HEADER HYDROLASE 19-JUL-07 2QNP
TITLE HIV-1 PROTEASE IN COMPLEX WITH A IODO DECORATED PYRROLIDINE-BASED
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG-POL POLYPROTEIN (PR160GAG-POL);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HIV-1 RETROPEPSIN;
COMPND 5 EC: 3.4.23.16;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 STRAIN: GAG-POL;
SOURCE 5 GENE: GAG-POL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS PROTEIN-LIGAND COMPLEX, AIDS, ASPARTYL PROTEASE, CAPSID MATURATION,
KEYWDS 2 CORE PROTEIN, CYTOPLASM, DNA INTEGRATION, DNA RECOMBINATION, DNA-
KEYWDS 3 DIRECTED DNA POLYMERASE, ENDONUCLEASE, HYDROLASE, LIPOPROTEIN,
KEYWDS 4 MAGNESIUM, MEMBRANE, METAL-BINDING, MULTIFUNCTIONAL ENZYME,
KEYWDS 5 MYRISTATE, NUCLEASE, NUCLEOTIDYLTRANSFERASE, PHOSPHORYLATION,
KEYWDS 6 PROTEASE, RNA-BINDING, RNA-DIRECTED DNA POLYMERASE, TRANSFERASE,
KEYWDS 7 VIRAL NUCLEOPROTEIN, VIRION, ZINC, ZINC-FINGER
EXPDTA X-RAY DIFFRACTION
AUTHOR J.BOETTCHER,A.BLUM,A.HEINE,W.E.DIEDERICH,G.KLEBE
REVDAT 6 13-MAR-24 2QNP 1 COMPND SOURCE
REVDAT 5 21-FEB-24 2QNP 1 REMARK
REVDAT 4 25-OCT-17 2QNP 1 REMARK
REVDAT 3 24-FEB-09 2QNP 1 VERSN
REVDAT 2 22-APR-08 2QNP 1 JRNL
REVDAT 1 15-APR-08 2QNP 0
JRNL AUTH A.BLUM,J.BOTTCHER,A.HEINE,G.KLEBE,W.E.DIEDERICH
JRNL TITL STRUCTURE-GUIDED DESIGN OF C2-SYMMETRIC HIV-1 PROTEASE
JRNL TITL 2 INHIBITORS BASED ON A PYRROLIDINE SCAFFOLD.
JRNL REF J.MED.CHEM. V. 51 2078 2008
JRNL REFN ISSN 0022-2623
JRNL PMID 18348517
JRNL DOI 10.1021/JM701142S
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 4.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.179
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.178
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2231
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 42541
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.176
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 36373
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 1713.7
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 1587.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 6939
REMARK 3 NUMBER OF RESTRAINTS : 6326
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.027
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.054
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.028
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.049
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000043827.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 196.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 WITH TWO SETS OF MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44939
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 5.00000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.33400
REMARK 200 R SYM FOR SHELL (I) : 33.4000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.830
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: HKL2MAP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M NACL, 0.1M BIS-TRIS, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 6.50
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 28.67800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.94950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.67800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.94950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2
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 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 B3168 LIES ON A SPECIAL POSITION.
