Header list of 1wz4.pdb file
Complete list - 2 20 Bytes
HEADER GENE REGULATION 23-FEB-05 1WZ4
TITLE SOLUTION CONFORMATION OF ADR SUBTYPE HBV PRE-S2 EPITOPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR SURFACE ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE SEQUENCE OCCURS NATURALLY IN PRES2(123-145)
SOURCE 4 REGION OF SURFACE ENVELOPE PROTEIN OF HEPATITIS B VIRUS
KEYWDS HELIX TURN HELIX, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.W.CHI,K.H.HAN
REVDAT 4 02-MAR-22 1WZ4 1 REMARK
REVDAT 3 19-JAN-10 1WZ4 1 JRNL
REVDAT 2 24-FEB-09 1WZ4 1 VERSN
REVDAT 1 16-MAY-06 1WZ4 0
JRNL AUTH S.W.CHI,D.H.KIM,J.S.KIM,M.K.LEE,K.H.HAN
JRNL TITL SOLUTION CONFORMATION OF AN IMMUNODOMINANT EPITOPE IN THE
JRNL TITL 2 HEPATITIS B VIRUS PRES2 SURFACE ANTIGEN.
JRNL REF ANTIVIRAL RES. V. 72 207 2006
JRNL REFN ISSN 0166-3542
JRNL PMID 16872688
JRNL DOI 10.1016/J.ANTIVIRAL.2006.06.009
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DISCOVER 2.98
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WZ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024175.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 298
REMARK 210 PH : 3.85; 3.85
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 5MM ADR123; 5MM ADR123
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; PE
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 TYR A 18 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 2 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 5 TYR A 18 CB - CG - CD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 6 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 7 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 9 TYR A 18 CB - CG - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 10 TYR A 18 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 10 TYR A 18 CB - CG - CD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 11 TYR A 18 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 12 TYR A 18 CB - CG - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 13 TYR A 18 CB - CG - CD1 ANGL. DEV. = -7.5 DEGREES
REMARK 500 14 TYR A 18 CB - CG - CD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 15 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 17 TYR A 18 CB - CG - CD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 18 TYR A 18 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 19 TYR A 18 CB - CG - CD2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 20 TYR A 18 CB - CG - CD2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 20 TYR A 18 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
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 ALA A 8 36.66 -96.33
REMARK 500 1 ASP A 11 143.74 166.50
REMARK 500 1 PRO A 12 -0.88 -50.48
REMARK 500 1 ARG A 13 44.40 -150.15
REMARK 500 1 ARG A 15 -59.54 -29.40
REMARK 500 1 TYR A 18 30.45 -160.20
REMARK 500 2 GLN A 7 -40.34 -29.36
REMARK 500 2 LEU A 10 -2.52 -140.84
REMARK 500 2 ASP A 11 144.40 168.90
REMARK 500 2 ARG A 13 47.54 -144.72
REMARK 500 2 TYR A 18 25.80 -146.46
REMARK 500 3 ASP A 11 136.86 171.74
REMARK 500 3 PRO A 12 -36.88 -32.21
REMARK 500 3 ARG A 13 49.20 -147.72
REMARK 500 3 LEU A 17 21.04 -76.01
REMARK 500 3 TYR A 18 24.59 -146.62
REMARK 500 4 ASP A 11 134.57 167.92
REMARK 500 4 PRO A 12 -35.18 -33.45
REMARK 500 4 ARG A 13 47.65 -145.01
REMARK 500 4 TYR A 18 19.74 -145.83
REMARK 500 5 ALA A 8 35.74 -94.85
REMARK 500 5 ASP A 11 148.09 166.68
REMARK 500 5 PRO A 12 8.98 -61.26
REMARK 500 5 ARG A 13 41.47 -151.23
