HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 10-DEC-12 4ICC
TITLE CRYSTAL STRUCTURE OF HUMAN AKR1B10 COMPLEXED WITH NADP+ AND JF0064
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDO-KETO REDUCTASE FAMILY 1 MEMBER B10;
COMPND 3 CHAIN: X;
COMPND 4 SYNONYM: ARL-1, ALDOSE REDUCTASE-LIKE, ALDOSE REDUCTASE-RELATED
COMPND 5 PROTEIN, ARP, HARP, SMALL INTESTINE REDUCTASE, SI REDUCTASE;
COMPND 6 EC: 1.1.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AKR1B10, AKR1B11;
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: PET30-XA/LIC
KEYWDS TIM BARREL, ALDO-KETO REDUCTASE, OXIDOREDUCTASE, HALOGENATED
KEYWDS 2 COMPOUND, CYTOSOLIC, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.COUSIDO-SIAH,F.X.RUIZ,A.MITSCHLER,S.PORTE,A.R.DE LERA,M.J.MARTIN,
AUTHOR 2 J.A.DE LA FUENTE,G.KLEBE,J.FARRES,X.PARES,A.PODJARNY
REVDAT 4 20-SEP-23 4ICC 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4ICC 1 REMARK
REVDAT 2 19-MAR-14 4ICC 1 JRNL
REVDAT 1 19-FEB-14 4ICC 0
JRNL AUTH A.COUSIDO-SIAH,F.X.RUIZ,A.MITSCHLER,S.PORTE,A.R.DE LERA,
JRNL AUTH 2 M.J.MARTIN,S.MANZANARO,J.A.DE LA FUENTE,F.TERWESTEN,M.BETZ,
JRNL AUTH 3 G.KLEBE,J.FARRES,X.PARES,A.PODJARNY
JRNL TITL IDENTIFICATION OF A NOVEL POLYFLUORINATED COMPOUND AS A LEAD
JRNL TITL 2 TO INHIBIT THE HUMAN ENZYMES ALDOSE REDUCTASE AND AKR1B10:
JRNL TITL 3 STRUCTURE DETERMINATION OF BOTH TERNARY COMPLEXES AND
JRNL TITL 4 IMPLICATIONS FOR DRUG DESIGN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 889 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24598757
JRNL DOI 10.1107/S1399004713033452
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 1754
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 23.5677 - 4.1117 1.00 2615 133 0.1499 0.1678
REMARK 3 2 4.1117 - 3.2664 1.00 2567 138 0.1615 0.1736
REMARK 3 3 3.2664 - 2.8543 1.00 2650 124 0.1846 0.1948
REMARK 3 4 2.8543 - 2.5937 1.00 2603 110 0.1846 0.1909
REMARK 3 5 2.5937 - 2.4080 1.00 2561 142 0.1835 0.2166
REMARK 3 6 2.4080 - 2.2661 1.00 2572 166 0.1609 0.2110
REMARK 3 7 2.2661 - 2.1527 1.00 2580 148 0.1628 0.2173
REMARK 3 8 2.1527 - 2.0591 1.00 2621 130 0.1467 0.1821
REMARK 3 9 2.0591 - 1.9798 1.00 2594 142 0.1493 0.2222
REMARK 3 10 1.9798 - 1.9116 1.00 2541 150 0.1423 0.1664
REMARK 3 11 1.9116 - 1.8518 1.00 2599 146 0.1393 0.1754
REMARK 3 12 1.8518 - 1.7989 0.98 2533 116 0.1309 0.1819
REMARK 3 13 1.7989 - 1.7516 0.97 2603 109 0.1476 0.1786
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.008 2823
REMARK 3 ANGLE : 1.305 3854
REMARK 3 CHIRALITY : 0.086 410
REMARK 3 PLANARITY : 0.007 484
REMARK 3 DIHEDRAL : 16.041 1074
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 4ICC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000076574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : DOUBLE MIRRORS MONOCHROMATOR
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35357
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1ZUA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 6000, 100 MM SODIUM
REMARK 280 CACODYLATE, PH 9, VAPOR DIFFUSION, HANGING 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 16.72467
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 33.44933
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ILE X 110 N CA C O CB CG1 CG2
REMARK 480 ILE X 110 CD1
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 X 10 -7.69 75.38
REMARK 500 HIS X 188 -178.64 -172.44
