Header list of 1gp8.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 11-MAY-99 1GP8
TITLE NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF
TITLE 2 BACTERIOPHAGE P22 SCAFFOLDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (SCAFFOLDING PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FUNCTIONAL DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE P22;
SOURCE 3 ORGANISM_TAXID: 10754;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: NF1829;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS SCAFFOLDING PROTEIN, COAT PROTEIN-BINDING DOMAIN, HELIX-LOOP-HELIX
KEYWDS 2 MOTIF, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 35
AUTHOR Y.SUN,M.H.PARKER,P.WEIGELE,S.CASJENS,P.E.PREVELIGE JR.,N.R.KRISHNA
REVDAT 5 23-FEB-22 1GP8 1 REMARK
REVDAT 4 24-FEB-09 1GP8 1 VERSN
REVDAT 3 06-JAN-04 1GP8 3 ATOM
REVDAT 2 24-APR-00 1GP8 1 JRNL HEADER
REVDAT 1 17-MAY-99 1GP8 0
JRNL AUTH Y.SUN,M.H.PARKER,P.WEIGELE,S.CASJENS,P.E.PREVELIGE JR.,
JRNL AUTH 2 N.R.KRISHNA
JRNL TITL STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF THE
JRNL TITL 2 SCAFFOLDING PROTEIN FROM A DOUBLE-STRANDED DNA VIRUS.
JRNL REF J.MOL.BIOL. V. 297 1195 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10764583
JRNL DOI 10.1006/JMBI.2000.3620
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. THE REFINEMENT WAS CARRIED OUT ON THE C-
REMARK 3 TERMINAL 40-RESIDUE SEGMENT.
REMARK 4
REMARK 4 1GP8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001043.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% WATER/90% D2O, 99.9% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY; 15N EDITED
REMARK 210 3D NOESY-HSQC; TOCSYHMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AM600; AVANCE600; INOVA600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 35
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: EXPERIMENTS WERE DONE ON THE C-TERMINAL 67-RESIDUE (238
REMARK 210 -303 PLUS ALANINE AT THE N-TERNINUS) SCAFFOLDING PROTEIN.
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 O THR A 291 H LEU A 295 1.59
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 ASN A 272 -71.08 -43.44
REMARK 500 1 ALA A 284 -76.11 -77.47
REMARK 500 1 SER A 285 43.45 -85.49
REMARK 500 1 LYS A 298 -70.46 -44.92
REMARK 500 1 LYS A 300 37.10 -89.62
REMARK 500 2 ASP A 267 -69.70 -101.43
REMARK 500 2 VAL A 268 -160.15 -72.03
REMARK 500 2 SER A 269 -33.66 -39.03
REMARK 500 2 ALA A 282 -77.21 -61.76
REMARK 500 2 ALA A 284 -77.53 -65.48
REMARK 500 2 SER A 285 41.26 -85.89
REMARK 500 2 ASP A 288 48.92 -89.45
REMARK 500 3 THR A 265 163.48 -48.18
REMARK 500 3 VAL A 268 -172.96 -68.78
REMARK 500 3 LYS A 273 -70.31 -41.98
REMARK 500 3 ALA A 275 -77.85 -42.00
REMARK 500 3 ALA A 284 -66.69 -103.69
REMARK 500 3 SER A 285 46.14 -85.19
REMARK 500 3 LYS A 286 -34.49 -138.33
REMARK 500 3 LYS A 300 46.07 -85.35
REMARK 500 4 ASP A 267 59.24 -66.14
REMARK 500 4 VAL A 268 -166.02 -78.09
REMARK 500 4 SER A 269 -39.46 -39.85
REMARK 500 4 ALA A 275 -73.63 -43.54
REMARK 500 4 ALA A 284 -75.70 -72.25
REMARK 500 4 SER A 285 43.68 -85.60
REMARK 500 4 GLU A 290 -70.33 -44.27
REMARK 500 5 ASP A 267 -176.29 -69.98
REMARK 500 5 VAL A 268 -163.72 -77.59
REMARK 500 5 ALA A 275 -70.74 -42.21
REMARK 500 5 LYS A 278 -72.64 -43.55
REMARK 500 5 ALA A 284 -70.15 -79.89
REMARK 500 5 SER A 285 45.01 -85.32
REMARK 500 5 LYS A 286 -31.17 -134.57
REMARK 500 5 LYS A 294 -72.40 -43.04
REMARK 500 6 VAL A 268 171.91 -45.45
REMARK 500 6 ASN A 272 -70.71 -61.37
REMARK 500 6 ALA A 284 -71.38 -73.91
REMARK 500 6 SER A 285 42.52 -85.35
REMARK 500 7 LYS A 273 -72.41 -42.87
REMARK 500 7 ALA A 284 -68.69 -90.50
REMARK 500 7 SER A 285 44.22 -83.14
REMARK 500 7 LYS A 286 -30.69 -134.81
REMARK 500 7 LYS A 294 -72.85 -43.24
REMARK 500 8 VAL A 268 -166.64 -56.20
REMARK 500 8 LYS A 273 -72.91 -42.44
REMARK 500 8 ALA A 275 -84.84 -42.63
REMARK 500 8 LYS A 278 -74.46 -46.94
REMARK 500 8 ALA A 282 -73.10 -54.33
REMARK 500 8 ALA A 284 -81.70 -68.80
REMARK 500
REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1GP8 A 264 303 UNP P26748 VG08_BPP22 264 303
SEQRES 1 A 40 ILE THR GLY ASP VAL SER ALA ALA ASN LYS ASP ALA ILE
SEQRES 2 A 40 ARG LYS GLN MET ASP ALA ALA ALA SER LYS GLY ASP VAL
SEQRES 3 A 40 GLU THR TYR ARG LYS LEU LYS ALA LYS LEU LYS GLY ILE
SEQRES 4 A 40 ARG
HELIX 1 1 VAL A 268 SER A 285 1 18
HELIX 2 2 ASP A 288 LYS A 300 1 13
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 - b 23 2 Bytes