Header list of 1hyw.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 22-JAN-01 1HYW
TITLE SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPW
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAD-TO-TAIL JOINING PROTEIN W;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GPW;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 GENE: W;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(LAMBDADE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS NOVEL FOLD; TWO HELICES, ONE TWO-STRANDED BETA-SHEET, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.L.MAXWELL,A.A.YEE,V.BOOTH,C.H.ARROWSMITH,M.GOLD,A.R.DAVIDSON
REVDAT 4 23-FEB-22 1HYW 1 REMARK
REVDAT 3 24-FEB-09 1HYW 1 VERSN
REVDAT 2 31-DEC-02 1HYW 1 REMARK
REVDAT 1 25-APR-01 1HYW 0
JRNL AUTH K.L.MAXWELL,A.A.YEE,V.BOOTH,C.H.ARROWSMITH,M.GOLD,
JRNL AUTH 2 A.R.DAVIDSON
JRNL TITL THE SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA PROTEIN W, A
JRNL TITL 2 SMALL MORPHOGENETIC PROTEIN POSSESSING A NOVEL FOLD.
JRNL REF J.MOL.BIOL. V. 308 9 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11302702
JRNL DOI 10.1006/JMBI.2001.4582
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1293 RESTRAINTS, 1171 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 72
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,50 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1HYW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012697.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 200MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM GPW U-15N, 13C; 10MM
REMARK 210 PHOSPHATE BUFFER NA, 200MM NACL,
REMARK 210 90% H2O,10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 3.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-15
REMARK 465 RES C SSSEQI
REMARK 465 ARG A 59
REMARK 465 ARG A 60
REMARK 465 ARG A 61
REMARK 465 GLY A 62
REMARK 465 PRO A 63
REMARK 465 ALA A 64
REMARK 465 GLY A 65
REMARK 465 PHE A 66
REMARK 465 TYR A 67
REMARK 465 VAL A 68
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 LEU A 43 H ILE A 47 1.54
REMARK 500 O ILE A 47 H GLU A 51 1.57
REMARK 500 O ALA A 24 H PHE A 35 1.57
REMARK 500 O ASP A 16 H THR A 19 1.59
REMARK 500 O VAL A 40 H LYS A 44 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 THR A 19 -66.39 -149.28
REMARK 500 1 LYS A 21 -163.72 -53.22
REMARK 500 1 ARG A 22 -36.96 -162.53
REMARK 500 1 ASP A 29 52.30 -101.49
REMARK 500 1 THR A 36 -154.89 -125.36
REMARK 500 1 ALA A 37 39.82 -96.54
REMARK 500 1 THR A 54 158.45 -45.87
REMARK 500 2 THR A 2 99.80 68.19
REMARK 500 2 ARG A 3 50.35 -115.51
REMARK 500 2 LYS A 21 -164.03 -52.68
REMARK 500 2 ARG A 22 -42.40 -155.10
REMARK 500 2 ASP A 29 39.74 -96.16
REMARK 500 2 THR A 36 -162.84 -123.55
REMARK 500 2 ALA A 37 43.56 -88.95
REMARK 500 2 THR A 38 -54.74 -131.21
REMARK 500 2 GLN A 53 -89.46 -76.78
REMARK 500 2 THR A 54 164.71 51.53
REMARK 500 2 MET A 56 79.55 54.49
REMARK 500 2 THR A 57 118.35 -161.99
REMARK 500 3 THR A 2 58.42 -143.75
REMARK 500 3 THR A 19 -67.15 -154.13
REMARK 500 3 LYS A 21 -166.07 -52.89
REMARK 500 3 ARG A 22 -41.62 -155.19
REMARK 500 3 THR A 36 -162.22 -123.98
REMARK 500 3 ALA A 37 43.49 -89.06
REMARK 500 3 THR A 38 -55.83 -131.18
REMARK 500 3 GLN A 53 -104.37 -71.93
REMARK 500 3 THR A 54 161.09 54.43
REMARK 500 3 MET A 56 89.28 57.43
REMARK 500 4 THR A 2 118.77 -163.67
REMARK 500 4 THR A 19 61.91 -152.22
REMARK 500 4 LYS A 21 -158.64 -54.01
REMARK 500 4 ARG A 22 -45.06 -166.19
REMARK 500 4 ASP A 29 47.56 -96.81
REMARK 500 4 THR A 36 -156.90 -125.64
REMARK 500 4 THR A 54 157.65 -37.80
REMARK 500 5 THR A 2 -48.83 177.78
REMARK 500 5 ARG A 3 72.89 -111.15
REMARK 500 5 THR A 19 -68.34 -152.20
REMARK 500 5 LYS A 21 -166.94 -52.21
REMARK 500 5 ARG A 22 -43.13 -154.07
REMARK 500 5 ASP A 29 44.45 -102.99
REMARK 500 5 THR A 36 -162.74 -124.00
REMARK 500 5 ALA A 37 43.70 -88.84
REMARK 500 5 THR A 38 -53.00 -131.67
REMARK 500 5 GLN A 53 -100.87 -73.20
REMARK 500 5 THR A 54 155.39 54.92
REMARK 500 5 THR A 57 124.87 61.13
REMARK 500 6 LYS A 21 -163.88 -53.11
REMARK 500 6 ARG A 22 -40.88 -155.82
REMARK 500
REMARK 500 THIS ENTRY HAS 135 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HYW A 1 68 UNP P68660 VHTJ_LAMBD 1 68
SEQRES 1 A 68 MET THR ARG GLN GLU GLU LEU ALA ALA ALA ARG ALA ALA
SEQRES 2 A 68 LEU HIS ASP LEU MET THR GLY LYS ARG VAL ALA THR VAL
SEQRES 3 A 68 GLN LYS ASP GLY ARG ARG VAL GLU PHE THR ALA THR SER
SEQRES 4 A 68 VAL SER ASP LEU LYS LYS TYR ILE ALA GLU LEU GLU VAL
SEQRES 5 A 68 GLN THR GLY MET THR GLN ARG ARG ARG GLY PRO ALA GLY
SEQRES 6 A 68 PHE TYR VAL
HELIX 1 1 ARG A 3 MET A 18 1 16
HELIX 2 2 SER A 39 THR A 54 1 16
SHEET 1 A 2 ALA A 24 GLN A 27 0
SHEET 2 A 2 ARG A 32 PHE A 35 -1 O VAL A 33 N VAL A 26
CISPEP 1 MET A 56 THR A 57 9 0.00
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