Header list of 1g03.pdb file
Complete list - r 6 2 Bytes
HEADER VIRAL PROTEIN 05-OCT-00 1G03
TITLE NMR STRUCTURE OF N-TERMINAL DOMAIN OF HTLV-I CA1-134
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HTLV-I CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN OF MAJOR CORE PROTEIN P24;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN T-LYMPHOTROPIC VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11908;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PCYB1
KEYWDS BETA HAIRPIN LOOP, HELIX CORE, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.C.CORNILESCU,F.BOUAMR,X.YAO,C.CARTER,N.TJANDRA
REVDAT 4 06-APR-16 1G03 1 AUTHOR VERSN
REVDAT 3 24-FEB-09 1G03 1 VERSN
REVDAT 2 01-APR-03 1G03 1 JRNL
REVDAT 1 21-MAR-01 1G03 0
JRNL AUTH C.C.CORNILESCU,F.BOUAMR,X.YAO,C.CARTER,N.TJANDRA
JRNL TITL STRUCTURAL ANALYSIS OF THE N-TERMINAL DOMAIN OF THE HUMAN
JRNL TITL 2 T-CELL LEUKEMIA VIRUS CAPSID PROTEIN.
JRNL REF J.MOL.BIOL. V. 306 783 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11243788
JRNL DOI 10.1006/JMBI.2000.4395
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.840
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G03 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-00.
REMARK 100 THE RCSB ID CODE IS RCSB012065.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 302
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 10MM; 10MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6 MM HTLV-I CAPSID U-15N,13C;
REMARK 210 0.6 MM HTLV-I CAPSID U-15N,13C;
REMARK 210 0.6 MM HTLV-I CAPSID U-15N; 0.6
REMARK 210 MM HTLV-I CAPSID U-15N,13C 4%
REMARK 210 DMPC/DHPC 3:1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_NOESY; 4D_
REMARK 210 13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, NMRPIPE 1.7, PIPP/
REMARK 210 STAPP 4.2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING DIPOLAR COUPLINGS
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 HE22 GLN A 46 HE22 GLN A 114 1.32
REMARK 500 O LEU A 78 H ALA A 82 1.50
REMARK 500 O ASP A 130 H ALA A 134 1.56
REMARK 500 O ASP A 54 H LEU A 58 1.58
REMARK 500 OD1 ASN A 103 H GLN A 106 1.58
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 PRO A 14 -109.19 -77.55
REMARK 500 1 TRP A 15 -22.07 70.11
REMARK 500 1 GLN A 16 40.05 -174.61
REMARK 500 1 SER A 28 -77.56 -58.64
REMARK 500 1 GLN A 29 -54.19 -9.77
REMARK 500 1 PRO A 32 87.71 -48.74
REMARK 500 1 SER A 34 170.26 60.24
REMARK 500 1 GLN A 36 -36.36 -36.19
REMARK 500 1 ASP A 49 68.49 23.27
REMARK 500 1 CYS A 63 -143.02 -107.33
REMARK 500 1 LEU A 66 -72.79 -50.20
REMARK 500 1 GLN A 74 -71.62 -49.85
REMARK 500 1 ASP A 76 -71.34 -25.09
REMARK 500 1 THR A 88 53.27 -171.03
REMARK 500 1 SER A 89 19.60 48.12
REMARK 500 1 TYR A 90 128.78 46.80
REMARK 500 1 ASN A 91 -57.63 -136.69
REMARK 500 1 ALA A 94 -53.94 -7.82
REMARK 500 1 ARG A 98 -27.26 -38.15
REMARK 500 1 ASN A 102 37.43 -70.04
REMARK 500 1 LEU A 109 5.26 -65.90
REMARK 500 1 SER A 127 -10.25 160.41
REMARK 500 1 ALA A 128 94.13 178.14
REMARK 500 1 LYS A 129 -179.69 174.20
REMARK 500 1 PRO A 131 9.48 -68.40
REMARK 500 1 TRP A 133 -46.09 175.10
REMARK 500 2 ARG A 13 67.47 -159.84
REMARK 500 2 GLN A 16 59.95 -172.80
REMARK 500 2 SER A 28 -70.96 -62.65
REMARK 500 2 GLN A 29 -53.58 -12.71
REMARK 500 2 ALA A 30 -157.73 -94.58
REMARK 500 2 PRO A 32 47.92 -63.91
REMARK 500 2 SER A 34 159.73 62.03
REMARK 500 2 GLN A 36 -39.99 -37.96
REMARK 500 2 ASP A 49 66.68 22.21
REMARK 500 2 LEU A 59 -68.85 -94.14
REMARK 500 2 CYS A 63 -147.77 -106.83
REMARK 500 2 SER A 64 -64.00 -163.43
REMARK 500 2 SER A 65 -84.49 -156.39
REMARK 500 2 SER A 69 -72.52 -56.45
REMARK 500 2 GLN A 74 -71.36 -48.45
REMARK 500 2 ASP A 76 -71.00 -24.74
REMARK 500 2 ARG A 85 -32.79 -39.55
REMARK 500 2 ILE A 87 -151.46 -62.73
REMARK 500 2 THR A 88 58.94 -66.74
REMARK 500 2 SER A 89 17.31 45.00
REMARK 500 2 TYR A 90 127.96 45.87
REMARK 500 2 ASN A 91 -55.64 -135.82
REMARK 500 2 ALA A 94 -55.87 -9.72
REMARK 500 2 ARG A 98 -25.59 -38.45
REMARK 500
REMARK 500 THIS ENTRY HAS 646 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QRJ RELATED DB: PDB
REMARK 900 RELATED ID: 1GDS RELATED DB: PDB
DBREF 1G03 A 1 134 UNP P14077 GAG_HTL1M 131 264
SEQRES 1 A 134 PRO VAL MET HIS PRO HIS GLY ALA PRO PRO ASN HIS ARG
SEQRES 2 A 134 PRO TRP GLN MET LYS ASP LEU GLN ALA ILE LYS GLN GLU
SEQRES 3 A 134 VAL SER GLN ALA ALA PRO GLY SER PRO GLN PHE MET GLN
SEQRES 4 A 134 THR ILE ARG LEU ALA VAL GLN GLN PHE ASP PRO THR ALA
SEQRES 5 A 134 LYS ASP LEU GLN ASP LEU LEU GLN TYR LEU CYS SER SER
SEQRES 6 A 134 LEU VAL ALA SER LEU HIS HIS GLN GLN LEU ASP SER LEU
SEQRES 7 A 134 ILE SER GLU ALA GLU THR ARG GLY ILE THR SER TYR ASN
SEQRES 8 A 134 PRO LEU ALA GLY PRO LEU ARG VAL GLN ALA ASN ASN PRO
SEQRES 9 A 134 GLN GLN GLN GLY LEU ARG ARG GLU TYR GLN GLN LEU TRP
SEQRES 10 A 134 LEU ALA ALA PHE ALA ALA LEU PRO GLY SER ALA LYS ASP
SEQRES 11 A 134 PRO SER TRP ALA
HELIX 1 1 MET A 17 ALA A 30 1 14
HELIX 2 2 PRO A 35 PHE A 48 1 14
HELIX 3 3 THR A 51 TYR A 61 1 11
HELIX 4 4 SER A 64 ILE A 87 1 24
HELIX 5 5 PRO A 96 ASN A 102 1 7
HELIX 6 6 GLN A 107 ALA A 123 1 17
SHEET 1 A 2 VAL A 2 MET A 3 0
SHEET 2 A 2 ASN A 11 HIS A 12 -1 O ASN A 11 N MET A 3
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 - r 6 2 Bytes