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 X 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 64I X 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZUA RELATED DB: PDB
REMARK 900 RELATED ID: 4ICF RELATED DB: PDB
REMARK 900 RELATED ID: 4IGS RELATED DB: PDB
REMARK 900 RELATED ID: 4ICE RELATED DB: PDB
DBREF 4ICC X 1 316 UNP O60218 AK1BA_HUMAN 1 316
SEQADV 4ICC ARG X 125 UNP O60218 LYS 125 ENGINEERED MUTATION
SEQADV 4ICC LEU X 301 UNP O60218 VAL 301 ENGINEERED MUTATION
SEQRES 1 X 316 MET ALA THR PHE VAL GLU LEU SER THR LYS ALA MLZ MET
SEQRES 2 X 316 PRO ILE VAL GLY LEU GLY THR TRP LYS SER PRO LEU GLY
SEQRES 3 X 316 MLY VAL MLZ GLU ALA VAL MLY VAL ALA ILE ASP ALA GLY
SEQRES 4 X 316 TYR ARG HIS ILE ASP CYS ALA TYR VAL TYR GLN ASN GLU
SEQRES 5 X 316 HIS GLU VAL GLY GLU ALA ILE GLN GLU MLZ ILE GLN GLU
SEQRES 6 X 316 MLY ALA VAL LYS ARG GLU ASP LEU PHE ILE VAL SER LYS
SEQRES 7 X 316 LEU TRP PRO THR PHE PHE GLU ARG PRO LEU VAL ARG LYS
SEQRES 8 X 316 ALA PHE GLU MLY THR LEU MLZ ASP LEU LYS LEU SER TYR
SEQRES 9 X 316 LEU ASP VAL TYR LEU ILE HIS TRP PRO GLN GLY PHE LYS
SEQRES 10 X 316 SER GLY ASP ASP LEU PHE PRO ARG ASP ASP LYS GLY ASN
SEQRES 11 X 316 ALA ILE GLY GLY LYS ALA THR PHE LEU ASP ALA TRP GLU
SEQRES 12 X 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL MLZ ALA
SEQRES 13 X 316 LEU GLY VAL SER ASN PHE SER HIS PHE GLN ILE GLU LYS
SEQRES 14 X 316 LEU LEU ASN LYS PRO GLY LEU MLZ TYR LYS PRO VAL THR
SEQRES 15 X 316 ASN GLN VAL GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 X 316 LEU ILE GLN TYR CYS HIS SER MLY GLY ILE THR VAL THR
SEQRES 17 X 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 X 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO MLZ ILE
SEQRES 19 X 316 LYS GLU ILE ALA ALA LYS HIS MLY MLZ THR ALA ALA GLN
SEQRES 20 X 316 VAL LEU ILE ARG PHE HIS ILE GLN ARG ASN VAL ILE VAL
SEQRES 21 X 316 ILE PRO MLY SER VAL THR PRO ALA ARG ILE VAL GLU ASN
SEQRES 22 X 316 ILE GLN VAL PHE ASP PHE LYS LEU SER ASP GLU GLU MET
SEQRES 23 X 316 ALA THR ILE LEU SER PHE ASN ARG ASN TRP ARG ALA CYS
SEQRES 24 X 316 ASN LEU LEU GLN SER SER HIS LEU GLU ASP TYR PRO PHE
SEQRES 25 X 316 ASN ALA GLU TYR
MODRES 4ICC MLZ X 12 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 27 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLZ X 29 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 33 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLZ X 62 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 66 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLY X 95 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLZ X 98 LYS N-METHYL-LYSINE
MODRES 4ICC MLZ X 155 LYS N-METHYL-LYSINE
MODRES 4ICC MLZ X 177 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 203 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLZ X 233 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 242 LYS N-DIMETHYL-LYSINE
MODRES 4ICC MLZ X 243 LYS N-METHYL-LYSINE
MODRES 4ICC MLY X 263 LYS N-DIMETHYL-LYSINE
HET MLZ X 12 10
HET MLY X 27 11
HET MLZ X 29 10
HET MLY X 33 11
HET MLZ X 62 10
HET MLY X 66 11
HET MLY X 95 11
HET MLZ X 98 10
HET MLZ X 155 10
HET MLZ X 177 10
HET MLY X 203 11
HET MLZ X 233 10
HET MLY X 242 11
HET MLZ X 243 10
HET MLY X 263 11
HET NAP X 401 48
HET 64I X 402 22
HETNAM MLZ N-METHYL-LYSINE
HETNAM MLY N-DIMETHYL-LYSINE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM 64I 2,2',3,3',5,5',6,6'-OCTAFLUOROBIPHENYL-4,4'-DIOL
