Header list of 1cmr.pdb file
Complete list - 3 20 Bytes
HEADER CURAREMIMETIC PROTEIN 15-MAR-96 1CMR
TITLE NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING
TITLE 2 A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD
TITLE 3 (PH 3.5, 20C), NMR, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHARYBDOTOXIN, ALPHA CHIMERA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: FIRST 6 RESIDUES OF CHARYBDOTOXIN NOT INCLUDED
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE CHIMERA WAS PREPARED BY SOLID PHASE SYNTHESIS
KEYWDS ANTAGONIST OF NICOTINIC ACETYLCHOLINE RECEPTOR, CURAREMIMETIC PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.ZINN-JUSTIN,M.GUENNEUGUES,E.DRAKOPOULOU,B.GILQUIN,C.VITA,A.MENEZ
REVDAT 4 03-NOV-21 1CMR 1 SEQADV
REVDAT 3 29-NOV-17 1CMR 1 REMARK HELIX
REVDAT 2 24-FEB-09 1CMR 1 VERSN
REVDAT 1 01-AUG-96 1CMR 0
JRNL AUTH S.ZINN-JUSTIN,M.GUENNEUGUES,E.DRAKOPOULOU,B.GILQUIN,C.VITA,
JRNL AUTH 2 A.MENEZ
JRNL TITL TRANSFER OF A BETA-HAIRPIN FROM THE FUNCTIONAL SITE OF SNAKE
JRNL TITL 2 CURAREMIMETIC TOXINS TO THE ALPHA/BETA SCAFFOLD OF SCORPION
JRNL TITL 3 TOXINS: THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CHIMERIC
JRNL TITL 4 PROTEIN.
JRNL REF BIOCHEMISTRY V. 35 8535 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8679614
JRNL DOI 10.1021/BI960466N
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.DRAKOPOULOU,S.ZINN-JUSTIN,M.GUENNEUGUES,B.GILQUIN,C.VITA,
REMARK 1 AUTH 2 A.MENEZ
REMARK 1 TITL CHANGING THE STRUCTURAL CONTEXT OF A FUNCTIONAL
REMARK 1 TITL 2 BETA-HAIRPIN. SYNTHESIS AND CHARACTERIZATION OF A CHIMERA
REMARK 1 TITL 3 CONTAINING THE CURAREMIMETIC LOOP OF A SNAKE TOXIN IN THE
REMARK 1 TITL 4 SCORPION ALPHA/BETA SCAFFOLD
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
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: NULL
REMARK 4
REMARK 4 1CMR 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_1000172397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
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: 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 THR A 2 -63.10 -105.55
REMARK 500 1 THR A 3 -150.71 -139.18
REMARK 500 1 VAL A 10 -52.02 -142.88
REMARK 500 1 HIS A 15 -124.95 -106.88
REMARK 500 1 ASN A 16 37.96 -154.17
REMARK 500 1 THR A 17 -165.15 -112.18
REMARK 500 1 SER A 18 -105.36 -125.88
REMARK 500 2 THR A 2 31.98 -157.54
REMARK 500 2 THR A 3 -116.97 -111.47
REMARK 500 2 SER A 4 -48.77 -160.91
REMARK 500 2 LYS A 5 47.26 -91.85
REMARK 500 2 CYS A 7 24.97 -147.73
REMARK 500 2 ASN A 16 31.10 79.14
REMARK 500 2 THR A 17 -160.91 -110.80
REMARK 500 2 SER A 18 -112.55 -108.85
REMARK 500 2 ASP A 23 -83.69 -107.72
REMARK 500 2 HIS A 24 -48.62 -149.19
REMARK 500 3 HIS A 15 -91.36 -98.55
REMARK 500 3 ASN A 16 -59.59 -149.48
REMARK 500 3 ASP A 23 -90.00 -100.94
REMARK 500 3 HIS A 24 -47.99 -142.80
REMARK 500 3 GLU A 30 -165.79 -116.74
REMARK 500 4 VAL A 10 -53.10 -140.62
REMARK 500 4 HIS A 15 -118.61 -105.44
REMARK 500 4 ASN A 16 42.45 -163.98
REMARK 500 4 SER A 18 -105.83 -118.39
REMARK 500 5 THR A 2 -30.08 -144.83
REMARK 500 5 VAL A 10 -50.84 -139.06
REMARK 500 5 LEU A 14 -62.37 -99.54
REMARK 500 5 HIS A 15 -91.70 -97.69
REMARK 500 5 ASN A 16 -60.20 -148.27
REMARK 500 5 ASP A 23 -87.52 -99.52
REMARK 500 5 HIS A 24 -49.36 -141.88
REMARK 500 6 THR A 3 -78.36 -123.07
REMARK 500 6 SER A 4 -40.49 -177.38
REMARK 500 6 SER A 9 46.19 73.76
REMARK 500 6 HIS A 15 -90.55 -100.10
REMARK 500 6 ASN A 16 -53.22 -162.53
REMARK 500 7 THR A 2 -29.64 -145.36
REMARK 500 7 SER A 9 44.88 73.28
REMARK 500 7 HIS A 15 -112.23 -108.06
REMARK 500 7 ASN A 16 48.67 -167.12
REMARK 500 7 THR A 17 -152.44 -111.12
REMARK 500 7 SER A 18 -91.44 -147.04
REMARK 500 7 ASP A 23 -89.18 -101.28
REMARK 500 7 HIS A 24 -48.14 -153.75
REMARK 500 8 THR A 2 -39.87 -142.49
REMARK 500 8 HIS A 15 -93.34 -99.13
REMARK 500 8 ASN A 16 -57.42 -159.94
REMARK 500 8 ASP A 23 -88.34 -98.73
REMARK 500
REMARK 500 THIS ENTRY HAS 121 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CMR A 1 31 UNP P13487 SCKA_LEIQH 7 37
SEQADV 1CMR LYS A 19 UNP P13487 ARG 25 ENGINEERED MUTATION
SEQADV 1CMR TRP A 21 UNP P13487 LYS 27 ENGINEERED MUTATION
SEQADV 1CMR ASP A 23 UNP P13487 MET 29 ENGINEERED MUTATION
SEQADV 1CMR HIS A 24 UNP P13487 ASN 30 ENGINEERED MUTATION
SEQADV 1CMR ARG A 25 UNP P13487 LYS 31 ENGINEERED MUTATION
SEQADV 1CMR GLY A 26 UNP P13487 LYS 32 ENGINEERED MUTATION
SEQADV 1CMR ILE A 28 UNP P13487 ARG 34 ENGINEERED MUTATION
SEQADV 1CMR GLU A 30 UNP P13487 TYR 36 ENGINEERED MUTATION
SEQRES 1 A 31 CYS THR THR SER LYS GLU CYS TRP SER VAL CYS GLN ARG
SEQRES 2 A 31 LEU HIS ASN THR SER LYS GLY TRP CYS ASP HIS ARG GLY
SEQRES 3 A 31 CYS ILE CYS GLU SER
HELIX 1 H1 LYS A 5 CYS A 7 5 3
HELIX 2 H2 VAL A 10 LEU A 14 1 5
SHEET 1 S1 2 LYS A 19 ASP A 23 0
SHEET 2 S1 2 GLY A 26 GLU A 30 -1
SSBOND 1 CYS A 1 CYS A 22 1555 1555 2.02
SSBOND 2 CYS A 7 CYS A 27 1555 1555 2.03
SSBOND 3 CYS A 11 CYS A 29 1555 1555 2.03
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 - 3 20 Bytes