REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.9.3 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK, REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.89 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.52 REMARK 3 NUMBER OF REFLECTIONS : 22242 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 + TEST SET) : 0.1935 REMARK 3 R VALUE (WORKING SET) : 0.1923 REMARK 3 FREE R VALUE : 0.2166 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.15 REMARK 3 FREE R VALUE TEST SET COUNT : 1145 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 : 11 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.73 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.52 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2336 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2244 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2217 REMARK 3 BIN R VALUE (WORKING SET) : 0.2250 REMARK 3 BIN FREE R VALUE : 0.2115 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.09 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 119 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 : 1508 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 180 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.96 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.42 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.2493 REMARK 3 B22 (A**2) : -0.5178 REMARK 3 B33 (A**2) : 0.7670 REMARK 3 B12 (A**2) : 0.0000 REMARK 3 B13 (A**2) : 0.0000 REMARK 3 B23 (A**2) : 0.0000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.193 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.116 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.105 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.106 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.100 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.9453 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.9427 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 1546 ; 2.00 ; HARMONIC REMARK 3 BOND ANGLES : 2087 ; 2.00 ; HARMONIC REMARK 3 TORSION ANGLES : 540 ; 2.00 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 42 ; 2.00 ; HARMONIC REMARK 3 GENERAL PLANES : 224 ; 5.00 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 1546 ; 20.00 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 201 ; 5.00 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 1951 ; 4.00 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.88 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.33 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.80 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2XXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-NOV-10. REMARK 100 THE PDBE ID CODE IS EBI-46197. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-FEB-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 5 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR REMARK 200 OPTICS : DYNAMICALLY BENDABLE REMARK 200 MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22400 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.65 REMARK 200 RESOLUTION RANGE LOW (A) : 40.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4 REMARK 200 DATA REDUNDANCY : 5.5 REMARK 200 R MERGE (I) : 0.09 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.10 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8 REMARK 200 DATA REDUNDANCY IN SHELL : 1.9 REMARK 200 R MERGE FOR SHELL (I) : 0.36 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.00 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2XV6 REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.4 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, 200MM AMMONIUM REMARK 280 ACETATE, 100MM SODIUM ACETATE PH 4.6 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 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 66.86000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.75500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 66.86000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 19.75500 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 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3420 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, T 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B2009 LIES ON A SPECIAL POSITION. REMARK 375 HOH B2057 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLN A 219 REMARK 465 GLY A 220 REMARK 465 MET B -1 REMARK 465 ALA B 0 REMARK 465 GLN B 1 REMARK 465 VAL B 2 REMARK 465 GLN B 3 REMARK 465 HIS B 114 REMARK 465 HIS B 115 REMARK 465 HIS B 116 REMARK 465 HIS B 117 REMARK 465 HIS B 118 REMARK 465 HIS B 119 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1114 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1115 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT T1012 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A8O RELATED DB: PDB REMARK 900 HIV CAPSID C-TERMINAL DOMAIN REMARK 900 RELATED ID: 2ITG RELATED DB: PDB REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE REMARK 900 SITE IN THE F185H CONSTRUCT REMARK 900 RELATED ID: 2H3Z RELATED DB: PDB REMARK 900 STRUCTURE OF THE HIV-1 MATRIX PROTEIN BOUND TO DI- REMARK 900 