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HEADER NON-VERTEBRATE HEMOGLOBIN 02-MAR-01 1H97 TITLE TREMATODE HEMOGLOBIN FROM PARAMPHISTOMUM EPICLITUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLOBIN-3; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MYOGLOBIN, HEMOGLOBIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PARAMPHISTOMUM EPICLITUM; SOURCE 3 CELLULAR_LOCATION: CYTOPLASM; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)PLYSS; SOURCE 6 EXPRESSION_SYSTEM_VECTOR: PET3A KEYWDS NON-VERTEBRATE HEMOGLOBIN EXPDTA X-RAY DIFFRACTION AUTHOR A.PESCE,S.DEWILDE,L.KIGER,M.MILANI,P.ASCENZI,M.C.MARDEN, AUTHOR 2 M.L.VAN HAUWAERT,J.VANFLETEREN,L.MOENS,M.BOLOGNESI REVDAT 2 01-APR-03 1H97 1 JRNL REVDAT 1 21-JUN-01 1H97 0 JRNL AUTH A.PESCE,S.DEWILDE,L.KIGER,M.MILANI,P.ASCENZI, JRNL AUTH 2 M.C.MARDEN,M.L.VAN HAUWAERT,J.VANFLETEREN,L.MOENS, JRNL AUTH 3 M.BOLOGNESI JRNL TITL VERY HIGH RESOLUTION STRUCTURE OF A TREMATODE JRNL TITL 2 HEMOGLOBIN DISPLAYING A TYRB10-TYRE7 HEME DISTAL JRNL TITL 3 RESIDUE PAIR AND HIGH OXYGEN AFFINITY. JRNL REF J.MOL.BIOL. V. 309 1153 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.17 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) : 1.17 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.5 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) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.121 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.173 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 5650 REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 56502 REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F). REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL 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)) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2343 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 106 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 MODEL REFINEMENT. REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 12 REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL REMARK 3 NUMBER OF RESTRAINTS : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES. REMARK 3 BOND LENGTHS (A) : 0.014 REMARK 3 ANGLE DISTANCES (A) : 0.031 REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL 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: NULL REMARK 4 REMARK 4 1H97 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-5964 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 4.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG REMARK 200 BEAMLINE : X31 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0, 1.74 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IP REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106124 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.170 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.5 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.05100 REMARK 200 R SYM (I) : 0.05100 REMARK 200 FOR THE DATA SET : 17.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.17 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.19 REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.00 REMARK 200 R MERGE FOR SHELL (I) : 0.34300 REMARK 200 R SYM FOR SHELL (I) : 0.34300 REMARK 200 FOR SHELL : 3.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 48.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 19.35000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.30000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.85000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.30000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.35000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.85000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, W 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 LYS A 124 CG CD CE NZ REMARK 470 GLN B 41 CG CD OE1 NE2 REMARK 470 LYS B 124 CG CD CE NZ 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 REMARK 500 OG SER B 82 O HOH W 186 2.16 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 NE2 GLN A 59 OE2 GLU B 61 4455 0.95 REMARK 500 NE2 GLN A 59 CD GLU B 61 4455 1.73 REMARK 500 O HOH W 319 O HOH W 516 3755 1.73 REMARK 500 CD GLN A 59 OE2 GLU B 61 4455 2.08 