Header list of 1k64.pdb file
Complete list - 23 20 Bytes
HEADER TOXIN 15-OCT-01 1K64 TITLE NMR STRUCTUE OF ALPHA-CONOTOXIN EI COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-CONOTOXIN EI; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE SOURCE 4 OF THE PEPTIDE IS NATURALLY FOUND IN CONUS ERMINEUS. KEYWDS OMEGA-SHAPED CONTAINING A-HELIX, TOXIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR K.H.PARK,J.E.SUK,R.JACOBSEN,W.R.GRAY,J.M.MCINTOSH,K.H.HAN REVDAT 3 23-FEB-22 1K64 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1K64 1 VERSN REVDAT 1 09-SEP-03 1K64 0 JRNL AUTH K.H.PARK,J.E.SUK,R.JACOBSEN,W.R.GRAY,J.M.MCINTOSH,K.H.HAN JRNL TITL SOLUTION CONFORMATION OF ALPHA-CONOTOXIN EI, A NEUROMUSCULAR JRNL TITL 2 TOXIN SPECIFIC FOR THE ALPHA 1/DELTA SUBUNIT INTERFACE OF JRNL TITL 3 TORPEDO NICOTINIC ACETYLCHOLINE RECEPTOR JRNL REF J.BIOL.CHEM. V. 276 49028 2001 JRNL REFN ISSN 0021-9258 JRNL PMID 11641403 JRNL DOI 10.1074/JBC.M107798200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 5.3B, DISCOVER 2.9.7 REMARK 3 AUTHORS : VARAIN INC. (VNMR), MSI INC. (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1K64 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-01. REMARK 100 THE DEPOSITION ID IS D_1000014607. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 278 REMARK 210 PH : 4.3 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 5MM A-CONOTOXIN EI REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; PE-COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : INOVA; UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : FELIX 95.0., DGII 3.0., CORMA REMARK 210 5.2, MARDIGRAS 3.2. REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MATRIX RELAXATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH REMARK 210 EXPERIMENTAL NOESY SPECTRUM, REMARK 210 STRUCTURES WITH ACCEPTABLE REMARK 210 COVALENT GEOMETRY,STRUCTURES REMARK 210 WITH THE LEAST RESTRAINT REMARK 210 VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10 REMARK 210 REMARK 210 REMARK: TOCSY, COSY, ROESY 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 3 CYS A 5 CA - CB - SG ANGL. DEV. = 9.0 DEGREES REMARK 500 6 CYS A 5 CA - CB - SG ANGL. DEV. = 8.2 DEGREES REMARK 500 7 CYS A 5 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 8 CYS A 4 CA - CB - SG ANGL. DEV. = 8.1 DEGREES REMARK 500 8 CYS A 5 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 12 CYS A 5 CA - CB - SG ANGL. DEV. = 10.4 DEGREES REMARK 500 14 CYS A 10 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 19 CYS A 5 CA - CB - SG ANGL. DEV. = 8.9 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 PRO A 8 -71.74 -24.68 REMARK 500 1 ASN A 14 66.68 -151.47 REMARK 500 2 PRO A 8 -73.18 -28.00 REMARK 500 2 GLN A 16 -35.36 -39.49 REMARK 500 3 THR A 9 -52.82 -29.71 REMARK 500 3 ASN A 14 73.47 -153.62 REMARK 500 3 GLN A 16 -33.00 -38.18 REMARK 500 4 ASP A 2 107.48 -59.38 REMARK 500 4 ASN A 14 73.24 -152.33 REMARK 500 5 ASN A 14 64.14 -151.11 REMARK 500 6 ASN A 14 68.88 -152.40 REMARK 500 7 PRO A 8 -69.13 -28.47 