HEADER VIRAL PROTEIN 14-DEC-07 2JYL
TITLE SOLUTION STRUCTURE OF A DOUBLE MUTANT OF THE CARBOXY-TERMINAL
TITLE 2 DIMERIZATION DOMAIN OF THE HIV-1 CAPSID PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAPSID PROTEIN P24 (CA);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: GAG-POL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HIV-1, CARBOXY-TERMINAL, DIMERIZATION DOMAIN, CTD, 3D-NMR, CAPSID
KEYWDS 2 PROTEIN (CA), DOUBLE MUTANT, MONOMER STRUCTURE, AIDS, ASPARTYL
KEYWDS 3 PROTEASE, CAPSID MATURATION, CORE PROTEIN, CYTOPLASM, DNA
KEYWDS 4 INTEGRATION, DNA RECOMBINATION, DNA-DIRECTED DNA POLYMERASE,
KEYWDS 5 ENDONUCLEASE, HYDROLASE, LIPOPROTEIN, MAGNESIUM, MEMBRANE, METAL-
KEYWDS 6 BINDING, MULTIFUNCTIONAL ENZYME, MYRISTATE, NUCLEASE,
KEYWDS 7 NUCLEOTIDYLTRANSFERASE, NUCLEUS, PHOSPHOPROTEIN, PROTEASE, RNA-
KEYWDS 8 BINDING, RNA-DIRECTED DNA POLYMERASE, TRANSFERASE, VIRAL
KEYWDS 9 NUCLEOPROTEIN, VIRION, ZINC, ZINC-FINGER, VIRAL PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR H.C.WONG,R.SHIN,N.R.KRISHNA
REVDAT 4 20-OCT-21 2JYL 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2JYL 1 VERSN
REVDAT 2 04-MAR-08 2JYL 1 JRNL
REVDAT 1 12-FEB-08 2JYL 0
JRNL AUTH H.C.WONG,R.SHIN,N.R.KRISHNA
JRNL TITL SOLUTION STRUCTURE OF A DOUBLE MUTANT OF THE
JRNL TITL 2 CARBOXY-TERMINAL DIMERIZATION DOMAIN OF THE HIV-1 CAPSID
JRNL TITL 3 PROTEIN.
JRNL REF BIOCHEMISTRY V. 47 2289 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18220423
JRNL DOI 10.1021/BI7022128
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA
REMARK 3 AUTHORS : GUNTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2JYL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000100452.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-98% 13C; U-98% 15N]
REMARK 210 PROTEIN, 50 MM SODIUM PHOSPHATE,
REMARK 210 90%H2O/10%D2O; 1 MM [U-98% 15N]
REMARK 210 PROTEIN, 50 MM SODIUM PHOSPHATE,
REMARK 210 90%H2O/10%D2O; 1 MM [U-95% 13C]
REMARK 210 PROTEIN, 50 MM SODIUM PHOSPHATE,
REMARK 210 90%H2O/10%D2O; 1 MM [U-98% 13C;
REMARK 210 U-98% 15N] PROTEIN, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100%D2O; 1 MM [U-98%
REMARK 210 15N] PROTEIN, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100%D2O; 1 MM [U-95%
REMARK 210 13C] PROTEIN, 50 MM SODIUM
REMARK 210 PHOSPHATE, 100%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCA; 3D
REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D HNCO;
REMARK 210 3D HCCH-TOCSY; 3D HNHA; 15N-HSQC-
REMARK 210 NOESY; 13C-HSQC-NOESY; HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURAL CONSTRAINTS INCLUDED NOE, HYDROGEN BONDS, AND
REMARK 210 TORSION ANGLE CONSTRAINTS
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 127
REMARK 465 GLY A 128
REMARK 465 SER A 129
REMARK 465 SER A 130
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 SER A 137
