HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-MAR-12 3VQE
TITLE HIV-1 IN CORE DOMAIN IN COMPLEX WITH [1-(4-FLUOROPHENYL)-5-METHYL-1H-
TITLE 2 PYRAZOL-4-YL]METHANOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POL POLYPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: INTEGRASE CORE DOMAIN, UNP RESIDUES 771-927;
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 STRAIN: NL43;
SOURCE 5 GENE: POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B+
KEYWDS RNASEH, DNA BINDING, DNA CLEAVAGE, DNA INTEGRATION, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.WIELENS,D.K.CHALMERS,M.W.PARKER,M.J.SCANLON
REVDAT 2 08-NOV-23 3VQE 1 REMARK SEQADV LINK
REVDAT 1 30-JAN-13 3VQE 0
JRNL AUTH J.WIELENS,S.J.HEADEY,D.I.RHODES,R.J.MULDER,O.DOLEZAL,
JRNL AUTH 2 J.J.DEADMAN,J.NEWMAN,D.K.CHALMERS,M.W.PARKER,T.S.PEAT,
JRNL AUTH 3 M.J.SCANLON
JRNL TITL PARALLEL SCREENING OF LOW MOLECULAR WEIGHT FRAGMENT
JRNL TITL 2 LIBRARIES: DO DIFFERENCES IN METHODOLOGY AFFECT HIT
JRNL TITL 3 IDENTIFICATION?
JRNL REF J BIOMOL SCREEN V. 18 147 2013
JRNL REFN ISSN 1087-0571
JRNL PMID 23139382
JRNL DOI 10.1177/1087057112465979
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_986)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 30890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1543
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.8292 - 3.7778 0.98 2629 137 0.2029 0.2143
REMARK 3 2 3.7778 - 2.9998 1.00 2701 142 0.1903 0.2204
REMARK 3 3 2.9998 - 2.6210 1.00 2661 140 0.1898 0.2009
REMARK 3 4 2.6210 - 2.3815 1.00 2664 140 0.1817 0.1845
REMARK 3 5 2.3815 - 2.2109 1.00 2696 142 0.1969 0.2571
REMARK 3 6 2.2109 - 2.0806 1.00 2656 140 0.1912 0.2126
REMARK 3 7 2.0806 - 1.9764 1.00 2640 139 0.1892 0.2358
REMARK 3 8 1.9764 - 1.8904 0.99 2710 143 0.2130 0.2496
REMARK 3 9 1.8904 - 1.8177 1.00 2648 139 0.2170 0.2537
REMARK 3 10 1.8177 - 1.7550 0.99 2670 141 0.2376 0.2532
REMARK 3 11 1.7550 - 1.7001 1.00 2672 140 0.2648 0.2988
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.40
REMARK 3 B_SOL : 41.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.530
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.37380
REMARK 3 B22 (A**2) : 0.37380
REMARK 3 B33 (A**2) : -0.74760
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 2185
REMARK 3 ANGLE : 1.495 2963
REMARK 3 CHIRALITY : 0.083 334
REMARK 3 PLANARITY : 0.006 371
REMARK 3 DIHEDRAL : 14.581 768
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3VQE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000095370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
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) : 0.9567
REMARK 200 MONOCHROMATOR : DOUBLE MIRROR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30896
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : 0.03300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.6800
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) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : 0.30800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.150
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: PDB ENTRY 3L3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMSO4, 0.1M NA CITRATE PH 4.6,
REMARK 280 50MM CDCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 68.82000
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 34.41000
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: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 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 SER A 56
REMARK 465 ASP A 139
REMARK 465 GLY A 140
REMARK 465 ILE A 141
REMARK 465 PRO A 142
REMARK 465 TYR A 143
REMARK 465 ASN A 144
REMARK 465 PRO A 145
REMARK 465 GLN A 146
REMARK 465 SER A 147
REMARK 465 GLN A 148
REMARK 465 GLY A 149
REMARK 465 VAL A 150
REMARK 465 ILE A 151
REMARK 465 GLU A 152
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 SER B 56
REMARK 465 ASP B 139
REMARK 465 GLY B 140
REMARK 465 ILE B 141
REMARK 465 PRO B 142
REMARK 465 TYR B 143
REMARK 465 ASN B 144
