Header list of 1qrj.pdb file
Complete list - b 12 2 Bytes
HEADER VIRAL PROTEIN 14-JUN-99 1QRJ
TITLE SOLUTION STRUCTURE OF HTLV-I CAPSID PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HTLV-I CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN T-CELL LYMPHOTROPHIC VIRUS TYPE 1;
SOURCE 3 ORGANISM_TAXID: 11926;
SOURCE 4 STRAIN: ATK;
SOURCE 5 GENE: GAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HMS174(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET16B;
SOURCE 11 OTHER_DETAILS: T7-RNA POLYMERASE-BASED EXPRESSION SYSTEM
KEYWDS HTLV-I, CAPSID PROTEIN, RETROVIRUS, TWO-DOMAIN PROTEIN, ALPHA HELICAL
KEYWDS 2 PROTEIN, HETERONUCLEAR NMR SPECTROSCOPY, VIRUS/VIRAL PROTEIN, VIRAL
KEYWDS 3 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.KHORASANIZADEH,R.CAMPOS-OLIVAS,C.A.CLARK,M.F.SUMMERS
REVDAT 5 16-OCT-13 1QRJ 1 ATOM REMARK SEQRES VERSN
REVDAT 4 24-FEB-09 1QRJ 1 VERSN
REVDAT 3 26-SEP-01 1QRJ 1 HELIX
REVDAT 2 13-JUL-99 1QRJ 1 JRNL
REVDAT 1 13-JUL-99 1QRJ 0
JRNL AUTH S.KHORASANIZADEH,R.CAMPOS-OLIVAS,C.A.CLARK,M.F.SUMMERS
JRNL TITL SEQUENCE-SPECIFIC 1H, 13C AND 15N CHEMICAL SHIFT ASSIGNMENT
JRNL TITL 2 AND SECONDARY STRUCTURE OF THE HTLV-I CAPSID PROTEIN.
JRNL REF J.BIOMOL.NMR V. 14 199 1999
JRNL REFN ISSN 0925-2738
JRNL PMID 10427751
JRNL DOI 10.1023/A:1008307507462
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.4
REMARK 3 AUTHORS : GUNTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QRJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-99.
REMARK 100 THE RCSB ID CODE IS RCSB009182.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.00
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM HTLV-I CAPSID U- 15N, U-
REMARK 210 13C/15N, U-13C/ 15N/2H; 50 MM
REMARK 210 PHOSPHATE BUFFER PH 6.0, 300 MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE THE PUBLICATION FOR THE
REMARK 210 SPECIFIC EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, NMRPIPE 1.7,
REMARK 210 NMRVIEW 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST DYANA
REMARK 210 TARGET FUNCTION: RANGE 0.37-0.74
REMARK 210 ANGSTROM SQUARED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 LEU A 155 H GLY A 158 1.47
REMARK 500 O PRO A 143 H PHE A 147 1.50
REMARK 500 O LYS A 165 H LEU A 169 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 HIS A 2 82.40 47.59
REMARK 500 1 HIS A 3 141.41 62.98
REMARK 500 1 HIS A 5 150.75 69.76
REMARK 500 1 HIS A 9 100.28 -177.18
REMARK 500 1 HIS A 14 50.66 -174.80
REMARK 500 1 MET A 15 100.38 52.23
REMARK 500 1 GLN A 25 -72.74 -69.55
REMARK 500 1 ALA A 30 166.45 -46.38
REMARK 500 1 PRO A 35 49.92 -75.09
REMARK 500 1 GLN A 47 -72.45 -80.59
REMARK 500 1 ASP A 49 93.92 72.79
REMARK 500 1 THR A 51 -170.90 -58.84
REMARK 500 1 CYS A 63 171.06 -59.22
REMARK 500 1 SER A 65 -70.75 -58.17
REMARK 500 1 ILE A 87 154.70 59.48
REMARK 500 1 THR A 88 -80.56 -36.30
REMARK 500 1 LEU A 97 -62.84 -120.65
REMARK 500 1 PRO A 104 48.08 -74.97
REMARK 500 1 GLN A 105 -45.43 -144.33
REMARK 500 1 ALA A 128 -164.22 -162.65
REMARK 500 1 ALA A 154 -30.85 -39.64
REMARK 500 1 TYR A 174 -73.27 -107.45
REMARK 500 1 SER A 175 -31.55 -39.90
REMARK 500 1 ASN A 176 60.31 -117.26
REMARK 500 1 ASN A 178 172.55 -46.96
REMARK 500 1 LYS A 179 -71.88 -61.13
REMARK 500 1 HIS A 190 29.45 -154.86
REMARK 500 1 GLN A 203 -32.35 -38.15
REMARK 500 1 LYS A 210 146.10 -178.94