REMARK 465 SER A 138
REMARK 465 GLY A 139
REMARK 465 LEU A 140
REMARK 465 VAL A 141
REMARK 465 PRO A 142
REMARK 465 ARG A 143
REMARK 465 GLY A 144
REMARK 465 SER A 145
REMARK 465 HIS A 146
REMARK 465 MET A 147
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 HH TYR A 164 O LEU A 190 1.45
REMARK 500 O LEU A 189 H ASN A 193 1.47
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 GLU A 175 46.48 -172.76
REMARK 500 GLN A 176 99.45 -40.56
REMARK 500 ALA A 177 159.41 179.55
REMARK 500 GLU A 180 65.07 -161.76
REMARK 500 ASN A 195 175.89 -52.13
REMARK 500 LEU A 205 -84.94 -44.85
REMARK 500 VAL A 221 142.06 -39.31
REMARK 500 ALA A 228 108.26 -39.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JYG RELATED DB: PDB
REMARK 900 ENSEMBLE OF NMR STRUCTURES
DBREF 2JYL A 148 231 UNP P12497 POL_HV1N5 280 363
SEQADV 2JYL MET A 127 UNP P12497 EXPRESSION TAG
SEQADV 2JYL GLY A 128 UNP P12497 EXPRESSION TAG
SEQADV 2JYL SER A 129 UNP P12497 EXPRESSION TAG
SEQADV 2JYL SER A 130 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 131 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 132 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 133 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 134 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 135 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 136 UNP P12497 EXPRESSION TAG
SEQADV 2JYL SER A 137 UNP P12497 EXPRESSION TAG
SEQADV 2JYL SER A 138 UNP P12497 EXPRESSION TAG
SEQADV 2JYL GLY A 139 UNP P12497 EXPRESSION TAG
SEQADV 2JYL LEU A 140 UNP P12497 EXPRESSION TAG
SEQADV 2JYL VAL A 141 UNP P12497 EXPRESSION TAG
SEQADV 2JYL PRO A 142 UNP P12497 EXPRESSION TAG
SEQADV 2JYL ARG A 143 UNP P12497 EXPRESSION TAG
SEQADV 2JYL GLY A 144 UNP P12497 EXPRESSION TAG
SEQADV 2JYL SER A 145 UNP P12497 EXPRESSION TAG
SEQADV 2JYL HIS A 146 UNP P12497 EXPRESSION TAG
SEQADV 2JYL MET A 147 UNP P12497 EXPRESSION TAG
SEQADV 2JYL ALA A 184 UNP P12497 TRP 316 ENGINEERED MUTATION
SEQADV 2JYL ALA A 185 UNP P12497 MET 317 ENGINEERED MUTATION
SEQRES 1 A 105 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 105 LEU VAL PRO ARG GLY SER HIS MET THR SER ILE LEU ASP
SEQRES 3 A 105 ILE ARG GLN GLY PRO LYS GLU PRO PHE ARG ASP TYR VAL
SEQRES 4 A 105 ASP ARG PHE TYR LYS THR LEU ARG ALA GLU GLN ALA SER
SEQRES 5 A 105 GLN GLU VAL LYS ASN ALA ALA THR GLU THR LEU LEU VAL
SEQRES 6 A 105 GLN ASN ALA ASN PRO ASP CYS LYS THR ILE LEU LYS ALA
SEQRES 7 A 105 LEU GLY PRO GLY ALA THR LEU GLU GLU MET MET THR ALA
SEQRES 8 A 105 CYS GLN GLY VAL GLY GLY PRO GLY HIS LYS ALA ARG VAL
SEQRES 9 A 105 LEU
HELIX 1 1 SER A 149 ILE A 153 5 5
HELIX 2 2 PRO A 160 GLN A 176 1 17
HELIX 3 3 ALA A 185 ASN A 193 1 9
HELIX 4 4 ASN A 195 GLY A 206 1 12
HELIX 5 5 THR A 210 VAL A 221 1 12
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
(ATOM LINES ARE NOT SHOWN.)
END
