Header list of 1mii.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 05-OCT-98 1MII TITLE SOLUTION STRUCTURE OF ALPHA-CONOTOXIN MII COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (ALPHA CONOTOXIN MII); COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.17; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES KEYWDS NEUROTOXIN, NICOTINIC ACETYLCHOLINE RECEPTOR, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.HILL,C.J.OOMEN,L.P.MIRANDA,J.P.BINGHAM,P.F.ALEWOOD,D.J.CRAIK REVDAT 4 23-FEB-22 1MII 1 REMARK LINK REVDAT 3 24-FEB-09 1MII 1 VERSN REVDAT 2 29-DEC-99 1MII 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 21-OCT-98 1MII 0 JRNL AUTH J.M.HILL,C.J.OOMEN,L.P.MIRANDA,J.P.BINGHAM,P.F.ALEWOOD, JRNL AUTH 2 D.J.CRAIK JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN MII JRNL TITL 2 BY NMR SPECTROSCOPY: EFFECTS OF SOLUTION ENVIRONMENT ON JRNL TITL 3 HELICITY. JRNL REF BIOCHEMISTRY V. 37 15621 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9843366 JRNL DOI 10.1021/BI981535W REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.J.SHON,S.C.KOERBER,J.E.RIVIER,B.M.OLIVERA,J.M.MCINTOSH REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF ALPHA-CONOTOXIN MII, REMARK 1 TITL 2 AN ALPHA3BETA2 NEURONAL NICOTINIC ACETYLCHOLINE REMARK 1 TITL 3 RECEPTOR-TARGETED LIGAND REMARK 1 REF BIOCHEMISTRY V. 36 15693 1997 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH G.E.CARTIER,D.YOSHIKAMI,W.R.GRAY,S.LUO,B.M.OLIVERA, REMARK 1 AUTH 2 J.M.MCINTOSH REMARK 1 TITL A NEW ALPHA-CONOTOXIN WHICH TARGETS ALPHA3BETA2 NICOTINIC REMARK 1 TITL 2 ACETYLCHOLINE RECEPTORS REMARK 1 REF J.BIOL.CHEM. V. 271 7522 1996 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 STRUCTURES WERE CALCULATED USING A SIMULATED ANNEALING PROTOCOL REMARK 3 WITH THE REMARK 3 PROGRAM X-PLOR. THESE STRUCTURES WERE THEN ENERGY MINIMIZED USING REMARK 3 1000 CYCLES REMARK 3 OF CONJUGATE GRADIENT MINIMIZATION WITH A REFINED FORCEFIELD BASED REMARK 3 ON THE REMARK 3 PROGRAMM CHARMM REMARK 4 REMARK 4 1MII COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000008359. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 3.9 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; E-COSY; TOCSY; NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX-750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES AND LEAST NUMBER REMARK 210 OF RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 2 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 3 CYS A 3 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 4 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 5 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 6 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 7 CYS A 3 CA - CB - SG ANGL. DEV. = 7.0 DEGREES REMARK 500 8 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 9 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 10 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 11 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 12 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 13 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 14 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 15 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 16 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 17 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 18 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 19 CYS A 3 CA - CB - SG ANGL. DEV. = 7.1 DEGREES REMARK 500 20 CYS A 3 CA - CB - SG ANGL. DEV. = 7.2 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 HIS A 12 65.04 -110.77 REMARK 500 1 ASN A 14 -65.03 -92.27 REMARK 500 2 HIS A 12 64.60 -107.12 REMARK 500 2 ASN A 14 -65.14 -92.27 REMARK 500 3 HIS A 12 64.50 -108.78 REMARK 500 3 ASN A 14 -65.14 -92.24 REMARK 500 4 HIS A 12 64.82 -106.90 REMARK 500 4 ASN A 14 -65.31 -92.20 REMARK 500 5 HIS A 12 64.62 -107.07 REMARK 500 5 ASN A 14 -65.26 -92.10 REMARK 500 6 HIS A 12 64.78 -106.87 REMARK 500 6 ASN A 14 -65.55 -92.21 REMARK 500 7 HIS A 12 64.64 -111.07 REMARK 500 7 ASN A 14 -65.22 -92.10 REMARK 500 8 HIS A 12 64.85 -107.06 REMARK 500 8 ASN A 14 -65.73 -92.07 REMARK 500 9 HIS A 12 64.58 -107.89 REMARK 500 9 ASN A 14 -65.50 -92.11 REMARK 500 10 HIS A 12 64.73 -107.26 REMARK 500 10 ASN A 14 -65.23 -92.16 REMARK 500 11 HIS A 12 64.55 -107.12 REMARK 500 11 ASN A 14 -65.46 -92.08 REMARK 500 12 HIS A 12 64.61 -107.17 REMARK 500 12 ASN A 14 -65.51 -92.15 REMARK 500 13 HIS A 12 64.32 -110.65 REMARK 500 13 ASN A 14 -64.70 -92.15 REMARK 500 14 HIS A 12 64.47 -107.27 REMARK 500 14 ASN A 14 -65.45 -92.22 REMARK 500 15 HIS A 12 64.57 -107.56 REMARK 500 15 ASN A 14 -65.48 -92.12 REMARK 500 16 HIS A 12 64.62 -110.42 REMARK 500 16 ASN A 14 -64.96 -92.17 REMARK 500 17 HIS A 12 64.69 -107.11 REMARK 500 17 ASN A 14 -65.45 -92.08 REMARK 500 18 HIS A 12 64.27 -109.45 REMARK 500 18 ASN A 14 -65.39 -92.17 REMARK 500 19 HIS A 12 64.70 -106.93 REMARK 500 19 ASN A 14 -65.19 -92.20 REMARK 500 20 HIS A 12 64.34 -107.78 REMARK 500 20 ASN A 14 -65.11 -92.19 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 17 DBREF 1MII A 1 16 UNP P56636 CXA2_CONMA 22 37 SEQRES 1 A 17 GLY CYS CYS SER ASN PRO VAL CYS HIS LEU GLU HIS SER SEQRES 2 A 17 ASN LEU CYS NH2 HET NH2 A 17 3 HETNAM NH2 AMINO GROUP FORMUL 1 NH2 H2 N HELIX 1 1 VAL A 7 GLU A 11 1 5 SSBOND 1 CYS A 2 CYS A 8 1555 1555 2.02 SSBOND 2 CYS A 3 CYS A 16 1555 1555 2.02 LINK C CYS A 16 N NH2 A 17 1555 1555 1.30 SITE 1 AC1 2 SER A 13 CYS A 16 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