HEADER TRANSFERASE 21-NOV-13 4OVL
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 EC: 2.7.7.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: POL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS HIV INTEGRASE, STRUCTURE BASED DRUG DESIGN, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.S.PEAT
REVDAT 3 27-DEC-23 4OVL 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 2 1 CRYST1
REVDAT 2 01-OCT-14 4OVL 1 JRNL
REVDAT 1 05-MAR-14 4OVL 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 ESSN 1573-4951
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) : 45.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 40069
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2137
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) : 2922
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3280
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.3560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.10000
REMARK 3 B12 (A**2) : 0.03000
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): 0.104
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.949
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2571 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2470 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3508 ; 1.404 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5695 ; 0.753 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 326 ; 5.065 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 108 ;30.281 ;25.370
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 442 ;13.497 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ; 8.144 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2958 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 586 ; 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): 1232 ; 1.707 ; 3.329
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1224 ; 1.699 ; 3.316
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1534 ; 2.979 ; 5.568
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1535 ; 2.978 ; 5.572
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1339 ; 2.008 ; 3.777
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1339 ; 2.007 ; 3.777
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1959 ; 3.309 ; 6.224
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3022 ; 6.011 ;18.228
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3023 ; 6.010 ;18.231
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 57 209 B 57 209 8896 0.09 0.05
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
REMARK 4
REMARK 4 4OVL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000200029.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.95661
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42336
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
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 (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.75300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
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, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 22.45233
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 44.90467
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: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 GLY A 189
REMARK 465 GLY A 190
REMARK 465 ILE A 191
REMARK 465 GLY A 192
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 GLY B 189
REMARK 465 GLY B 190
REMARK 465 ILE B 191
REMARK 465 GLY B 192
REMARK 465 THR B 210
REMARK 465 LYS B 211
REMARK 465 GLU B 212
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O3 GOL A 309 O HOH A 461 1.98
REMARK 500 OE1 GLU A 87 OXT ACY B 306 2.18
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 PRO A 142 94.71 -65.50
REMARK 500 PRO B 142 94.44 -64.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1TD A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACY B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1TD B 308
DBREF 4OVL A 50 212 UNP Q76353 Q76353_9HIV1 50 212
DBREF 4OVL B 50 212 UNP Q76353 Q76353_9HIV1 50 212
SEQADV 4OVL MET A 30 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY A 31 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 32 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 33 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 34 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 35 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 36 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 37 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 38 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 39 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 40 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 41 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY A 42 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL LEU A 43 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL VAL A 44 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL PRO A 45 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL ARG A 46 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY A 47 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 48 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS A 49 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER A 56 UNP Q76353 CYS 56 ENGINEERED MUTATION