REMARK 500 O HOH W 113 O HOH W 180 3745 2.12 REMARK 500 O HOH W 70 O HOH W 215 3745 2.15 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 LYS A 64 CD LYS A 64 CE 0.277 REMARK 500 LYS A 117 CD LYS A 117 CE -0.160 REMARK 500 ILE B 9 CG1 ILE B 9 CD1 -0.144 REMARK 500 GLU B 50 CB GLU B 50 CG -0.169 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLU B 61 OE1 - CD - OE2 ANGL. DEV. =-15.2 DEGREES REMARK 500 LYS B 88 CD - CE - NZ ANGL. DEV. = 19.7 DEGREES REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: HEA REMARK 800 SITE_DESCRIPTION: HEM BINDING SITE FOR CHAIN A REMARK 800 SITE_IDENTIFIER: HEB REMARK 800 SITE_DESCRIPTION: HEM BINDING SITE FOR CHAIN B DBREF 1H97 A 1 147 UNP P80721 GLB_PAREP 1 147 DBREF 1H97 B 1 147 UNP P80721 GLB_PAREP 1 147 SEQADV 1H97 SER A 44 UNP P80721 ILE 44 DIFFERENT ISOFORM SEQADV 1H97 SER B 44 UNP P80721 ILE 44 DIFFERENT ISOFORM SEQRES 1 A 147 THR LEU THR LYS HIS GLU GLN ASP ILE LEU LEU LYS GLU SEQRES 2 A 147 LEU GLY PRO HIS VAL ASP THR PRO ALA HIS ILE VAL GLU SEQRES 3 A 147 THR GLY LEU GLY ALA TYR HIS ALA LEU PHE THR ALA HIS SEQRES 4 A 147 PRO GLN TYR ILE SER HIS PHE SER ARG LEU GLU GLY HIS SEQRES 5 A 147 THR ILE GLU ASN VAL MET GLN SER GLU GLY ILE LYS HIS SEQRES 6 A 147 TYR ALA ARG THR LEU THR GLU ALA ILE VAL HIS MET LEU SEQRES 7 A 147 LYS GLU ILE SER ASN ASP ALA GLU VAL LYS LYS ILE ALA SEQRES 8 A 147 ALA GLN TYR GLY LYS ASP HIS THR SER ARG LYS VAL THR SEQRES 9 A 147 LYS ASP GLU PHE MET SER GLY GLU PRO ILE PHE THR LYS SEQRES 10 A 147 TYR PHE GLN ASN LEU VAL LYS ASP ALA GLU GLY LYS ALA SEQRES 11 A 147 ALA VAL GLU LYS PHE LEU LYS HIS VAL PHE PRO MET MET SEQRES 12 A 147 ALA ALA GLU ILE SEQRES 1 B 147 THR LEU THR LYS HIS GLU GLN ASP ILE LEU LEU LYS GLU SEQRES 2 B 147 LEU GLY PRO HIS VAL ASP THR PRO ALA HIS ILE VAL GLU SEQRES 3 B 147 THR GLY LEU GLY ALA TYR HIS ALA LEU PHE THR ALA HIS SEQRES 4 B 147 PRO GLN TYR ILE SER HIS PHE SER ARG LEU GLU GLY HIS SEQRES 5 B 147 THR ILE GLU ASN VAL MET GLN SER GLU GLY ILE LYS HIS SEQRES 6 B 147 TYR ALA ARG THR LEU THR GLU ALA ILE VAL HIS MET LEU SEQRES 7 B 147 LYS GLU ILE SER ASN ASP ALA GLU VAL LYS LYS ILE ALA SEQRES 8 B 147 ALA GLN TYR GLY LYS ASP HIS THR SER ARG LYS VAL THR SEQRES 9 B 147 LYS ASP GLU PHE MET SER GLY GLU PRO ILE PHE THR LYS SEQRES 10 B 147 TYR PHE GLN ASN LEU VAL LYS ASP ALA GLU GLY LYS ALA SEQRES 11 B 147 ALA VAL GLU LYS PHE LEU LYS HIS VAL PHE PRO MET MET SEQRES 12 B 147 ALA ALA GLU ILE HET SO4 A1148 5 HET SO4 B1148 5 HET SO4 B1149 5 HET SO4 B1150 5 HET HEM A 148 43 HET HEM B 148 43 HETNAM SO4 SULFATE ION HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 HEM 2(C34 H32 FE N4 O4) FORMUL 9 HOH *342(H2 O) HELIX 1 1 THR A 3 GLY A 15 1 13 HELIX 2 2 PRO A 16 VAL A 18 5 3 HELIX 3 3 THR A 20 HIS A 39 1 20 HELIX 4 4 PRO A 40 GLU A 50 5 11 HELIX 5 5 ASN A 56 GLN A 59 5 4 HELIX 6 6 SER A 60 LYS A 79 1 20 HELIX 7 7 ASN A 83 ASP A 97 1 15 HELIX 8 8 THR A 104 VAL A 123 1 20 HELIX 9 9 ASP A 125 ALA A 145 1 21 HELIX 10 10 THR B 3 GLY B 15 1 13 HELIX 11 11 PRO B 16 VAL B 18 5 3 HELIX 12 12 THR B 20 HIS B 39 1 20 HELIX 13 13 PRO B 40 GLU B 50 5 11 HELIX 14 14 ASN B 56 GLN B 59 5 4 HELIX 15 15 SER B 60 ILE B 81 1 22 HELIX 16 16 ASN B 83 ASP B 97 1 15 HELIX 17 17 THR B 104 VAL B 123 1 20 HELIX 18 18 ASP B 125 ALA B 145 1 21 LINK FE HEM A 148 NE2 HIS A 98 LINK FE HEM B 148 NE2 HIS B 98 SITE 1 HEA 16 TYR A 42 HIS A 45 PHE A 46 SER A 47 SITE 2 HEA 16 HIS A 65 TYR A 66 THR A 69 LEU A 70 SITE 3 HEA 16 HIS A 98 ARG A 101 PHE A 108 PHE A 140 SITE 4 HEA 16 MET A 143 HOH W 14 HOH W 28 HOH W 152 SITE 1 HEB 18 TYR B 42 HIS B 45 PHE B 46 SER B 47 SITE 2 HEB 18 THR B 69 LEU B 70 ASP B 97 HIS B 98 SITE 3 HEB 18 ARG B 101 PHE B 108 GLY B 111 PHE B 140 SITE 4 HEB 18 HOH W 30 HOH W 195 HOH W 208 HOH W 223 SITE 5 HEB 18 HOH W 239 HOH W 290 CRYST1 38.700 83.700 94.600 90.00 90.00 90.00 P 21 21 21 4 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 0.025840 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011947 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010571 0.00000 MTRIX1 1 0.996900 0.061480 -0.049100 8.61937 1 MTRIX2 1 0.055710 -0.110910 0.992270 18.82644 1 MTRIX3 1 0.055560 -0.991930 -0.113990 22.54264 1