REMARK 500 7 ASN A 14 70.74 -151.38 REMARK 500 7 GLN A 16 -34.81 -39.09 REMARK 500 9 PRO A 8 -75.36 -22.29 REMARK 500 9 ASN A 14 70.87 -152.05 REMARK 500 9 GLN A 16 -39.33 -35.42 REMARK 500 10 PRO A 8 -73.32 -24.63 REMARK 500 10 ASN A 14 71.99 -151.97 REMARK 500 11 ASP A 2 104.86 -47.77 REMARK 500 11 ASN A 14 71.37 -150.36 REMARK 500 11 GLN A 16 -56.70 -28.11 REMARK 500 12 ASP A 2 97.85 -29.75 REMARK 500 12 ASN A 14 71.39 -152.66 REMARK 500 13 ASN A 14 82.95 -150.90 REMARK 500 15 ASP A 2 129.11 -36.10 REMARK 500 15 THR A 9 -52.99 -29.89 REMARK 500 15 ASN A 14 68.79 -150.29 REMARK 500 16 PRO A 8 -54.19 -29.98 REMARK 500 16 THR A 9 -52.99 -29.82 REMARK 500 16 ASN A 14 73.40 -153.03 REMARK 500 16 GLN A 16 -36.10 -39.67 REMARK 500 17 PRO A 8 -70.86 -25.75 REMARK 500 17 ASN A 14 72.02 -151.73 REMARK 500 18 ASN A 14 74.99 -152.52 REMARK 500 18 GLN A 16 -60.92 -20.78 REMARK 500 19 ASP A 2 97.39 -29.95 REMARK 500 19 ASN A 14 69.89 -152.22 REMARK 500 20 ASN A 14 73.22 -152.01 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 10 ASN A 11 5 -146.61 REMARK 500 ILE A 17 CYS A 18 8 -144.74 REMARK 500 CYS A 10 ASN A 11 11 -144.84 REMARK 500 ILE A 17 CYS A 18 12 -149.77 REMARK 500 ARG A 1 ASP A 2 13 136.43 REMARK 500 CYS A 10 ASN A 11 20 -145.70 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 TYR A 6 0.07 SIDE CHAIN REMARK 500 2 ARG A 1 0.10 SIDE CHAIN REMARK 500 3 ARG A 1 0.08 SIDE CHAIN REMARK 500 7 TYR A 6 0.10 SIDE CHAIN REMARK 500 8 TYR A 6 0.10 SIDE CHAIN REMARK 500 9 ARG A 1 0.10 SIDE CHAIN REMARK 500 10 TYR A 6 0.08 SIDE CHAIN REMARK 500 14 TYR A 6 0.09 SIDE CHAIN REMARK 500 15 ARG A 1 0.11 SIDE CHAIN REMARK 500 15 TYR A 6 0.12 SIDE CHAIN REMARK 500 17 TYR A 6 0.08 SIDE CHAIN REMARK 500 19 ARG A 1 0.09 SIDE CHAIN REMARK 500 19 TYR A 6 0.12 SIDE CHAIN REMARK 500 20 TYR A 6 0.11 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 19 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PLP RELATED DB: PDB REMARK 900 1PLP CONTAINS THE CYTOPLASMIC DOMAIN OF PHOSPHOLAMBAN REMARK 900 RELATED ID: 1QS3 RELATED DB: PDB REMARK 900 1QS3 CONTAINS CONFORMATION OF AN ANTITOXIC ANALOG OF ALPHA- REMARK 900 CONOTOXIN GI REMARK 900 RELATED ID: 1DG2 RELATED DB: PDB REMARK 900 1DG2 CONTAINS CONFORMATION OF A-CONOTOXIN AUIB DBREF 1K64 A 1 18 UNP P50982 CXA1_CONER 1 18 SEQADV 1K64 HYP A 3 UNP P50982 PRO 3 MODIFIED RESIDUE SEQRES 1 A 19 ARG ASP HYP CYS CYS TYR HIS PRO THR CYS ASN MET SER SEQRES 2 A 19 ASN PRO GLN ILE CYS NH2 MODRES 1K64 HYP A 3 PRO 4-HYDROXYPROLINE HET HYP A 3 15 HET NH2 A 19 3 HETNAM HYP 4-HYDROXYPROLINE HETNAM NH2 AMINO GROUP HETSYN HYP HYDROXYPROLINE FORMUL 1 HYP C5 H9 N O3 FORMUL 1 NH2 H2 N HELIX 1 1 ASP A 2 TYR A 6 5 5 HELIX 2 2 HIS A 7 SER A 13 1 7 HELIX 3 3 ASN A 14 CYS A 18 5 5 SSBOND 1 CYS A 4 CYS A 10 1555 1555 2.04 SSBOND 2 CYS A 5 CYS A 18 1555 1555 2.04 LINK C ASP A 2 N HYP A 3 1555 1555 1.34 LINK C HYP A 3 N CYS A 4 1555 1555 1.33 LINK C CYS A 18 N NH2 A 19 1555 1555 1.33 SITE 1 AC1 2 PRO A 15 CYS A 18 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 - 23 20 Bytes