HEADER TRANSFERASE 07-DEC-13 4CIE
TITLE INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL CHALLENGE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTEGRASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 50-212;
COMPND 5 EC: 2.7.7.7;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS TRANSFERASE, HIV INTEGRASE, STRUCTURE BASED DRUG DESIGN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.PEAT
REVDAT 4 20-DEC-23 4CIE 1 JRNL REMARK
REVDAT 3 25-JUN-14 4CIE 1 JRNL
REVDAT 2 26-FEB-14 4CIE 1 JRNL
REVDAT 1 08-JAN-14 4CIE 0
JRNL AUTH T.S.PEAT,O.DOLEZAL,J.NEWMAN,D.MOBLEY,J.J.DEADMAN
JRNL TITL INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
JRNL TITL 2 CHALLENGE.
JRNL REF J.COMPUT.AIDED MOL.DES. V. 28 347 2014
JRNL REFN ISSN 0920-654X
JRNL PMID 24532034
JRNL DOI 10.1007/S10822-014-9721-7
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39662
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2091
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2948
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 140
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05000
REMARK 3 B22 (A**2) : 0.05000
REMARK 3 B33 (A**2) : -0.17000
REMARK 3 B12 (A**2) : 0.05000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.094
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.556
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2664 ; 0.005 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2540 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3658 ; 1.240 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5880 ; 0.711 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 343 ; 4.940 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 111 ;30.221 ;25.405
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 457 ;13.342 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.720 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 409 ; 0.053 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3089 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 597 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1271 ; 1.312 ; 3.258
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1266 ; 1.310 ; 3.251
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1604 ; 2.254 ; 5.468
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1393 ; 1.613 ; 3.645
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4CIE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1290059184.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41777
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 19.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
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 3ZSQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE PROTEIN WAS CONCENTRATED TO 5.5
REMARK 280 MG/ML IN 40 MM TRIS PH 8.0, 250 MM NACL, 30 MM MGCL2, 5 MM DTT
REMARK 280 AND SET UP IN A 1:1 RATIO WITH 1.6 TO 2.0 M AMMONIUM SULFATE,
REMARK 280 100 MM SODIUM ACETATE BUFFER PH 5.0 TO 5.5., PH 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 22.31433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.62867
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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. (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 MET A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 SER A 33
REMARK 465 HIS A 34
REMARK 465 HIS A 35
REMARK 465 HIS A 36
REMARK 465 HIS A 37
REMARK 465 HIS A 38
REMARK 465 HIS A 39
REMARK 465 SER A 40
REMARK 465 SER A 41
REMARK 465 GLY A 42
REMARK 465 LEU A 43
REMARK 465 VAL A 44
REMARK 465 PRO A 45
REMARK 465 ARG A 46
REMARK 465 GLY A 47
REMARK 465 SER A 48
REMARK 465 HIS A 49
REMARK 465 MET A 50
REMARK 465 HIS A 51
REMARK 465 GLY A 52
REMARK 465 GLN A 53
REMARK 465 VAL A 54
REMARK 465 ASP A 55
REMARK 465 SER A 56
REMARK 465 LYS A 188
REMARK 465 GLY A 189
REMARK 465 GLY A 190
REMARK 465 ILE A 191
REMARK 465 GLY A 192
REMARK 465 GLY A 193
REMARK 465 GLN A 209
REMARK 465 THR A 210
REMARK 465 LYS A 211
REMARK 465 GLU A 212
REMARK 465 MET B 30
REMARK 465 GLY B 31
REMARK 465 SER B 32
REMARK 465 SER B 33
REMARK 465 HIS B 34
REMARK 465 HIS B 35
REMARK 465 HIS B 36
REMARK 465 HIS B 37
REMARK 465 HIS B 38
REMARK 465 HIS B 39
REMARK 465 SER B 40
REMARK 465 SER B 41
REMARK 465 GLY B 42
REMARK 465 LEU B 43
REMARK 465 VAL B 44
REMARK 465 PRO B 45
REMARK 465 ARG B 46
REMARK 465 GLY B 47
REMARK 465 SER B 48
REMARK 465 HIS B 49
REMARK 465 MET B 50
REMARK 465 HIS B 51
REMARK 465 GLY B 52
REMARK 465 GLN B 53
REMARK 465 VAL B 54
REMARK 465 ASP B 55
