Header list of 1pjw.pdb file
Complete list - b 23 2 Bytes
HEADER VIRAL PROTEIN 04-JUN-03 1PJW
TITLE SOLUTION STRUCTURE OF THE DOMAIN III OF THE JAPAN ENCEPHALITIS VIRUS
TITLE 2 ENVELOPE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN III;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: JAPANESE ENCEPHALITIS VIRUS;
SOURCE 3 ORGANISM_TAXID: 11072;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS FLAVIVIRUS, JEV, E PROTEIN, EPITOPE MAPPING, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.P.WU,C.W.WU,Y.P.TSAO,Y.C.LOU,C.W.LIN
REVDAT 3 23-FEB-22 1PJW 1 REMARK
REVDAT 2 24-FEB-09 1PJW 1 VERSN
REVDAT 1 25-NOV-03 1PJW 0
JRNL AUTH K.P.WU,C.W.WU,Y.P.TSAO,T.W.KUO,Y.C.LOU,C.W.LIN,S.C.WU,
JRNL AUTH 2 J.W.CHENG
JRNL TITL STRUCTURAL BASIS OF A FLAVIVIRUS RECOGNIZED BY ITS
JRNL TITL 2 NEUTRALIZING ANTIBODY: SOLUTION STRUCTURE OF THE DOMAIN III
JRNL TITL 3 OF THE JAPANESE ENCEPHALITIS VIRUS ENVELOPE PROTEIN.
JRNL REF J.BIOL.CHEM. V. 278 46007 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12952958
JRNL DOI 10.1074/JBC.M307776200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR 3.851
REMARK 3 AUTHORS : BO BLANTON (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 957 RESTRAINTS, 717 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 194
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,46 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1PJW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019375.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.3MM JEV DOMAIN III PROTEIN,
REMARK 210 N15-C13 LABLED AND N15-LABLED,
REMARK 210 136MM NACL, 2.68MM KCL, 10MM
REMARK 210 NA2HPO4, 1.76MM KH2PO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.1, NMRPIPE, X-PLOR
REMARK 210 3.851
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 H THR A 26 O THR A 30 1.60
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 9 109.43 -47.56
REMARK 500 1 THR A 14 41.96 -161.56
REMARK 500 1 LEU A 54 29.96 81.47
REMARK 500 1 VAL A 60 -49.08 -143.89
REMARK 500 1 VAL A 66 170.68 -44.65
REMARK 500 1 ASN A 67 157.70 -47.08
REMARK 500 1 LYS A 78 88.86 -62.87
REMARK 500 1 GLU A 84 62.87 -113.43
REMARK 500 1 MET A 96 -150.77 -108.38
REMARK 500 1 ASP A 98 -105.67 -74.98
REMARK 500 1 ALA A 108 152.36 179.76
REMARK 500 2 LYS A 6 -164.03 -106.66
REMARK 500 2 THR A 14 42.12 -160.84
REMARK 500 2 LEU A 54 29.55 81.17
REMARK 500 2 VAL A 60 -36.22 -139.20
REMARK 500 2 VAL A 66 173.30 -47.16
REMARK 500 2 LYS A 78 88.06 -63.21
REMARK 500 2 GLU A 84 68.56 -117.95
REMARK 500 2 ASP A 98 -108.41 -64.00
REMARK 500 2 ALA A 108 131.06 -172.69
REMARK 500 3 TYR A 10 174.47 -46.79
