Header list of 1k0h.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 19-SEP-01 1K0H
TITLE SOLUTION STRUCTURE OF BACTERIOPHAGE LAMBDA GPFII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GPFII;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TAIL ATTACHMENT PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 GENE: FII;
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 TWISTED BETA-SANDWICH, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.L.MAXWELL,A.A.YEE,C.H.ARROWSMITH,M.GOLD,A.R.DAVIDSON
REVDAT 4 23-FEB-22 1K0H 1 REMARK
REVDAT 3 24-FEB-09 1K0H 1 VERSN
REVDAT 2 18-DEC-02 1K0H 1 REMARK
REVDAT 1 17-JUL-02 1K0H 0
JRNL AUTH K.L.MAXWELL,A.A.YEE,C.H.ARROWSMITH,M.GOLD,A.R.DAVIDSON
JRNL TITL THE SOLUTION STRUCTURE OF THE BACTERIOPHAGE LAMBDA HEAD-TAIL
JRNL TITL 2 JOINING PROTEIN, GPFII.
JRNL REF J.MOL.BIOL. V. 318 1395 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12083526
JRNL DOI 10.1016/S0022-2836(02)00276-0
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: NULL
REMARK 4
REMARK 4 1K0H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014405.
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 : 1.3MM GPFII U-15N, 13C; 10MM
REMARK 210 PHOSPHATE BUFFER NA, 200MM NACL
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, XEASY 1.3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
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 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 ILE A 83 H GLU A 86 1.54
REMARK 500 H LEU A 65 O LEU A 103 1.57
REMARK 500 H ILE A 29 O ALA A 37 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 6 -76.29 64.48
REMARK 500 1 LEU A 7 -59.21 -163.76
REMARK 500 1 ASP A 9 60.12 -156.50
REMARK 500 1 ALA A 10 -54.80 -144.13
REMARK 500 1 ALA A 15 -66.29 -144.17
REMARK 500 1 ASP A 16 67.88 68.02
REMARK 500 1 GLU A 17 146.45 -173.87
REMARK 500 1 THR A 18 76.13 67.42
REMARK 500 1 ASN A 48 -73.29 70.90
REMARK 500 1 TYR A 51 -77.70 -100.85
REMARK 500 1 VAL A 56 -46.31 -161.09
REMARK 500 1 ARG A 57 -64.25 67.76
REMARK 500 1 VAL A 58 24.01 49.29
REMARK 500 1 GLU A 59 -49.57 -165.09
REMARK 500 1 THR A 69 -101.43 -171.21
REMARK 500 1 ASP A 70 35.29 177.95
REMARK 500 1 LEU A 75 61.53 -65.05
REMARK 500 1 ARG A 77 159.44 -42.02
REMARK 500 1 GLU A 86 31.16 98.65
REMARK 500 1 ARG A 92 174.15 -44.29
REMARK 500 1 SER A 94 85.02 -161.61
REMARK 500 1 ASP A 96 -52.16 -170.72
REMARK 500 1 ASP A 97 77.11 -108.18
REMARK 500 1 LEU A 103 77.22 61.99
REMARK 500 1 VAL A 109 94.12 -32.08
REMARK 500 1 ALA A 112 109.78 -48.87
REMARK 500 1 VAL A 113 25.16 -141.04
REMARK 500 1 ASN A 114 76.27 48.63
REMARK 500 2 ALA A 2 -68.63 69.28
REMARK 500 2 ASP A 5 60.75 -107.18
REMARK 500 2 PHE A 8 117.91 59.76
REMARK 500 2 ASP A 9 -51.51 -127.42
REMARK 500 2 ALA A 10 -64.62 -178.94
REMARK 500 2 ALA A 15 -179.11 55.02
REMARK 500 2 THR A 18 91.36 52.42
REMARK 500 2 TYR A 22 172.28 -59.26
REMARK 500 2 MET A 23 -81.99 -62.87
REMARK 500 2 GLU A 33 -75.63 -57.10
REMARK 500 2 GLU A 47 48.11 -107.66
REMARK 500 2 TYR A 51 63.11 -68.45
REMARK 500 2 ALA A 52 -67.12 67.21
REMARK 500 2 GLN A 54 136.51 69.72
REMARK 500 2 VAL A 58 37.58 -94.79
REMARK 500 2 GLU A 59 71.63 74.96
REMARK 500 2 SER A 61 -44.57 -169.99
REMARK 500 2 THR A 69 122.86 167.49
REMARK 500 2 ASP A 70 62.28 -66.36
REMARK 500 2 LEU A 75 63.24 -67.11
REMARK 500 2 ILE A 83 -136.84 -122.70
REMARK 500 2 GLU A 86 19.78 57.71
REMARK 500
REMARK 500 THIS ENTRY HAS 298 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K0H A 1 117 UNP P03714 VCF2_LAMBD 1 117
SEQRES 1 A 117 MET ALA ASP PHE ASP ASN LEU PHE ASP ALA ALA ILE ALA
SEQRES 2 A 117 ARG ALA ASP GLU THR ILE ARG GLY TYR MET GLY THR SER
SEQRES 3 A 117 ALA THR ILE THR SER GLY GLU GLN SER GLY ALA VAL ILE
SEQRES 4 A 117 ARG GLY VAL PHE ASP ASP PRO GLU ASN ILE SER TYR ALA
SEQRES 5 A 117 GLY GLN GLY VAL ARG VAL GLU GLY SER SER PRO SER LEU
SEQRES 6 A 117 PHE VAL ARG THR ASP GLU VAL ARG GLN LEU ARG ARG GLY
SEQRES 7 A 117 ASP THR LEU THR ILE GLY GLU GLU ASN PHE TRP VAL ASP
SEQRES 8 A 117 ARG VAL SER PRO ASP ASP GLY GLY SER CYS HIS LEU TRP
SEQRES 9 A 117 LEU GLY ARG GLY VAL PRO PRO ALA VAL ASN ARG ARG ARG
SHEET 1 A 5 SER A 64 VAL A 67 0
SHEET 2 A 5 ALA A 37 ASP A 44 -1 N ASP A 44 O SER A 64
SHEET 3 A 5 SER A 26 THR A 30 -1 N ILE A 29 O ALA A 37
SHEET 4 A 5 THR A 80 ILE A 83 -1 O THR A 80 N THR A 30
SHEET 5 A 5 PHE A 88 TRP A 89 -1 O PHE A 88 N LEU A 81
CISPEP 1 PRO A 110 PRO A 111 3 0.49
CISPEP 2 PRO A 110 PRO A 111 8 0.82
CRYST1 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