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 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 65 CG CD OE1 OE2
REMARK 470 LYS B 55 CG CD CE NZ
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 A 57 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 41 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLN B 92 OE1 - CD - NE2 ANGL. DEV. = 16.4 DEGREES
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 CL B 2601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 2602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QN2 A 2501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PQZ RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH A PYRROLIDINE-BASED INHIBITOR
REMARK 900 RELATED ID: 2PWC RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH A AMINO DECORATED PYRROLIDINE-BASED
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2PWR RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH A CARBAMOYL DECORATED PYRROLIDINE-
REMARK 900 BASED INHIBITOR
REMARK 900 RELATED ID: 2QNN RELATED DB: PDB
REMARK 900 HIV-1 PROTEASE IN COMPLEX WITH A MULTIPLE DECORATED PYRROLIDINE-
REMARK 900 BASED INHIBITOR
REMARK 900 RELATED ID: 2QNQ RELATED DB: PDB
DBREF 2QNP A 1 99 UNP P03367 POL_HV1BR 501 599
DBREF 2QNP B 1 99 UNP P03367 POL_HV1BR 501 599
SEQRES 1 A 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 A 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 A 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 A 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 A 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 A 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 A 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 A 99 GLN ILE GLY CYS THR LEU ASN PHE
SEQRES 1 B 99 PRO GLN ILE THR LEU TRP GLN ARG PRO LEU VAL THR ILE
SEQRES 2 B 99 LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR
SEQRES 3 B 99 GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO
SEQRES 4 B 99 GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY
SEQRES 5 B 99 PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU
SEQRES 6 B 99 ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY
SEQRES 7 B 99 PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR
SEQRES 8 B 99 GLN ILE GLY CYS THR LEU ASN PHE
HET CL A2602 1
HET QN2 A2501 41
HET CL B2601 1
HET CL B2603 1
HETNAM CL CHLORIDE ION
HETNAM QN2 N,N'-(3S,4S)-PYRROLIDINE-3,4-DIYLBIS[N-(4-IODOBENZYL)
HETNAM 2 QN2 BENZENESULFONAMIDE]
FORMUL 3 CL 3(CL 1-)
FORMUL 4 QN2 C30 H29 I2 N3 O4 S2
FORMUL 7 HOH *183(H2 O)
HELIX 1 1 GLY A 86 THR A 91 1 6
HELIX 2 2 GLY B 86 ILE B 93 1 8
SHEET 1 A 4 GLN A 2 ILE A 3 0
SHEET 2 A 4 THR B 96 ASN B 98 -1 O LEU B 97 N ILE A 3
SHEET 3 A 4 THR A 96 ASN A 98 -1 N THR A 96 O ASN B 98
SHEET 4 A 4 GLN B 2 ILE B 3 -1 O ILE B 3 N LEU A 97
SHEET 1 B 8 TRP A 42 GLY A 49 0
SHEET 2 B 8 GLY A 52 ILE A 66 -1 O GLN A 58 N LYS A 43
SHEET 3 B 8 HIS A 69 VAL A 77 -1 O VAL A 75 N TYR A 59
SHEET 4 B 8 THR A 31 LEU A 33 1 N LEU A 33 O LEU A 76
SHEET 5 B 8 ILE A 84 ILE A 85 -1 O ILE A 84 N VAL A 32
SHEET 6 B 8 GLN A 18 LEU A 24 1 N LEU A 23 O ILE A 85
SHEET 7 B 8 LEU A 10 ILE A 15 -1 N ILE A 13 O LYS A 20
SHEET 8 B 8 GLY A 52 ILE A 66 -1 O GLU A 65 N LYS A 14
SHEET 1 C 8 LYS B 43 GLY B 49 0
SHEET 2 C 8 GLY B 52 ILE B 66 -1 O GLN B 58 N LYS B 43
SHEET 3 C 8 HIS B 69 VAL B 77 -1 O HIS B 69 N ILE B 66
SHEET 4 C 8 VAL B 32 LEU B 33 1 N LEU B 33 O LEU B 76
SHEET 5 C 8 ILE B 84 ILE B 85 -1 O ILE B 84 N VAL B 32
SHEET 6 C 8 GLN B 18 LEU B 24 1 N LEU B 23 O ILE B 85
SHEET 7 C 8 LEU B 10 ILE B 15 -1 N ILE B 13 O LYS B 20
SHEET 8 C 8 GLY B 52 ILE B 66 -1 O GLU B 65 N LYS B 14
SITE 1 AC1 3 THR B 74 ASN B 88 HOH B3105
SITE 1 AC2 4 GLY A 73 THR A 74 ASN A 88 ARG B 41
SITE 1 AC3 16 ASP A 25 GLY A 27 ALA A 28 ASP A 30
SITE 2 AC3 16 GLY A 48 GLY A 49 ILE A 50 ILE A 84
SITE 3 AC3 16 ASP B 25 GLY B 27 ALA B 28 GLY B 48
SITE 4 AC3 16 GLY B 49 ILE B 50 PRO B 81 ILE B 84
CRYST1 57.356 85.899 46.648 90.00 90.00 90.00 P 21 21 2 8
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 0.017435 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