C4-PHOSPHATIDYLINOSITOL-(4,5)-BISPHOSPHATE REMARK 900 RELATED ID: 2H3Q RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF HIV-1 MYRMA BOUND TO DI-C4- REMARK 900 PHOSPHATIDYLINOSITOL-(4,5)-BISPHOSPHATE REMARK 900 RELATED ID: 1HIW RELATED DB: PDB REMARK 900 TRIMERIC HIV-1 MATRIX PROTEIN REMARK 900 RELATED ID: 1WKN RELATED DB: PDB REMARK 900 A PLAUSIBLE MODEL OF FULL-LENGTH INTEGRASEDNA COMPLEX REMARK 900 RELATED ID: 9HVP RELATED DB: PDB REMARK 900 HIV-1 PROTEASE COMPLEX WITH A-74704 REMARK 900 RELATED ID: 1QS4 RELATED DB: PDB REMARK 900 CORE DOMAIN OF HIV-1 INTEGRASE COMLEXED WITH MG++ REMARK 900 AND 1-(5- CHLOROINDOL-3-YL)-3-HYDROXY-3-(2H- REMARK 900 TETRAZOL-5-YL)-PROPENONE REMARK 900 RELATED ID: 1BL3 RELATED DB: PDB REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE REMARK 900 RELATED ID: 2H3I RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE HIV-1 MYRISTOYLATED MATRIX REMARK 900 PROTEIN REMARK 900 RELATED ID: 1A43 RELATED DB: PDB REMARK 900 STRUCTURE OF THE HIV-1 CAPSID PROTEIN DIMERIZATION REMARK 900 DOMAINAT 2.6A RESOLUTION REMARK 900 RELATED ID: 1BIZ RELATED DB: PDB REMARK 900 HIV-1 INTEGRASE CORE DOMAIN REMARK 900 RELATED ID: 1WJB RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN REMARK 900 OF HIV-1 INTEGRASE (D FORM), NMR, 40 STRUCTURES REMARK 900 RELATED ID: 1K6Y RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A TWO-DOMAIN FRAGMENT OF HIV- REMARK 900 1INTEGRASE REMARK 900 RELATED ID: 1GWP RELATED DB: PDB REMARK 900 STRUCTURE OF THE N-TERMINAL DOMAIN OF THE MATURE HIV REMARK 900 -1 CAPSID PROTEIN REMARK 900 RELATED ID: 2H3V RELATED DB: PDB REMARK 900 STRUCTURE OF THE HIV-1 MATRIX PROTEIN BOUND TO DI- REMARK 900 C8-PHOSPHATIDYLINOSITOL-(4,5)-BISPHOSPHATE REMARK 900 RELATED ID: 1B9F RELATED DB: PDB REMARK 900 MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS REMARK 900 CORRELATED WITH CATALYTIC ACTIVITY REMARK 900 RELATED ID: 2H3F RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE HIV-1 MA PROTEIN REMARK 900 RELATED ID: 4PHV RELATED DB: PDB REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1) PROTEASE REMARK 900 COMPLEX WITH N,N-BIS(2(R)-HYDROXY-1(S)-INDANYL)- REMARK 900 2,6-(R,R)- DIPHENYLMETHYL-4-HYDROXY-1,7- REMARK 900 HEPTANDIAMIDE REMARK 900 RELATED ID: 1B92 RELATED DB: PDB REMARK 900 MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS REMARK 900 CORRELATED WITH CATALYTIC ACTIVITY REMARK 900 RELATED ID: 1BAJ RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT PLUS GAG P2 REMARK 900 DOMAIN REMARK 900 RELATED ID: 1BHL RELATED DB: PDB REMARK 900 CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE REMARK 900 RELATED ID: 2B4J RELATED DB: PDB REMARK 900 STRUCTURAL BASIS FOR THE RECOGNITION BETWEEN HIV- REMARK 900 1INTEGRASE AND LEDGF/P75 REMARK 900 RELATED ID: 1UPH RELATED DB: PDB REMARK 900 HIV-1 MYRISTOYLATED MATRIX REMARK 900 RELATED ID: 1BIS RELATED DB: PDB REMARK 900 HIV-1 INTEGRASE CORE DOMAIN REMARK 900 RELATED ID: 1M9D RELATED DB: PDB REMARK 900 X-RAY CRYSTAL STRUCTURE OF CYCLOPHILIN A/HIV-1 CA REMARK 900 N-TERMINAL DOMAIN (1-146) O-TYPE CHIMERA COMPLEX. REMARK 900 RELATED ID: 1AFV RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3 REMARK 900 RELATED ID: 5HVP RELATED DB: PDB REMARK 900 HIV-1 PROTEASE COMPLEX WITH ACETYL-PEPSTATIN (NY5 REMARK 900 STRAIN) REMARK 900 RELATED ID: 1B9D RELATED DB: PDB REMARK 900 MOBILITY OF AN HIV-1 INTEGRASE ACTIVE SITE LOOP IS REMARK 900 CORRELATED WITH CATALYTIC ACTIVITY REMARK 900 RELATED ID: 2HMX RELATED DB: PDB REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX PROTEIN 2HMX REMARK 900 3 REMARK 900 RELATED ID: 2X2D RELATED DB: PDB REMARK 900 ACETYL-CYPA:HIV-1 N-TERM CAPSID DOMAIN COMPLEX REMARK 900 RELATED ID: 1AUM RELATED DB: PDB REMARK 900 HIV CAPSID C-TERMINAL DOMAIN (CAC146) REMARK 900 RELATED ID: 1AK4 RELATED DB: PDB REMARK 900 HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN REMARK 900 OF HIV-1 CAPSID REMARK 900 RELATED ID: 1BIU RELATED DB: PDB REMARK 900 HIV-1 INTEGRASE CORE DOMAIN COMPLEXED WITH MG++ REMARK 900 RELATED ID: 1BI4 RELATED DB: PDB REMARK 900 CATALYTIC DOMAIN OF HIV-1 INTEGRASE REMARK 900 RELATED ID: 1WJD RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE N-TERMINAL ZN BINDING DOMAIN REMARK 900 OF HIV-1 INTEGRASE (E FORM), NMR, 38 STRUCTURES REMARK 900 RELATED ID: 2HVP RELATED DB: PDB REMARK 900 HIV-1 PROTEASE REMARK 900 RELATED ID: 1ITG RELATED DB: PDB REMARK 900 HIV-1 INTEGRASE (CATALYTIC DOMAIN COMPRISING RESIDUES 50 REMARK 900 - 212) MUTANT WITH GLY-SER-HIS APPENDED TO THE N- REMARK 900 TERMINUS AND PHE 185 REPLACED BY LYS (INS(47-49), REMARK 900 F185K) REMARK 900 RELATED ID: 2XT1 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HIV-1 CAPSID PROTEIN C- REMARK 900 TERMINAL DOMAIN (146-231) IN COMPLEX WITH A CAMELID REMARK 900 VHH. REMARK 900 RELATED ID: 2XXC RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A CAMELID VHH RAISED AGAINST THE REMARK 900 HIV-1 CAPSID PROTEIN C-TERMINAL DOMAIN. REMARK 900 RELATED ID: 2XV6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE HIV-1 CAPSID PROTEIN C- REMARK 900 TERMINAL DOMAIN (146-220) IN COMPLEX WITH A CAMELID REMARK 900 VHH.