HEADER OXIDOREDUCTASE 12-NOV-06 2NVD
TITLE HUMAN ALDOSE REDUCTASE COMPLEXED WITH NOVEL NAPHTHO[1,2-D]ISOTHIAZOLE
TITLE 2 ACETIC ACID DERIVATIVE (2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AR, ALDEHYDE REDUCTASE;
COMPND 5 EC: 1.1.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HALR2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ALDOSE REDUCTASE, TIM-BARREL, PROTEIN-LIGAND COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.STEUBER,A.HEINE,G.KLEBE
REVDAT 4 25-OCT-23 2NVD 1 REMARK
REVDAT 3 24-FEB-09 2NVD 1 VERSN
REVDAT 2 15-MAY-07 2NVD 1 JRNL
REVDAT 1 24-APR-07 2NVD 0
JRNL AUTH H.STEUBER,M.ZENTGRAF,C.LA MOTTA,S.SARTINI,A.HEINE,G.KLEBE
JRNL TITL EVIDENCE FOR A NOVEL BINDING SITE CONFORMER OF ALDOSE
JRNL TITL 2 REDUCTASE IN LIGAND-BOUND STATE
JRNL REF J.MOL.BIOL. V. 369 186 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17418233
JRNL DOI 10.1016/J.JMB.2007.03.021
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.6
REMARK 3 CROSS-VALIDATION METHOD : FREE R
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) : 0.192
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.130
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2087
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 33994
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.187
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.128
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1935
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 36809
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2508
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 117
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2850.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2521.0
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 15
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 26284
REMARK 3 NUMBER OF RESTRAINTS : 31907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 2.300
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.025
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.056
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.064
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.035
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.003
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.057
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: ANISOTROPIC SCALING APPLIED BY THE
REMARK 3 METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
REMARK 3 ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY ?
REMARK 4
REMARK 4 2NVD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040347.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42162
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : 0.03500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 39.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.16900
REMARK 200 R SYM FOR SHELL (I) : 0.16900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1EL3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 120MM AMMONIUM CITRATE, 20% PEG 6000,
REMARK 280 PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 33.32000
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 0
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 TRP A 219 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 219 CZ3 CH2
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 TYR A 209 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 TYR A 209 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 GLN A 283 CG - CD - OE1 ANGL. DEV. = 16.9 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 NAP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITB A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITB A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ITB A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FZD RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH TOLRESTAT AT 1.08 A
REMARK 900 RESOLUTION.
REMARK 900 RELATED ID: 2NVC RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH NOVEL NAPHTHO[1,2-D]
REMARK 900 ISOTHIAZOLE ACETIC ACID DERIVATIVE (3)
DBREF 2NVD A 0 315 UNP P15121 ALDR_HUMAN 0 315
SEQADV 2NVD ILE A 4 UNP P15121 LEU 4 SEE REMARK 999
SEQRES 1 A 316 MET ALA SER ARG ILE LEU LEU ASN ASN GLY ALA LYS MET