REMARK 500 3 THR A 14 44.04 -161.43
REMARK 500 3 LYS A 16 61.85 -111.48
REMARK 500 3 LEU A 54 30.51 79.53
REMARK 500 3 VAL A 60 -37.37 -148.24
REMARK 500 3 VAL A 66 -170.61 -55.07
REMARK 500 3 LYS A 78 89.56 -64.34
REMARK 500 3 GLU A 84 70.05 -118.07
REMARK 500 3 ASP A 98 -75.58 -71.14
REMARK 500 3 ALA A 108 141.14 179.73
REMARK 500 4 THR A 9 155.42 -46.67
REMARK 500 4 THR A 14 -76.55 -158.24
REMARK 500 4 LYS A 16 81.97 -56.04
REMARK 500 4 LEU A 54 30.76 77.21
REMARK 500 4 VAL A 60 -36.41 -143.86
REMARK 500 4 VAL A 66 -175.02 -57.92
REMARK 500 4 ASN A 67 156.91 -46.93
REMARK 500 4 ALA A 71 65.01 -66.09
REMARK 500 4 LYS A 78 88.33 -62.96
REMARK 500 4 GLU A 84 72.72 -106.57
REMARK 500 4 ASP A 98 -82.82 -65.97
REMARK 500 4 SER A 110 -150.47 -65.15
REMARK 500 5 LEU A 5 73.98 -103.71
REMARK 500 5 THR A 9 76.30 -114.26
REMARK 500 5 THR A 14 61.70 -160.54
REMARK 500 5 LEU A 54 30.39 80.07
REMARK 500 5 VAL A 60 -59.42 -133.83
REMARK 500 5 VAL A 66 171.25 -44.34
REMARK 500 5 ASN A 67 162.20 -46.86
REMARK 500 5 LYS A 78 89.11 -63.92
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 62 0.24 SIDE CHAIN
REMARK 500 3 ARG A 62 0.21 SIDE CHAIN
REMARK 500 4 ARG A 62 0.24 SIDE CHAIN
REMARK 500 5 ARG A 62 0.31 SIDE CHAIN
REMARK 500 6 ARG A 62 0.17 SIDE CHAIN
REMARK 500 7 ARG A 62 0.31 SIDE CHAIN
REMARK 500 8 ARG A 62 0.30 SIDE CHAIN
REMARK 500 9 ARG A 62 0.30 SIDE CHAIN
REMARK 500 10 ARG A 62 0.30 SIDE CHAIN
REMARK 500 11 ARG A 62 0.21 SIDE CHAIN
REMARK 500 13 ARG A 62 0.25 SIDE CHAIN
REMARK 500 14 ARG A 62 0.26 SIDE CHAIN
REMARK 500 15 ARG A 62 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PJW A 1 111 UNP Q9J0X3 Q9J0X3_9FLAV 292 402
SEQRES 1 A 111 ASP LYS LEU ALA LEU LYS GLY THR THR TYR GLY MET CYS
SEQRES 2 A 111 THR GLU LYS PHE SER PHE ALA LYS ASN PRO ALA ASP THR
SEQRES 3 A 111 GLY HIS GLY THR VAL VAL ILE GLU LEU SER TYR SER GLY
SEQRES 4 A 111 SER ASP GLY PRO CYS LYS ILE PRO ILE VAL SER VAL ALA
SEQRES 5 A 111 SER LEU ASN ASP MET THR PRO VAL GLY ARG LEU VAL THR
SEQRES 6 A 111 VAL ASN PRO PHE VAL ALA THR SER SER ALA ASN SER LYS
SEQRES 7 A 111 VAL LEU VAL GLU MET GLU PRO PRO PHE GLY ASP SER TYR
SEQRES 8 A 111 ILE VAL VAL GLY MET GLY ASP LYS GLN ILE ASN HIS HIS
SEQRES 9 A 111 TRP HIS LYS ALA GLY SER THR
SHEET 1 A 3 PHE A 17 ASP A 25 0
SHEET 2 A 3 VAL A 31 TYR A 37 -1 O VAL A 32 N ALA A 24
SHEET 3 A 3 LYS A 78 MET A 83 -1 O VAL A 81 N ILE A 33
SHEET 1 B 3 ILE A 48 ALA A 52 0
SHEET 2 B 3 SER A 90 GLY A 95 -1 O TYR A 91 N VAL A 51
SHEET 3 B 3 GLN A 100 TRP A 105 -1 O HIS A 103 N ILE A 92
SSBOND 1 CYS A 13 CYS A 44 1555 1555 2.02
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