REMARK 465 PRO B 145
REMARK 465 GLN B 146
REMARK 465 SER B 147
REMARK 465 GLN B 148
REMARK 465 GLY B 149
REMARK 465 VAL B 150
REMARK 465 ILE B 151
REMARK 465 GLU B 152
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 GLN B 209
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 NH1 ARG B 187 OE1 GLU B 198 2.01
REMARK 500 OE1 GLU B 69 O HOH B 432 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 187 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1001 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 65 SG
REMARK 620 2 HIS A 67 NE2 116.0
REMARK 620 3 GLU A 92 OE1 103.4 94.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A1002 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 65 SG
REMARK 620 2 GLU A 92 OE2 90.5
REMARK 620 3 ASP A 116 OD2 104.1 161.3
REMARK 620 4 HOH A1106 O 165.9 81.3 82.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 301 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 65 SG
REMARK 620 2 HIS B 67 NE2 116.5
REMARK 620 3 GLU B 92 OE1 105.3 92.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD B 302 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 65 SG
REMARK 620 2 GLU B 92 OE2 89.4
REMARK 620 3 ASP B 116 OD2 104.2 159.0
REMARK 620 4 HOH B 403 O 166.5 82.2 81.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMQ A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMQ B 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L3U RELATED DB: PDB
REMARK 900 RELATED ID: 3L3V RELATED DB: PDB
REMARK 900 RELATED ID: 3OVN RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ4 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ5 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ6 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ7 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ8 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQ9 RELATED DB: PDB
REMARK 900 RELATED ID: 3VQA RELATED DB: PDB
REMARK 900 RELATED ID: 3VQB RELATED DB: PDB
REMARK 900 RELATED ID: 3VQC RELATED DB: PDB
REMARK 900 RELATED ID: 3VQD RELATED DB: PDB
REMARK 900 RELATED ID: 3VQP RELATED DB: PDB
REMARK 900 RELATED ID: 3VQQ RELATED DB: PDB
DBREF 3VQE A 56 212 UNP Q72498 Q72498_9HIV1 771 927
DBREF 3VQE B 56 212 UNP Q72498 Q72498_9HIV1 771 927
SEQADV 3VQE SER A 56 UNP Q72498 CYS 771 ENGINEERED MUTATION
SEQADV 3VQE GLY A 123 UNP Q72498 SER 838 ENGINEERED MUTATION
SEQADV 3VQE ALA A 124 UNP Q72498 THR 839 ENGINEERED MUTATION
SEQADV 3VQE ARG A 127 UNP Q72498 LYS 842 ENGINEERED MUTATION
SEQADV 3VQE ASP A 131 UNP Q72498 TRP 846 ENGINEERED MUTATION
SEQADV 3VQE ASP A 139 UNP Q72498 PHE 854 ENGINEERED MUTATION
SEQADV 3VQE HIS A 185 UNP Q72498 PHE 900 ENGINEERED MUTATION
SEQADV 3VQE SER B 56 UNP Q72498 CYS 771 ENGINEERED MUTATION
SEQADV 3VQE GLY B 123 UNP Q72498 SER 838 ENGINEERED MUTATION
SEQADV 3VQE ALA B 124 UNP Q72498 THR 839 ENGINEERED MUTATION
SEQADV 3VQE ARG B 127 UNP Q72498 LYS 842 ENGINEERED MUTATION
SEQADV 3VQE ASP B 131 UNP Q72498 TRP 846 ENGINEERED MUTATION
SEQADV 3VQE ASP B 139 UNP Q72498 PHE 854 ENGINEERED MUTATION
SEQADV 3VQE HIS B 185 UNP Q72498 PHE 900 ENGINEERED MUTATION
SEQRES 1 A 157 SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU
SEQRES 2 A 157 GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER
SEQRES 3 A 157 GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY
SEQRES 4 A 157 GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG
SEQRES 5 A 157 TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN
SEQRES 6 A 157 PHE THR GLY ALA THR VAL ARG ALA ALA CYS ASP TRP ALA
SEQRES 7 A 157 GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN
SEQRES 8 A 157 SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS
SEQRES 9 A 157 LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU
SEQRES 10 A 157 LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS
SEQRES 11 A 157 LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU
SEQRES 12 A 157 ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS
SEQRES 13 A 157 GLU
SEQRES 1 B 157 SER SER PRO GLY ILE TRP GLN LEU ASP CYS THR HIS LEU