SEQADV 4OVL ASP A 139 UNP Q76353 PHE 139 ENGINEERED MUTATION
SEQADV 4OVL HIS A 185 UNP Q76353 PHE 185 ENGINEERED MUTATION
SEQADV 4OVL MET B 30 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY B 31 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 32 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 33 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 34 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 35 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 36 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 37 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 38 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 39 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 40 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 41 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY B 42 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL LEU B 43 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL VAL B 44 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL PRO B 45 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL ARG B 46 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL GLY B 47 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 48 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL HIS B 49 UNP Q76353 EXPRESSION TAG
SEQADV 4OVL SER B 56 UNP Q76353 CYS 56 ENGINEERED MUTATION
SEQADV 4OVL ASP B 139 UNP Q76353 PHE 139 ENGINEERED MUTATION
SEQADV 4OVL HIS B 185 UNP Q76353 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 A 301 5
HET SO4 A 302 5
HET ACY A 303 4
HET ACY A 304 4
HET ACY A 305 4
HET ACY A 306 4
HET ACY A 307 4
HET 1TD A 308 20
HET GOL A 309 6
HET SO4 B 301 5
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET EDO B 305 4
HET ACY B 306 4
HET ACY B 307 4
HET 1TD B 308 20
HETNAM SO4 SULFATE ION
HETNAM ACY ACETIC ACID
HETNAM 1TD 3-[(E)-(2-OXIDANYLIDENE-1H-INDOL-3-YLIDENE)
HETNAM 2 1TD METHYL]BENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 6(O4 S 2-)
FORMUL 5 ACY 7(C2 H4 O2)
FORMUL 10 1TD 2(C16 H11 N O3)
FORMUL 11 GOL C3 H8 O3
FORMUL 16 EDO C2 H6 O2
FORMUL 20 HOH *137(H2 O)
HELIX 1 AA1 THR A 93 TRP A 108 1 16
HELIX 2 AA2 ASN A 117 SER A 123 1 7
HELIX 3 AA3 SER A 123 GLY A 134 1 12
HELIX 4 AA4 PRO A 145 ARG A 166 1 22
HELIX 5 AA5 ASP A 167 ALA A 169 5 3
HELIX 6 AA6 HIS A 171 LYS A 186 1 16
HELIX 7 AA7 SER A 195 GLN A 209 1 15
HELIX 8 AA8 THR B 93 TRP B 108 1 16
HELIX 9 AA9 ASN B 117 SER B 123 1 7
HELIX 10 AB1 SER B 123 GLY B 134 1 12
HELIX 11 AB2 PRO B 145 ARG B 166 1 22
HELIX 12 AB3 ASP B 167 ALA B 169 5 3
HELIX 13 AB4 HIS B 171 LYS B 186 1 16
HELIX 14 AB5 SER B 195 GLN B 209 1 15
SHEET 1 AA1 5 ILE A 84 ILE A 89 0
SHEET 2 AA1 5 LYS A 71 HIS A 78 -1 N LEU A 74 O GLU A 87
SHEET 3 AA1 5 ILE A 60 LEU A 68 -1 N THR A 66 O ILE A 73
SHEET 4 AA1 5 THR A 112 HIS A 114 1 O HIS A 114 N LEU A 63
SHEET 5 AA1 5 LYS A 136 GLU A 138 1 O GLU A 138 N VAL A 113
SHEET 1 AA2 5 ILE B 84 ILE B 89 0
SHEET 2 AA2 5 LYS B 71 HIS B 78 -1 N ALA B 76 O GLU B 85
SHEET 3 AA2 5 ILE B 60 LEU B 68 -1 N ASP B 64 O VAL B 75
SHEET 4 AA2 5 THR B 112 HIS B 114 1 O HIS B 114 N LEU B 63
SHEET 5 AA2 5 LYS B 136 GLU B 138 1 O GLU B 138 N VAL B 113
SITE 1 AC1 6 THR A 66 HIS A 67 LYS A 111 LYS A 159
SITE 2 AC1 6 HOH A 458 HOH A 467
SITE 1 AC2 5 LYS A 71 HIS A 171 LEU A 172 HOH A 431
SITE 2 AC2 5 HOH A 469
SITE 1 AC3 8 TYR A 99 LYS A 103 HOH A 433 HOH A 468
SITE 2 AC3 8 GLU B 87 ACY B 306 HOH B 442 HOH B 453
SITE 1 AC4 9 ASN A 184 HIS A 185 ACY A 306 HOH A 435
SITE 2 AC4 9 ALA B 105 GLY B 106 ARG B 107 TRP B 108
SITE 3 AC4 9 PRO B 109
SITE 1 AC5 6 GLU A 85 GLU A 87 PHE A 100 LYS A 103
SITE 2 AC5 6 LEU A 104 ARG A 107
SITE 1 AC6 7 TRP A 108 GLY A 197 VAL A 201 ACY A 304
SITE 2 AC6 7 ARG B 107 TRP B 108 PRO B 109
SITE 1 AC7 8 GLY A 106 ARG A 107 TRP A 108 PRO A 109
SITE 2 AC7 8 ASN B 184 HIS B 185 ACY B 307 HOH B 438
SITE 1 AC8 11 ALA A 169 GLU A 170 HIS A 171 THR A 174
SITE 2 AC8 11 HOH A 406 GLN B 95 LEU B 102 THR B 125
SITE 3 AC8 11 ALA B 128 ALA B 129 TRP B 132
SITE 1 AC9 5 SER A 123 THR A 124 THR A 125 HOH A 461
SITE 2 AC9 5 HOH B 406
SITE 1 BC1 5 THR B 66 HIS B 67 LYS B 136 LYS B 159
SITE 2 BC1 5 HOH B 418
SITE 1 BC2 4 LYS B 71 HIS B 171 LEU B 172 HOH B 436
SITE 1 BC3 5 ARG A 107 GLU B 85 GLU B 87 PHE B 100
SITE 2 BC3 5 LYS B 103
SITE 1 BC4 7 GLY B 94 SER B 123 THR B 124 THR B 125
SITE 2 BC4 7 EDO B 305 HOH B 408 HOH B 462
SITE 1 BC5 6 SER B 119 SER B 123 SO4 B 304 HOH B 403
SITE 2 BC5 6 HOH B 440 HOH B 449
SITE 1 BC6 8 GLU A 87 ACY A 303 HOH A 428 HOH A 452
SITE 2 BC6 8 TYR B 99 LYS B 103 HOH B 433 HOH B 467
SITE 1 BC7 7 ARG A 107 TRP A 108 PRO A 109 ACY A 307
SITE 2 BC7 7 TRP B 108 GLY B 197 VAL B 201
SITE 1 BC8 10 GLN A 95 THR A 125 ALA A 128 ALA A 129
SITE 2 BC8 10 TRP A 132 ALA B 169 GLU B 170 HIS B 171
SITE 3 BC8 10 THR B 174 HOH B 411
CRYST1 71.492 71.492 67.357 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 0.013988 0.008076 0.000000 0.00000
SCALE2 0.000000 0.016151 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