SEQRES 2 A 316 PRO ILE LEU GLY LEU GLY THR TRP LYS SER PRO PRO GLY
SEQRES 3 A 316 GLN VAL THR GLU ALA VAL LYS VAL ALA ILE ASP VAL GLY
SEQRES 4 A 316 TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR GLN ASN GLU
SEQRES 5 A 316 ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS LEU ARG GLU
SEQRES 6 A 316 GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE VAL SER LYS
SEQRES 7 A 316 LEU TRP CYS THR TYR HIS GLU LYS GLY LEU VAL LYS GLY
SEQRES 8 A 316 ALA CYS GLN LYS THR LEU SER ASP LEU LYS LEU ASP TYR
SEQRES 9 A 316 LEU ASP LEU TYR LEU ILE HIS TRP PRO THR GLY PHE LYS
SEQRES 10 A 316 PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU SER GLY ASN
SEQRES 11 A 316 VAL VAL PRO SER ASP THR ASN ILE LEU ASP THR TRP ALA
SEQRES 12 A 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL LYS ALA
SEQRES 13 A 316 ILE GLY ILE SER ASN PHE ASN HIS LEU GLN VAL GLU MET
SEQRES 14 A 316 ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO ALA VAL
SEQRES 15 A 316 ASN GLN ILE GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 A 316 LEU ILE GLN TYR CYS GLN SER LYS GLY ILE VAL VAL THR
SEQRES 17 A 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 A 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO ARG ILE
SEQRES 19 A 316 LYS ALA ILE ALA ALA LYS HIS ASN LYS THR THR ALA GLN
SEQRES 20 A 316 VAL LEU ILE ARG PHE PRO MET GLN ARG ASN LEU VAL VAL
SEQRES 21 A 316 ILE PRO LYS SER VAL THR PRO GLU ARG ILE ALA GLU ASN
SEQRES 22 A 316 PHE LYS VAL PHE ASP PHE GLU LEU SER SER GLN ASP MET
SEQRES 23 A 316 THR THR LEU LEU SER TYR ASN ARG ASN TRP ARG VAL CYS
SEQRES 24 A 316 ALA LEU LEU SER CYS THR SER HIS LYS ASP TYR PRO PHE
SEQRES 25 A 316 HIS GLU GLU PHE
HET NAP A 500 48
HET ITB A 600 23
HET ITB A 700 23
HET ITB A 800 23
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM ITB 2-(CARBOXYMETHYL)-1-OXO-1,2-DIHYDRONAPHTHO[1,2-
HETNAM 2 ITB D]ISOTHIAZOLE-4-CARBOXYLIC ACID 3,3-DIOXIDE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN ITB 2-CARBOXYMETHYL-1,3,3-TRIOXO-1,2-DIHYDRONAPHTHO[1,2-
HETSYN 2 ITB D]ISOTHIAZOLE-4-CARBOXYLIC ACID
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 ITB 3(C14 H9 N O7 S)
FORMUL 6 HOH *214(H2 O)
HELIX 1 1 PRO A 23 GLY A 38 1 16
HELIX 2 2 ALA A 45 GLN A 49 5 5
HELIX 3 3 ASN A 50 GLU A 64 1 15
HELIX 4 4 LYS A 68 LEU A 72 5 5
HELIX 5 5 TRP A 79 HIS A 83 5 5
HELIX 6 6 GLU A 84 GLY A 86 5 3
HELIX 7 7 LEU A 87 LYS A 100 1 14
HELIX 8 8 ASN A 136 GLU A 150 1 15
HELIX 9 9 ASN A 162 ASN A 171 1 10
HELIX 10 10 GLN A 192 LYS A 202 1 11
HELIX 11 11 SER A 226 GLU A 229 5 4
HELIX 12 12 ASP A 230 ASN A 241 1 12
HELIX 13 13 THR A 243 GLN A 254 1 12
HELIX 14 14 THR A 265 LYS A 274 1 10
HELIX 15 15 SER A 281 SER A 290 1 10
HELIX 16 16 LEU A 300 THR A 304 5 5
SHEET 1 A 2 ARG A 3 LEU A 5 0
SHEET 2 A 2 LYS A 11 PRO A 13 -1 O MET A 12 N ILE A 4
SHEET 1 B 7 HIS A 41 ASP A 43 0
SHEET 2 B 7 PHE A 73 LEU A 78 1 O VAL A 75 N ILE A 42
SHEET 3 B 7 LEU A 106 ILE A 109 1 O LEU A 108 N LEU A 78
SHEET 4 B 7 ILE A 156 SER A 159 1 O GLY A 157 N TYR A 107
SHEET 5 B 7 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 6 B 7 VAL A 205 TYR A 209 1 O TYR A 209 N ILE A 184
SHEET 7 B 7 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 31 GLY A 18 THR A 19 TRP A 20 ASP A 43
SITE 2 AC1 31 TYR A 48 HIS A 110 SER A 159 ASN A 160
SITE 3 AC1 31 GLN A 183 TYR A 209 SER A 210 PRO A 211
SITE 4 AC1 31 LEU A 212 GLY A 213 SER A 214 PRO A 215
SITE 5 AC1 31 ASP A 216 ALA A 245 ILE A 260 PRO A 261
SITE 6 AC1 31 LYS A 262 SER A 263 VAL A 264 THR A 265
SITE 7 AC1 31 ARG A 268 GLU A 271 ASN A 272 ITB A 600
SITE 8 AC1 31 HOH A1021 HOH A1085 HOH A1147
SITE 1 AC2 11 TRP A 20 VAL A 47 TYR A 48 HIS A 110
SITE 2 AC2 11 TRP A 111 SER A 214 ARG A 217 VAL A 297
SITE 3 AC2 11 CYS A 298 NAP A 500 HOH A1063
SITE 1 AC3 10 SER A 2 ARG A 3 LYS A 11 ARG A 40
SITE 2 AC3 10 GLU A 70 GLU A 71 LYS A 307 ITB A 800
SITE 3 AC3 10 HOH A1058 HOH A1100
SITE 1 AC4 5 LYS A 68 GLU A 70 GLU A 71 ITB A 700
SITE 2 AC4 5 HOH A1193
CRYST1 49.390 66.640 47.140 90.00 91.88 90.00 P 1 21 1 2
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 0.020247 0.000000 0.000665 0.00000
SCALE2 0.000000 0.015006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021225 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