REMARK 500 1 LYS A 212 148.86 61.94
REMARK 500 2 HIS A 3 -61.55 71.70
REMARK 500 2 HIS A 4 164.66 -47.36
REMARK 500 2 HIS A 5 -60.75 -138.32
REMARK 500 2 SER A 6 161.92 63.44
REMARK 500 2 ARG A 13 85.13 -156.96
REMARK 500 2 HIS A 14 47.22 39.46
REMARK 500 2 MET A 15 85.34 178.46
REMARK 500 2 GLN A 25 -72.44 -72.83
REMARK 500 2 ALA A 30 170.89 -52.61
REMARK 500 2 GLN A 47 -76.13 -79.41
REMARK 500 2 ASP A 49 95.14 71.50
REMARK 500 2 LEU A 62 -61.96 -91.98
REMARK 500 2 THR A 88 -84.83 -38.76
REMARK 500 2 ALA A 128 111.18 79.00
REMARK 500 2 ASP A 130 115.24 165.68
REMARK 500 2 TYR A 174 -78.39 -110.47
REMARK 500 2 SER A 175 -32.50 -37.05
REMARK 500 2 ASN A 176 57.74 -110.74
REMARK 500 2 ASN A 178 -175.58 -52.28
REMARK 500 2 THR A 191 -54.86 -121.09
REMARK 500
REMARK 500 THIS ENTRY HAS 468 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QRJ A 1 214 UNP P03345 GAG_HTL1A 146 344
SEQADV 1QRJ HIS A 1 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 2 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 3 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 4 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 5 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ SER A 6 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ SER A 7 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ GLY A 8 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 9 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ ILE A 10 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ GLU A 11 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ GLY A 12 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ ARG A 13 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ HIS A 14 UNP P03345 EXPRESSION TAG
SEQADV 1QRJ MET A 15 UNP P03345 EXPRESSION TAG
SEQRES 1 A 214 HIS HIS HIS HIS HIS SER SER GLY HIS ILE GLU GLY ARG
SEQRES 2 A 214 HIS MET GLN MET LYS ASP LEU GLN ALA ILE LYS GLN GLU
SEQRES 3 A 214 VAL SER GLN ALA ALA PRO GLY SER PRO GLN PHE MET GLN
SEQRES 4 A 214 THR ILE ARG LEU ALA VAL GLN GLN PHE ASP PRO THR ALA
SEQRES 5 A 214 LYS ASP LEU GLN ASP LEU LEU GLN TYR LEU CYS SER SER
SEQRES 6 A 214 LEU VAL ALA SER LEU HIS HIS GLN GLN LEU ASP SER LEU
SEQRES 7 A 214 ILE SER GLU ALA GLU THR ARG GLY ILE THR GLY TYR ASN
SEQRES 8 A 214 PRO LEU ALA GLY PRO LEU ARG VAL GLN ALA ASN ASN PRO
SEQRES 9 A 214 GLN GLN GLN GLY LEU ARG ARG GLU TYR GLN GLN LEU TRP
SEQRES 10 A 214 LEU ALA ALA PHE ALA ALA LEU PRO GLY SER ALA LYS ASP
SEQRES 11 A 214 PRO SER TRP ALA SER ILE LEU GLN GLY LEU GLU GLU PRO
SEQRES 12 A 214 TYR HIS ALA PHE VAL GLU ARG LEU ASN ILE ALA LEU ASP
SEQRES 13 A 214 ASN GLY LEU PRO GLU GLY THR PRO LYS ASP PRO ILE LEU
SEQRES 14 A 214 ARG SER LEU ALA TYR SER ASN ALA ASN LYS GLU CYS GLN
SEQRES 15 A 214 LYS LEU LEU GLN ALA ARG GLY HIS THR ASN SER PRO LEU
SEQRES 16 A 214 GLY ASP MET LEU ARG ALA CYS GLN THR TRP THR PRO LYS
SEQRES 17 A 214 ASP LYS THR LYS VAL LEU
HELIX 1 1 GLN A 16 ALA A 30 1 15
HELIX 2 2 GLN A 36 PHE A 48 1 13
HELIX 3 3 THR A 51 GLN A 60 1 10
HELIX 4 4 SER A 64 ARG A 85 1 22
HELIX 5 5 LEU A 97 ASN A 102 1 6
HELIX 6 6 GLN A 107 ALA A 122 1 16
HELIX 7 7 SER A 132 ILE A 136 5 5
HELIX 8 8 PRO A 143 ASN A 157 1 15
HELIX 9 9 LYS A 165 TYR A 174 1 10
HELIX 10 10 ASN A 178 GLY A 189 1 12
HELIX 11 11 PRO A 194 GLN A 203 1 10
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 12 2 Bytes