Header list of 1xbh.pdb file
Complete list - 2 20 Bytes
HEADER BETA-HAIRPIN 17-FEB-99 1XBH
TITLE A BETA-HAIRPIN MIMIC FROM FCERI-ALPHA-CYCLO(L-262)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CYCLO(L-262));
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: DISULFIDE BETWEEN CYS1 AND CYS13
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: DERIVED FROM C-C' LOOP OF HUMAN FCERI-ALPHA
KEYWDS BETA-HAIRPIN, PEPTIDE MIMIC, ALLERGY, FCERI, IGE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.M.MCDONNELL,D.FUSHMAN,S.M.CAHILL,B.J.SUTTON,D.COWBURN
REVDAT 3 02-MAR-22 1XBH 1 REMARK LINK
REVDAT 2 24-FEB-09 1XBH 1 VERSN
REVDAT 1 21-FEB-99 1XBH 0
JRNL AUTH J.M.MCDONNELL,D.FUSHMAN,S.M.CAHILL,B.J.SUTTON,D.COWBURN
JRNL TITL SOLUTION STRUCTURES OF FCERI ALPHA-CHAIN MIMICS: A
JRNL TITL 2 BETA-HAIRPIN PEPTIDE AND ITS RETROENANTIOMER
JRNL REF J.AM.CHEM.SOC. V. 119 5321 1997
JRNL REFN ISSN 0002-7863
JRNL DOI 10.1021/JA963884O
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XBH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000502.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 5.50
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; ROESY; TOCSY; DQF-COSY;
REMARK 210 HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 TYR A 3 34.84 -179.48
REMARK 500 1 TYR A 4 157.18 -41.77
REMARK 500 1 LYS A 5 69.77 -177.14
REMARK 500 1 ASP A 6 177.09 173.69
REMARK 500 1 GLU A 8 34.30 38.35
REMARK 500 2 ILE A 2 142.63 61.35
REMARK 500 2 TYR A 3 69.72 -162.95
REMARK 500 2 TYR A 4 141.04 -34.45
REMARK 500 2 LYS A 5 86.69 -165.25
REMARK 500 2 TYR A 12 171.90 58.99
REMARK 500 3 TYR A 3 74.36 -162.12
REMARK 500 3 ASP A 6 149.01 172.19
REMARK 500 3 GLU A 8 47.53 38.99
REMARK 500 3 TYR A 12 171.53 69.81
REMARK 500 4 TYR A 3 76.46 -160.23
REMARK 500 4 ASP A 6 146.66 178.99
REMARK 500 4 TYR A 12 171.71 70.11
REMARK 500 5 TYR A 3 26.69 -163.72
REMARK 500 5 ASP A 6 -169.33 168.96
REMARK 500 5 GLU A 8 32.43 37.23
REMARK 500 6 ILE A 2 153.25 56.69
REMARK 500 6 TYR A 3 63.89 175.72
REMARK 500 6 TYR A 4 151.75 -49.82
REMARK 500 6 LYS A 5 79.62 -167.76
REMARK 500 6 LEU A 10 149.82 -170.07
REMARK 500 6 LYS A 11 138.21 -176.77
REMARK 500 7 TYR A 3 90.35 -22.30
REMARK 500 7 TYR A 4 83.80 -60.16
REMARK 500 7 ASP A 6 155.95 167.89
REMARK 500 7 TYR A 12 102.08 -41.71
REMARK 500 8 ILE A 2 140.41 60.94
REMARK 500 8 GLU A 8 -14.92 85.97
REMARK 500 8 TYR A 12 170.86 64.56
REMARK 500 9 TYR A 3 31.52 -165.52
REMARK 500 9 TYR A 4 148.18 -37.22
REMARK 500 9 LYS A 5 63.95 -170.30
REMARK 500 9 ASP A 6 179.87 174.80
REMARK 500 9 GLU A 8 44.07 38.71
REMARK 500 9 LYS A 11 148.05 -175.17
REMARK 500 10 TYR A 3 31.91 -172.30
REMARK 500 10 TYR A 4 155.89 -37.00
REMARK 500 10 LYS A 5 46.13 -175.89
REMARK 500 10 GLU A 8 37.91 38.64
REMARK 500 11 TYR A 3 25.96 -160.86
REMARK 500 11 TYR A 4 119.26 -36.69
REMARK 500 11 ASP A 6 -173.02 176.97
REMARK 500 11 GLU A 8 33.14 38.90
REMARK 500 11 LYS A 11 120.55 -174.60
REMARK 500 12 TYR A 3 85.48 -46.83
REMARK 500 12 TYR A 4 134.16 -35.17
REMARK 500
REMARK 500 THIS ENTRY HAS 64 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XBH A 1 13 PDB 1XBH 1XBH 1 13
SEQRES 1 A 13 CYS ILE TYR TYR LYS ASP GLY GLU ALA LEU LYS TYR DCY
MODRES 1XBH DCY A 13 CYS D-CYSTEINE
HET DCY A 13 10
HETNAM DCY D-CYSTEINE
FORMUL 1 DCY C3 H7 N O2 S
SHEET 1 A 2 LYS A 5 ASP A 6 0
SHEET 2 A 2 ALA A 9 LEU A 10 -1 O ALA A 9 N ASP A 6
SSBOND 1 CYS A 1 DCY A 13 1555 1555 2.11
LINK C TYR A 12 N DCY A 13 1555 1555 1.33
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 - 2 20 Bytes