REMARK 465 SER B 56
REMARK 465 LYS B 188
REMARK 465 GLY B 189
REMARK 465 GLY B 190
REMARK 465 ILE B 191
REMARK 465 GLY B 192
REMARK 465 GLY B 193
REMARK 465 GLN B 209
REMARK 465 THR B 210
REMARK 465 LYS B 211
REMARK 465 GLU B 212
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y7N A 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Y7N B 1217
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CHN RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CHO RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CHP RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CHQ RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CHY RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CHZ RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CIF RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
REMARK 900 RELATED ID: 4CIG RELATED DB: PDB
REMARK 900 INTERROGATING HIV INTEGRASE FOR COMPOUNDS THAT BIND- A SAMPL
REMARK 900 CHALLENGE
DBREF 4CIE A 50 212 UNP F2WR52 F2WR52_9HIV1 50 212
DBREF 4CIE B 50 212 UNP F2WR52 F2WR52_9HIV1 50 212
SEQADV 4CIE MET A 30 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY A 31 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 32 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 33 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 34 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 35 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 36 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 37 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 38 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 39 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 40 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 41 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY A 42 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE LEU A 43 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE VAL A 44 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE PRO A 45 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE ARG A 46 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY A 47 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 48 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS A 49 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER A 56 UNP F2WR52 CYS 56 ENGINEERED MUTATION
SEQADV 4CIE ASP A 139 UNP F2WR52 PHE 139 ENGINEERED MUTATION
SEQADV 4CIE HIS A 185 UNP F2WR52 PHE 185 ENGINEERED MUTATION
SEQADV 4CIE MET B 30 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY B 31 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 32 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 33 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 34 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 35 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 36 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 37 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 38 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 39 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 40 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 41 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY B 42 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE LEU B 43 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE VAL B 44 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE PRO B 45 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE ARG B 46 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE GLY B 47 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 48 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE HIS B 49 UNP F2WR52 EXPRESSION TAG
SEQADV 4CIE SER B 56 UNP F2WR52 CYS 56 ENGINEERED MUTATION
SEQADV 4CIE ASP B 139 UNP F2WR52 PHE 139 ENGINEERED MUTATION
SEQADV 4CIE HIS B 185 UNP F2WR52 PHE 185 ENGINEERED MUTATION
SEQRES 1 A 183 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 183 LEU VAL PRO ARG GLY SER HIS MET HIS GLY GLN VAL ASP
SEQRES 3 A 183 SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU
SEQRES 4 A 183 GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER
SEQRES 5 A 183 GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY
SEQRES 6 A 183 GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG
SEQRES 7 A 183 TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN
SEQRES 8 A 183 PHE THR SER THR THR VAL LYS ALA ALA CYS TRP TRP ALA
SEQRES 9 A 183 GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN
SEQRES 10 A 183 SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS