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 1 MLZ 8(C7 H16 N2 O2)
FORMUL 1 MLY 7(C8 H18 N2 O2)
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 64I C12 H2 F8 O2
FORMUL 4 HOH *173(H2 O)
HELIX 1 1 MLY X 27 ALA X 38 1 12
HELIX 2 2 ALA X 46 GLN X 50 5 5
HELIX 3 3 ASN X 51 GLU X 65 1 15
HELIX 4 4 LYS X 69 LEU X 73 5 5
HELIX 5 5 GLU X 85 LYS X 101 1 17
HELIX 6 6 THR X 137 GLU X 151 1 15
HELIX 7 7 SER X 163 ASN X 172 1 10
HELIX 8 8 GLN X 193 MLY X 203 1 11
HELIX 9 9 ASP X 231 HIS X 241 1 11
HELIX 10 10 THR X 244 GLN X 255 1 12
HELIX 11 11 THR X 266 GLN X 275 1 10
HELIX 12 12 SER X 282 SER X 291 1 10
HELIX 13 13 LEU X 301 SER X 305 5 5
SHEET 1 A 2 PHE X 4 GLU X 6 0
SHEET 2 A 2 MLZ X 12 PRO X 14 -1 O MET X 13 N VAL X 5
SHEET 1 B 8 GLY X 17 LEU X 18 0
SHEET 2 B 8 HIS X 42 ASP X 44 1 O ASP X 44 N LEU X 18
SHEET 3 B 8 PHE X 74 LEU X 79 1 O VAL X 76 N ILE X 43
SHEET 4 B 8 LEU X 105 ILE X 110 1 O LEU X 109 N LEU X 79
SHEET 5 B 8 VAL X 154 SER X 160 1 O MLZ X 155 N LEU X 105
SHEET 6 B 8 THR X 182 GLU X 186 1 O THR X 182 N VAL X 159
SHEET 7 B 8 THR X 206 TYR X 210 1 O TYR X 210 N VAL X 185
SHEET 8 B 8 ILE X 259 VAL X 260 1 O ILE X 259 N ALA X 209
LINK C ALA X 11 N MLZ X 12 1555 1555 1.34
LINK C MLZ X 12 N MET X 13 1555 1555 1.33
LINK C GLY X 26 N MLY X 27 1555 1555 1.33
LINK C MLY X 27 N VAL X 28 1555 1555 1.33
LINK C VAL X 28 N MLZ X 29 1555 1555 1.33
LINK C MLZ X 29 N GLU X 30 1555 1555 1.34
LINK C VAL X 32 N MLY X 33 1555 1555 1.33
LINK C MLY X 33 N VAL X 34 1555 1555 1.33
LINK C GLU X 61 N MLZ X 62 1555 1555 1.33
LINK C MLZ X 62 N ILE X 63 1555 1555 1.33
LINK C AGLU X 65 N MLY X 66 1555 1555 1.33
LINK C BGLU X 65 N MLY X 66 1555 1555 1.33
LINK C MLY X 66 N ALA X 67 1555 1555 1.33
LINK C GLU X 94 N MLY X 95 1555 1555 1.33
LINK C MLY X 95 N THR X 96 1555 1555 1.34
LINK C LEU X 97 N MLZ X 98 1555 1555 1.33
LINK C MLZ X 98 N ASP X 99 1555 1555 1.34
LINK C VAL X 154 N MLZ X 155 1555 1555 1.33
LINK C MLZ X 155 N ALA X 156 1555 1555 1.33
LINK C LEU X 176 N MLZ X 177 1555 1555 1.33
LINK C MLZ X 177 N TYR X 178 1555 1555 1.33
LINK C SER X 202 N MLY X 203 1555 1555 1.33
LINK C MLY X 203 N GLY X 204 1555 1555 1.33
LINK C PRO X 232 N MLZ X 233 1555 1555 1.31
LINK C MLZ X 233 N ILE X 234 1555 1555 1.30
LINK C HIS X 241 N MLY X 242 1555 1555 1.33
LINK C MLY X 242 N MLZ X 243 1555 1555 1.34
LINK C MLZ X 243 N THR X 244 1555 1555 1.33
LINK C PRO X 262 N MLY X 263 1555 1555 1.34
LINK C MLY X 263 N SER X 264 1555 1555 1.33
SITE 1 AC1 36 GLY X 19 THR X 20 TRP X 21 ASP X 44
SITE 2 AC1 36 TYR X 49 LYS X 78 HIS X 111 SER X 160
SITE 3 AC1 36 ASN X 161 GLN X 184 TYR X 210 SER X 211
SITE 4 AC1 36 PRO X 212 LEU X 213 GLY X 214 SER X 215
SITE 5 AC1 36 PRO X 216 ASP X 217 LEU X 229 ALA X 246
SITE 6 AC1 36 ILE X 261 PRO X 262 MLY X 263 SER X 264
SITE 7 AC1 36 VAL X 265 THR X 266 ARG X 269 GLU X 272
SITE 8 AC1 36 ASN X 273 64I X 402 HOH X 526 HOH X 579
SITE 9 AC1 36 HOH X 580 HOH X 582 HOH X 591 HOH X 661
SITE 1 AC2 11 TRP X 21 TYR X 49 TRP X 80 HIS X 111
SITE 2 AC2 11 TRP X 112 TRP X 220 CYS X 299 ASN X 300
SITE 3 AC2 11 LEU X 301 NAP X 401 HOH X 620
CRYST1 79.345 79.345 50.174 90.00 90.00 120.00 P 31 3
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 0.012603 0.007276 0.000000 0.00000
SCALE2 0.000000 0.014553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019931 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