REMARK 500 5 ARG A 15 -49.09 -29.94
REMARK 500 5 TYR A 18 16.90 -145.38
REMARK 500 6 ALA A 8 31.25 -95.32
REMARK 500 6 ASP A 11 137.60 168.52
REMARK 500 6 PRO A 12 -39.65 -31.90
REMARK 500 6 ARG A 13 50.71 -143.06
REMARK 500 6 LEU A 17 20.92 -74.24
REMARK 500 6 TYR A 18 25.26 -146.87
REMARK 500 7 ASP A 11 159.82 173.68
REMARK 500 7 ARG A 13 53.51 -153.84
REMARK 500 7 TYR A 18 22.42 -145.72
REMARK 500 8 ALA A 8 31.35 -99.44
REMARK 500 8 ASP A 11 136.22 171.96
REMARK 500 8 PRO A 12 -34.25 -33.65
REMARK 500 8 ARG A 13 48.75 -147.41
REMARK 500 8 LEU A 17 20.98 -73.20
REMARK 500 8 TYR A 18 25.36 -145.62
REMARK 500 9 ASP A 11 151.58 168.03
REMARK 500 9 ARG A 13 47.54 -144.68
REMARK 500 9 TYR A 18 23.16 -141.38
REMARK 500 10 ASP A 11 135.45 178.32
REMARK 500 10 PRO A 12 -32.52 -36.15
REMARK 500 10 ARG A 13 49.44 -147.04
REMARK 500 10 TYR A 18 36.76 -147.80
REMARK 500 11 GLN A 7 -37.12 -37.02
REMARK 500 11 ASP A 11 139.65 166.71
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 13 VAL A 14 7 149.83
REMARK 500 LEU A 17 TYR A 18 10 -144.19
REMARK 500 ARG A 13 VAL A 14 13 145.99
REMARK 500 PRO A 12 ARG A 13 14 149.41
REMARK 500 ARG A 13 VAL A 14 17 147.52
REMARK 500 ARG A 13 VAL A 14 18 149.68
REMARK 500 ASP A 11 PRO A 12 19 143.89
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 PHE A 5 0.17 SIDE CHAIN
REMARK 500 1 TYR A 18 0.24 SIDE CHAIN
REMARK 500 2 PHE A 5 0.17 SIDE CHAIN
REMARK 500 2 TYR A 18 0.19 SIDE CHAIN
REMARK 500 2 PHE A 19 0.08 SIDE CHAIN
REMARK 500 3 PHE A 5 0.12 SIDE CHAIN
REMARK 500 3 TYR A 18 0.18 SIDE CHAIN
REMARK 500 3 PHE A 19 0.09 SIDE CHAIN
REMARK 500 4 PHE A 5 0.15 SIDE CHAIN
REMARK 500 4 TYR A 18 0.07 SIDE CHAIN
REMARK 500 4 PHE A 19 0.12 SIDE CHAIN
REMARK 500 5 PHE A 5 0.17 SIDE CHAIN
REMARK 500 5 TYR A 18 0.29 SIDE CHAIN
REMARK 500 5 PHE A 19 0.08 SIDE CHAIN
REMARK 500 6 PHE A 5 0.11 SIDE CHAIN
REMARK 500 6 TYR A 18 0.18 SIDE CHAIN
REMARK 500 6 PHE A 19 0.09 SIDE CHAIN
REMARK 500 7 PHE A 5 0.16 SIDE CHAIN
REMARK 500 7 TYR A 18 0.08 SIDE CHAIN
REMARK 500 7 PHE A 19 0.11 SIDE CHAIN
REMARK 500 8 PHE A 5 0.11 SIDE CHAIN
REMARK 500 8 TYR A 18 0.18 SIDE CHAIN
REMARK 500 8 PHE A 19 0.09 SIDE CHAIN
REMARK 500 9 PHE A 5 0.11 SIDE CHAIN
REMARK 500 9 TYR A 18 0.14 SIDE CHAIN
REMARK 500 9 PHE A 19 0.11 SIDE CHAIN
REMARK 500 10 PHE A 5 0.16 SIDE CHAIN
REMARK 500 10 TYR A 18 0.25 SIDE CHAIN
REMARK 500 10 PHE A 19 0.09 SIDE CHAIN
REMARK 500 11 PHE A 5 0.18 SIDE CHAIN
REMARK 500 11 TYR A 18 0.14 SIDE CHAIN
REMARK 500 11 PHE A 19 0.11 SIDE CHAIN
REMARK 500 12 PHE A 5 0.11 SIDE CHAIN
REMARK 500 12 TYR A 18 0.14 SIDE CHAIN
REMARK 500 12 PHE A 19 0.09 SIDE CHAIN
REMARK 500 13 PHE A 5 0.18 SIDE CHAIN
REMARK 500 13 TYR A 18 0.08 SIDE CHAIN
REMARK 500 13 PHE A 19 0.09 SIDE CHAIN
REMARK 500 14 PHE A 5 0.17 SIDE CHAIN
REMARK 500 14 TYR A 18 0.24 SIDE CHAIN
REMARK 500 15 PHE A 5 0.15 SIDE CHAIN
REMARK 500 15 TYR A 18 0.09 SIDE CHAIN
REMARK 500 15 PHE A 19 0.12 SIDE CHAIN
REMARK 500 16 PHE A 5 0.12 SIDE CHAIN
REMARK 500 16 TYR A 18 0.19 SIDE CHAIN
REMARK 500 17 PHE A 5 0.12 SIDE CHAIN
REMARK 500 17 TYR A 18 0.25 SIDE CHAIN
REMARK 500 18 PHE A 5 0.15 SIDE CHAIN
REMARK 500 18 TYR A 18 0.19 SIDE CHAIN
REMARK 500 18 PHE A 19 0.12 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1WZ4 A 1 23 UNP P03140 VMSA_HPBVR 123 145
SEQRES 1 A 23 ASN SER THR THR PHE HIS GLN ALA LEU LEU ASP PRO ARG
SEQRES 2 A 23 VAL ARG GLY LEU TYR PHE PRO ALA GLY GLY
HELIX 1 1 ASN A 1 GLN A 7 1 7
HELIX 2 2 VAL A 14 TYR A 18 5 5
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