REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH C.BERTHET-COLOMINAS,S.MONACO,A.NOVELLI,G.SIBAI, REMARK 1 AUTH 2 F.MALLET,S.CUSACK REMARK 1 TITL HEAD-TO-TAIL DIMERS AND INTERDOMAIN FLEXIBILITY REMARK 1 TITL 2 REVEALED BY THE CRYSTAL STRUCTURE OF HIV-1 CAPSID REMARK 1 TITL 3 PROTEIN (P24) COMPLEXED WITH A MONOCLONAL ANTIBODY REMARK 1 TITL 4 FAB REMARK 1 REF EMBO J. V. 18 1124 1999 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 10064580 REMARK 1 DOI 10.1093/EMBOJ/18.5.1124 REMARK 1 REMARK 1 REFERENCE 2 REMARK 1 AUTH V.CHEYNET,B.VERRIER,F.MALLET REMARK 1 TITL OVEREXPRESSION OF HIV-1 PROTEINS IN E. COLI BY A REMARK 1 TITL 2 MODIFIED EXPRESSION VECTOR AND THEIR ONE-STEP REMARK 1 TITL 3 PURIFICATION REMARK 1 REF PROTEIN EXPR.PURIF. V. 4 367 1993 REMARK 1 REFN ISSN 1046-5928 REMARK 1 PMID 8251747 REMARK 1 DOI 10.1006/PREP.1993.1048 REMARK 2 REMARK 2 RESOLUTION. 3.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.0 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.0 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.7 REMARK 3 NUMBER OF REFLECTIONS : 14740 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.284 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.6 REMARK 3 FREE R VALUE TEST SET COUNT : 1528 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5028 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.201 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : NULL REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: PARTIALLY DISORDERED REGIONS: L152 - REMARK 3 L155 AND H134 - H140 MISSING RESIDUES IN P24: HIS TAG, 12 REMARK 3 FIRSTS AA, P146, P86 TO P95 REMARK 4 REMARK 4 1E6J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-AUG-00. REMARK 100 THE PDBE ID CODE IS EBI-5216. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JAN-98 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID14-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.945 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14742 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 27.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7 REMARK 200 DATA REDUNDANCY : 2.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.09400 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : 33.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.27600 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: FAB13B5, 1AFV, 1AM3 REMARK 200 REMARK 200 REMARK: PATTERSON CORRELATION ALGORITHM OF XPLOR USED IN REMARK 200 CONJUNCTION WITH AMORE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.6 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 7MG/ML IN 7% PEG8000, REMARK 280 0.1M TRIS-HCL PH=7.5, 5MM DTT, 0.5MM K2PTCL4 AT 4C USING THE REMARK 280 HANGING DROP SYSTEM REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 96.54000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.80000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 96.54000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.80000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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 GENERATING THE BIOMOLECULE 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 5550 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 39220 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.4 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 PRO H 219 O REMARK 470 ASN L 210 O REMARK 470 GLY P 220 O REMARK 475 REMARK 475 ZERO OCCUPANCY RESIDUES REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY) REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES; REMARK 475 C=CHAIN IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE) REMARK 475 M RES C SSEQI REMARK 475 GLY H 134 REMARK 475 SER H 135 REMARK 475 ALA H 136 REMARK 475 ALA H 137 REMARK 475 GLN H 138 REMARK 475 THR H 139 REMARK 475 ASN H 140 REMARK 475 GLU L 152 REMARK 475 ARG L 153 REMARK 475 GLN L 154 REMARK 475 ASN L 155 REMARK 475 VAL P 11 REMARK 475 HIS P 12 REMARK 475 VAL P 86 REMARK 475 HIS P 87 REMARK 475 ALA P 88 REMARK 475 GLY P 89 REMARK 475 PRO P 90 REMARK 475 ILE P 91 REMARK 475 ALA P 92 REMARK 475 PRO P 93 REMARK 475 GLY P 94 REMARK 475 GLN P 95 REMARK 475 SER P 146 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 480 I=INSERTION CODE): REMARK 480 M RES CSSEQI ATOMS REMARK 480 ASP H 66 CG OD1 OD2 REMARK 480 GLU P 29 CG CD OE1 OE2 REMARK 480 LYS P 30 CG CD CE NZ REMARK 480 ASP P 166 CG OD1 OD2 REMARK 480 GLN P 176 CG CD OE1 NE2 REMARK 480 LYS P 182 CG CD CE NZ 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 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 LEU H 45 104.66 70.92 REMARK 500 LYS H 67 -51.57 -159.21 REMARK 500 ALA H 92 -171.20 -176.50 REMARK 500 ARG H 102 -105.47 -125.25 REMARK 500 ALA H 136 -165.47 86.91 REMARK 500 GLN H 138 96.48 175.58 REMARK 500 SER H 167 -43.02 -144.15 REMARK 500 GLN H 178 -55.16 -122.88 REMARK 500 SER H 179 -69.12 -154.39 REMARK 500 GLU L 49 60.61 27.11 REMARK 500 ILE L 50 -53.98 69.87 REMARK 500 ALA L 83 -169.87 -177.94 REMARK 500 ASN L 136 75.31 43.69 REMARK 500 PRO L 139 179.40 -59.78 REMARK 500 ASN L 188 -39.96 -142.17 REMARK 500 LYS L 197 2.81 -64.03 REMARK 500 SER L 199 149.60 -170.43 REMARK 500 ALA P 31 -97.51 54.66 REMARK 500 PHE P 32 30.90 -144.79 REMARK 500 HIS P 62 28.27 49.98 REMARK 500 VAL P 86 -93.60 7.63 REMARK 500 PRO P 90 81.15 -65.56 REMARK 500 ALA P 92 100.78 72.59 REMARK 500 GLN P 95 -73.51 -139.54 REMARK 500 THR P 119 75.54 -115.49 REMARK 500 PRO P 125 61.60 -68.20 REMARK 500 ALA P 174 59.86 -116.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1AFV RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT PLUS GAG P2 DOMAIN REMARK 900 RELATED ID: 1A80 RELATED DB: PDB REMARK 900 HIV CAPSID C-TERMINAL DOMAIN REMARK 900 RELATED ID: 1TAM RELATED DB: PDB REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS, NMR, MINIMIZED AVERAGE REMARK 900 STRUCTURE REMARK 900 RELATED ID: 1ESK RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF NCP7 FROM HIV-1 REMARK 900 RELATED ID: 1E6O RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FAB13B5 AGAINST HIV-1 CAPSID REMARK 900 PROTEIN P24