 7 -54.26 -153.00 REMARK 500 19 CYS A 4 94.86 -165.96 REMARK 500 19 ALA A 7 38.95 -92.41 REMARK 500 19 CYS A 8 -63.49 -96.26 REMARK 500 19 LYS A 10 46.24 -91.99 REMARK 500 20 ALA A 7 53.87 -90.22 REMARK 500 20 CYS A 8 -88.60 -106.77 REMARK 500 21 TYR A 11 16.67 80.90 REMARK 500 22 CYS A 4 92.69 -164.35 REMARK 500 23 CYS A 8 -92.33 -121.94 REMARK 500 24 CYS A 4 93.25 -161.19 REMARK 500 24 CYS A 8 -92.47 -113.62 REMARK 500 24 LYS A 10 47.92 -84.26 REMARK 500 25 CYS A 8 41.36 -97.71 REMARK 500 26 CYS A 4 52.95 -152.71 REMARK 500 26 TYR A 11 55.23 -112.52 REMARK 500 27 CYS A 4 51.38 -145.05 REMARK 500 27 CYS A 8 -65.80 -148.27 REMARK 500 27 SER A 13 -153.18 -152.76 REMARK 500 28 CYS A 4 73.25 -156.42 REMARK 500 29 CYS A 4 42.08 -162.54 REMARK 500 29 LYS A 10 -69.39 79.22 REMARK 500 29 TYR A 12 95.23 -65.92 REMARK 500 31 CYS A 4 68.28 -114.58 REMARK 500 31 PRO A 6 32.97 -73.80 REMARK 500 31 LYS A 10 -123.22 74.12 REMARK 500 32 TYR A 12 -177.21 -175.37 REMARK 500 33 CYS A 3 69.27 -117.00 REMARK 500 REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 CYS A 3 CYS A 4 6 -147.58 REMARK 500 TYR A 12 SER A 13 18 -147.64 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 4 TYR A 12 0.06 SIDE CHAIN REMARK 500 8 TYR A 12 0.09 SIDE CHAIN REMARK 500 13 TYR A 12 0.06 SIDE CHAIN REMARK 500 14 TYR A 12 0.09 SIDE CHAIN REMARK 500 17 TYR A 12 0.09 SIDE CHAIN REMARK 500 21 TYR A 12 0.08 SIDE CHAIN REMARK 500 23 TYR A 12 0.08 SIDE CHAIN REMARK 500 31 TYR A 12 0.10 SIDE CHAIN REMARK 500 32 TYR A 12 0.08 SIDE CHAIN REMARK 500 36 TYR A 12 0.07 SIDE CHAIN REMARK 500 37 TYR A 12 0.08 SIDE CHAIN REMARK 500 38 TYR A 12 0.09 SIDE CHAIN REMARK 500 41 TYR A 12 0.07 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 15 DBREF 1B45 A 1 14 UNP P56973 CXA1_CONCN 1 14 SEQRES 1 A 15 GLY ARG CYS CYS HIS PRO ALA CYS GLY LYS TYR TYR SER SEQRES 2 A 15 CYS NH2 HET NH2 A 15 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 PRO A 6 CYS A 8 5 3 SSBOND 1 CYS A 3 CYS A 8 1555 1555 2.02 SSBOND 2 CYS A 4 CYS A 14 1555 1555 2.03 LINK C CYS A 14 N NH2 A 15 1555 1555 1.36 SITE 1 AC1 1 CYS 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 - 16 20 Bytes