SEQRES 2 B 157 GLU GLY LYS VAL ILE LEU VAL ALA VAL HIS VAL ALA SER
SEQRES 3 B 157 GLY TYR ILE GLU ALA GLU VAL ILE PRO ALA GLU THR GLY
SEQRES 4 B 157 GLN GLU THR ALA TYR PHE LEU LEU LYS LEU ALA GLY ARG
SEQRES 5 B 157 TRP PRO VAL LYS THR VAL HIS THR ASP ASN GLY SER ASN
SEQRES 6 B 157 PHE THR GLY ALA THR VAL ARG ALA ALA CYS ASP TRP ALA
SEQRES 7 B 157 GLY ILE LYS GLN GLU ASP GLY ILE PRO TYR ASN PRO GLN
SEQRES 8 B 157 SER GLN GLY VAL ILE GLU SER MET ASN LYS GLU LEU LYS
SEQRES 9 B 157 LYS ILE ILE GLY GLN VAL ARG ASP GLN ALA GLU HIS LEU
SEQRES 10 B 157 LYS THR ALA VAL GLN MET ALA VAL PHE ILE HIS ASN HIS
SEQRES 11 B 157 LYS ARG LYS GLY GLY ILE GLY GLY TYR SER ALA GLY GLU
SEQRES 12 B 157 ARG ILE VAL ASP ILE ILE ALA THR ASP ILE GLN THR LYS
SEQRES 13 B 157 GLU
HET CD A1001 1
HET CD A1002 1
HET CL A1003 1
HET SO4 A1004 5
HET SO4 A1005 5
HET FMQ A1006 15
HET CD B 301 1
HET CD B 302 1
HET CL B 303 1
HET SO4 B 304 5
HET SO4 B 305 5
HET FMQ B 306 15
HETNAM CD CADMIUM ION
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM FMQ [1-(4-FLUOROPHENYL)-5-METHYL-1H-PYRAZOL-4-YL]METHANOL
FORMUL 3 CD 4(CD 2+)
FORMUL 5 CL 2(CL 1-)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 8 FMQ 2(C11 H11 F N2 O)
FORMUL 15 HOH *77(H2 O)
HELIX 1 1 THR A 93 TRP A 108 1 16
HELIX 2 2 GLY A 118 THR A 122 5 5
HELIX 3 3 GLY A 123 GLY A 134 1 12
HELIX 4 4 MET A 154 ARG A 166 1 13
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 GLN A 209 1 15
HELIX 8 8 THR B 93 GLY B 106 1 14
HELIX 9 9 GLY B 118 THR B 122 5 5
HELIX 10 10 GLY B 123 GLY B 134 1 12
HELIX 11 11 MET B 154 ARG B 166 1 13
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 A 5 ILE A 84 ILE A 89 0
SHEET 2 A 5 LYS A 71 HIS A 78 -1 N ALA A 76 O GLU A 85
SHEET 3 A 5 ILE A 60 LEU A 68 -1 N GLN A 62 O VAL A 77
SHEET 4 A 5 THR A 112 HIS A 114 1 O HIS A 114 N LEU A 63
SHEET 5 A 5 LYS A 136 GLN A 137 1 O LYS A 136 N VAL A 113
SHEET 1 B 5 ILE B 84 ILE B 89 0
SHEET 2 B 5 LYS B 71 HIS B 78 -1 N ALA B 76 O GLU B 85
SHEET 3 B 5 ILE B 60 LEU B 68 -1 N GLN B 62 O VAL B 77
SHEET 4 B 5 THR B 112 HIS B 114 1 O HIS B 114 N LEU B 63
SHEET 5 B 5 LYS B 136 GLN B 137 1 O LYS B 136 N VAL B 113
LINK SG CYS A 65 CD CD A1001 1555 1555 2.53
LINK SG CYS A 65 CD CD A1002 1555 1555 2.57
LINK NE2 HIS A 67 CD CD A1001 1555 1555 2.23
LINK OE1 GLU A 92 CD CD A1001 1555 1555 2.16
LINK OE2 GLU A 92 CD CD A1002 1555 1555 2.57
LINK OD2 ASP A 116 CD CD A1002 1555 1555 2.37
LINK CD CD A1002 O HOH A1106 1555 1555 2.32
LINK SG CYS B 65 CD CD B 301 1555 1555 2.52
LINK SG CYS B 65 CD CD B 302 1555 1555 2.56
LINK NE2 HIS B 67 CD CD B 301 1555 1555 2.22
LINK OE1 GLU B 92 CD CD B 301 1555 1555 2.21
LINK OE2 GLU B 92 CD CD B 302 1555 1555 2.61
LINK OD2 ASP B 116 CD CD B 302 1555 1555 2.35
LINK CD CD B 302 O HOH B 403 1555 1555 2.36
SITE 1 AC1 4 CYS A 65 HIS A 67 GLU A 92 ASP B 131
SITE 1 AC2 6 CYS A 65 GLU A 92 ASP A 116 CL A1003
SITE 2 AC2 6 HOH A1106 HOH B 402
SITE 1 AC3 4 CYS A 65 ASP A 116 ASN A 120 CD A1002
SITE 1 AC4 6 LYS A 71 ARG A 166 GLU A 170 HIS A 171
SITE 2 AC4 6 LEU A 172 HOH A1126
SITE 1 AC5 4 THR A 66 HIS A 67 LYS A 159 ARG B 127
SITE 1 AC6 8 HIS A 185 ARG A 187 SER A 195 GLY A 197
SITE 2 AC6 8 GLU A 198 VAL A 201 PRO B 109 ILE B 204
SITE 1 AC7 4 ASP A 131 CYS B 65 HIS B 67 GLU B 92
SITE 1 AC8 6 HOH A1105 CYS B 65 GLU B 92 ASP B 116
SITE 2 AC8 6 CL B 303 HOH B 403
SITE 1 AC9 4 CYS B 65 ASP B 116 ASN B 120 CD B 302
SITE 1 BC1 7 LYS B 71 ARG B 166 GLU B 170 HIS B 171
SITE 2 BC1 7 LEU B 172 HOH B 419 HOH B 432
SITE 1 BC2 4 ARG A 127 THR B 66 HIS B 67 LYS B 159
SITE 1 BC3 10 PRO A 109 LYS A 111 ILE A 204 HIS B 185
SITE 2 BC3 10 ARG B 187 SER B 195 GLY B 197 GLU B 198
SITE 3 BC3 10 VAL B 201 HOH B 405
CRYST1 49.460 49.460 103.230 90.00 90.00 120.00 P 32 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 0.020218 0.011673 0.000000 0.00000
SCALE2 0.000000 0.023346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009687 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
