HEADER OXIDOREDUCTASE 09-FEB-06 2FZ9
TITLE HUMAN ALDOSE REDUCTASE COMPLEXED WITH INHIBITOR ZOPOLRESTAT AFTER SIX
TITLE 2 DAYS SOAKING.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.21;
COMPND 5 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: ALDR1;
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: PET 15B
KEYWDS TIM BARREL, BACKBONE FLIP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.STEUBER,M.ZENTGRAF,C.GERLACH,C.A.SOTRIFFER,A.HEINE,G.KLEBE
REVDAT 5 30-AUG-23 2FZ9 1 REMARK
REVDAT 4 31-JAN-18 2FZ9 1 REMARK
REVDAT 3 24-FEB-09 2FZ9 1 VERSN
REVDAT 2 07-NOV-06 2FZ9 1 JRNL
REVDAT 1 03-OCT-06 2FZ9 0
JRNL AUTH H.STEUBER,M.ZENTGRAF,C.GERLACH,C.A.SOTRIFFER,A.HEINE,G.KLEBE
JRNL TITL EXPECT THE UNEXPECTED OR CAVEAT FOR DRUG DESIGNERS: MULTIPLE
JRNL TITL 2 STRUCTURE DETERMINATIONS USING ALDOSE REDUCTASE CRYSTALS
JRNL TITL 3 TREATED UNDER VARYING SOAKING AND CO-CRYSTALLISATION
JRNL TITL 4 CONDITIONS.
JRNL REF J.MOL.BIOL. V. 363 174 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16952371
JRNL DOI 10.1016/J.JMB.2006.08.011
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 80.2
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) : 0.166
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.166
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1711
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 34430
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.153
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.153
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1444
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 27364
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2517
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 77
REMARK 3 SOLVENT ATOMS : 308
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2904.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 11767
REMARK 3 NUMBER OF RESTRAINTS : 10827
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 ANGLE DISTANCES (A) : 0.026
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.026
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.048
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.017
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.064
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 AND 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 4
REMARK 4 2FZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036489.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
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 : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35630
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.71000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AB INITIO
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 (%): 43.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM AMMONIUM CITRATE, 25 % PEG 6000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 5
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 33.55000
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 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. = 14.0 DEGREES
REMARK 500 ARG A 217 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 LEU A 288 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
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 LYS A 21 -1.03 84.48
REMARK 500 ASP A 134 38.54 -86.71
REMARK 500 LEU A 300 111.78 -164.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ZST LIGAND IS ALSO KNOWN AS ZOPOLRESTAT.
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 ZST A 600
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FZ8 RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH ZOPOLRESTAT AFTER 1 DAY
REMARK 900 SOAKING.
REMARK 900 RELATED ID: 1MAR RELATED DB: PDB
REMARK 900 HUMAN ALDOSE REDUCTASE COMPLEXED WITH INHIBITOR ZOPOLRESTAT
REMARK 900 RELATED ID: 2FZB RELATED DB: PDB
REMARK 900 RELATED ID: 2FZD RELATED DB: PDB
DBREF 2FZ9 A 0 315 UNP P15121 ALDR_HUMAN 1 316
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 ZST A 600 29
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM ZST 3,4-DIHYDRO-4-OXO-3-((5-TRIFLUOROMETHYL-2-
HETNAM 2 ZST BENZOTHIAZOLYL)METHYL)-1-PHTHALAZINE ACETIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 ZST C19 H12 F3 N3 O3 S
FORMUL 4 HOH *308(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 LEU A 87 LYS A 100 1 14
HELIX 7 7 ASN A 136 GLU A 150 1 15
HELIX 8 8 ASN A 162 ASN A 171 1 10
HELIX 9 9 GLN A 192 LYS A 202 1 11
HELIX 10 10 SER A 226 GLU A 229 5 4
HELIX 11 11 ASP A 230 ASN A 241 1 12
HELIX 12 12 THR A 243 GLN A 254 1 12
HELIX 13 13 THR A 265 LYS A 274 1 10
HELIX 14 14 SER A 281 SER A 290 1 10
HELIX 15 15 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 8 LEU A 17 GLY A 18 0
SHEET 2 B 8 HIS A 41 ASP A 43 1 O ASP A 43 N LEU A 17
SHEET 3 B 8 PHE A 73 LEU A 78 1 O VAL A 75 N ILE A 42
SHEET 4 B 8 LEU A 106 ILE A 109 1 O LEU A 108 N LEU A 78
SHEET 5 B 8 ILE A 156 SER A 159 1 O GLY A 157 N TYR A 107
SHEET 6 B 8 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 7 B 8 VAL A 205 TYR A 209 1 O THR A 207 N ILE A 184
SHEET 8 B 8 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 35 GLY A 18 THR A 19 TRP A 20 LYS A 21
SITE 2 AC1 35 ASP A 43 TYR A 48 HIS A 110 TRP A 111
SITE 3 AC1 35 SER A 159 ASN A 160 GLN A 183 TYR A 209
SITE 4 AC1 35 SER A 210 PRO A 211 LEU A 212 GLY A 213
SITE 5 AC1 35 SER A 214 PRO A 215 ASP A 216 ALA A 245
SITE 6 AC1 35 ILE A 260 PRO A 261 LYS A 262 SER A 263
SITE 7 AC1 35 VAL A 264 THR A 265 ARG A 268 GLU A 271
SITE 8 AC1 35 ASN A 272 ZST A 600 HOH A1100 HOH A1117
SITE 9 AC1 35 HOH A1140 HOH A1173 HOH A1229
SITE 1 AC2 15 TRP A 20 TYR A 48 HIS A 110 TRP A 111
SITE 2 AC2 15 THR A 113 PHE A 122 TRP A 219 CYS A 298
SITE 3 AC2 15 ALA A 299 LEU A 300 CYS A 303 TYR A 309
SITE 4 AC2 15 PRO A 310 NAP A 500 HOH A1174
CRYST1 49.450 67.100 47.300 90.00 92.43 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 0.020222 -0.000001 0.000858 0.00000
SCALE2 0.000000 0.014903 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