SEQRES 11 A 183 LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU
SEQRES 12 A 183 LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS
SEQRES 13 A 183 LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU
SEQRES 14 A 183 ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS
SEQRES 15 A 183 GLU
SEQRES 1 B 183 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 183 LEU VAL PRO ARG GLY SER HIS MET HIS GLY GLN VAL ASP
SEQRES 3 B 183 SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU
SEQRES 4 B 183 GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER
SEQRES 5 B 183 GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY
SEQRES 6 B 183 GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG
SEQRES 7 B 183 TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN
SEQRES 8 B 183 PHE THR SER THR THR VAL LYS ALA ALA CYS TRP TRP ALA
SEQRES 9 B 183 GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN
SEQRES 10 B 183 SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS
SEQRES 11 B 183 LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU
SEQRES 12 B 183 LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS
SEQRES 13 B 183 LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU
SEQRES 14 B 183 ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS
SEQRES 15 B 183 GLU
HET SO4 A1209 5
HET SO4 A1210 5
HET SO4 A1211 5
HET SO4 A1212 5
HET CL A1213 1
HET ACY A1214 4
HET Y7N A1215 31
HET SO4 B1209 5
HET SO4 B1210 5
HET SO4 B1211 5
HET SO4 B1212 5
HET CL B1213 1
HET ACY B1214 4
HET ACY B1215 4
HET ACY B1216 4
HET Y7N B1217 31
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM ACY ACETIC ACID
HETNAM Y7N 5-[(E)-[(2S)-2-(6-AZANYLHEXANOYLAMINO)-2,3-
HETNAM 2 Y7N DIHYDROINDEN-1-YLIDENE]METHYL]-1,3-BENZODIOXOLE-4-
HETNAM 3 Y7N CARBOXYLIC ACID
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 7 CL 2(CL 1-)
FORMUL 8 ACY 4(C2 H4 O2)
FORMUL 9 Y7N 2(C24 H26 N2 O5)
FORMUL 19 HOH *138(H2 O)
HELIX 1 1 THR A 93 TRP A 108 1 16
HELIX 2 2 ASN A 117 SER A 123 1 7
HELIX 3 3 SER A 123 GLY A 134 1 12
HELIX 4 4 PRO A 145 ARG A 166 1 22
HELIX 5 5 ASP A 167 ALA A 169 5 3
HELIX 6 6 HIS A 171 LYS A 186 1 16
HELIX 7 7 SER A 195 ILE A 208 1 14
HELIX 8 8 THR B 93 TRP B 108 1 16
HELIX 9 9 ASN B 117 SER B 123 1 7
HELIX 10 10 SER B 123 GLY B 134 1 12
HELIX 11 11 PRO B 145 ARG B 166 1 22
HELIX 12 12 ASP B 167 ALA B 169 5 3
HELIX 13 13 HIS B 171 LYS B 186 1 16
HELIX 14 14 SER B 195 ILE B 208 1 14
SHEET 1 AA 5 ILE A 84 ILE A 89 0
SHEET 2 AA 5 LYS A 71 HIS A 78 -1 O VAL A 72 N ILE A 89
SHEET 3 AA 5 ILE A 60 LEU A 68 -1 O GLN A 62 N VAL A 77
SHEET 4 AA 5 THR A 112 HIS A 114 1 O THR A 112 N TRP A 61
SHEET 5 AA 5 LYS A 136 GLU A 138 1 O LYS A 136 N VAL A 113
SHEET 1 BA 5 ILE B 84 ILE B 89 0
SHEET 2 BA 5 LYS B 71 HIS B 78 -1 O VAL B 72 N ILE B 89
SHEET 3 BA 5 ILE B 60 LEU B 68 -1 O GLN B 62 N VAL B 77
SHEET 4 BA 5 THR B 112 HIS B 114 1 O THR B 112 N TRP B 61
SHEET 5 BA 5 LYS B 136 GLU B 138 1 O LYS B 136 N VAL B 113
SITE 1 AC1 6 THR B 66 HIS B 67 LYS B 111 LYS B 136
SITE 2 AC1 6 LYS B 159 HOH B2038
SITE 1 AC2 5 THR A 66 HIS A 67 LYS A 111 LYS A 159
SITE 2 AC2 5 HOH A2052
SITE 1 AC3 6 LYS B 71 ARG B 166 HIS B 171 LEU B 172
SITE 2 AC3 6 HOH B2007 HOH B2047
SITE 1 AC4 6 LYS A 71 ARG A 166 HIS A 171 LEU A 172
SITE 2 AC4 6 HOH A2008 HOH A2064
SITE 1 AC5 7 GLY B 94 SER B 123 THR B 124 THR B 125
SITE 2 AC5 7 HOH B2019 HOH B2020 HOH B2031
SITE 1 AC6 6 GLY A 94 SER A 123 THR A 124 THR A 125
SITE 2 AC6 6 HOH A2023 HOH A2045
SITE 1 AC7 5 GLU A 85 ALA A 86 PHE A 100 LYS A 103
SITE 2 AC7 5 ARG B 107
SITE 1 AC8 4 ARG A 107 GLU B 85 PHE B 100 LYS B 103
SITE 1 AC9 1 HIS A 185
SITE 1 BC1 1 HIS B 185
SITE 1 BC2 7 HOH A2013 HOH A2014 HOH A2065 HOH A2067
SITE 2 BC2 7 TYR B 99 LYS B 103 ACY B1215
SITE 1 BC3 6 TYR A 99 LYS A 103 HOH A2029 HOH A2079
SITE 2 BC3 6 ACY B1214 HOH B2009
SITE 1 BC4 2 LYS A 173 GLU B 96
SITE 1 BC5 4 GLU A 96 HOH A2078 LYS B 173 Y7N B1217
SITE 1 BC6 12 ASP A 167 GLN A 168 GLU A 170 HIS A 171
SITE 2 BC6 12 THR A 174 MET A 178 HOH A2063 HOH A2080
SITE 3 BC6 12 GLN B 95 TYR B 99 LEU B 102 ALA B 129
SITE 1 BC7 14 GLN A 95 TYR A 99 LEU A 102 ALA A 129
SITE 2 BC7 14 ACY A1214 HOH A2025 ASP B 167 GLN B 168
SITE 3 BC7 14 GLU B 170 HIS B 171 THR B 174 MET B 178
SITE 4 BC7 14 HOH B2045 HOH B2058
CRYST1 71.244 71.244 66.943 90.00 90.00 120.00 P 31 6
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 0.014036 0.008104 0.000000 0.00000
SCALE2 0.000000 0.016208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014938 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
