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HEADER OXYGEN TRANSPORT 06-MAY-93 1HDA TITLE A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF TITLE 2 BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE- TITLE 3 BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR TITLE 4 EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN (DEOXY) (ALPHA CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN (DEOXY) (BETA CHAIN); COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: BOS TAURUS KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR G.FERMI REVDAT 2 08-MAR-95 1HDA 1 HELIX REVDAT 1 31-MAY-94 1HDA 0 JRNL AUTH M.F.PERUTZ,G.FERMI,C.POYART,J.PAGNIER,J.KISTER JRNL TITL A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. JRNL TITL 2 STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF JRNL TITL 3 SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE JRNL TITL 4 CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN JRNL TITL 5 HAEMOGLOBIN. JRNL REF J.MOL.BIOL. V. 233 536 1993 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ, X-PLOR REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4386 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 42 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HDA 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 3.100 (2007-03-17) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 31.91000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.66000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.75500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.66000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.91000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.75500 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 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, B, C, D 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 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 OD1 ASP A 116 O HOH 776 2.10 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 NZ LYS B 120 OD1 ASP D 21 1655 2.13 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 ARG D 116 CD - NE - CZ ANGL. DEV. = 21.2 DEGREES DBREF 1HDA A 1 141 UNP P01966 HBA_BOVIN 1 141 DBREF 1HDA B 2 146 UNP P02070 HBB_BOVIN 1 145 DBREF 1HDA C 1 141 UNP P01966 HBA_BOVIN 1 141 DBREF 1HDA D 2 146 UNP P02070 HBB_BOVIN 1 145 SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER SEQRES 5 A 141 ALA GLN VAL LYS GLY HIS GLY ALA LYS VAL ALA ALA ALA SEQRES 6 A 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY SEQRES 7 A 141 ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER SEQRES 9 A 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 A 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE SEQRES 2 B 145 TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA SEQRES 3 B 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 B 145 PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA SEQRES 5 B 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS SEQRES 6 B 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP SEQRES 7 B 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS SEQRES 8 B 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU SEQRES 9 B 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE SEQRES 10 B 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN SEQRES 11 B 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG SEQRES 12 B 145 TYR HIS SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS GLY ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY GLY HIS ALA ALA GLU TYR GLY ALA SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR SEQRES 4 C 141 LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER SEQRES 5 C 141 ALA GLN VAL LYS GLY HIS GLY ALA LYS VAL ALA ALA ALA SEQRES 6 C 141 LEU THR LYS ALA VAL GLU HIS LEU ASP ASP LEU PRO GLY SEQRES 7 C 141 ALA LEU SER GLU LEU SER ASP LEU HIS ALA HIS LYS LEU SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS SER SEQRES 9 C 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO SER ASP PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA SEQRES 11 C 141 ASN VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR ALA PHE SEQRES 2 D 145 TRP GLY LYS VAL LYS VAL ASP GLU VAL GLY GLY GLU ALA SEQRES 3 D 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 D 145 PHE PHE GLU SER PHE GLY ASP LEU SER THR ALA ASP ALA SEQRES 5 D 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS LYS SEQRES 6 D 145 VAL LEU ASP SER PHE SER ASN GLY MET LYS HIS LEU ASP SEQRES 7 D 145 ASP LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU HIS SEQRES 8 D 145 CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS LEU SEQRES 9 D 145 LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG ASN PHE SEQRES 10 D 145 GLY LYS GLU PHE THR PRO VAL LEU GLN ALA ASP PHE GLN SEQRES 11 D 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS ARG SEQRES 12 D 145 TYR HIS HET HEM A 143 43 HET HEM B 148 43 HET HEM C 143 43 HET HEM D 148 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 9 HOH *42(H2 O) HELIX 1 AA1 SER A 3 GLY A 18 1 16 HELIX 2 AB1 HIS A 20 SER A 35 1 16 HELIX 3 AC1 PHE A 36 TYR A 42 1 7 HELIX 4 AE1 SER A 52 GLU A 71 1 20 HELIX 5 AF1 LEU A 80 ALA A 88 1 9 HELIX 6 AG1 ASP A 94 HIS A 112 1 19 HELIX 7 AH1 THR A 118 SER A 138 1 21 HELIX 8 BA1 THR B 4 VAL B 18 1 15 HELIX 9 BB1 LYS B 19 VAL B 34 1 16 HELIX 10 BC1 TYR B 35 PHE B 41 1 7 HELIX 11 BD1 THR B 50 ASN B 56 1 7 HELIX 12 BE1 ASN B 57 LYS B 76 1 20 HELIX 13 BF1 PHE B 85 CYS B 93 1 9 HELIX 14 BG1 ASP B 99 ASN B 117 1 19 HELIX 15 BH1 THR B 123 HIS B 143 1 21 HELIX 16 CA2 SER C 3 GLY C 18 1 16 HELIX 17 CB2 HIS C 20 SER C 35 1 16 HELIX 18 CC2 PHE C 36 TYR C 42 1 7 HELIX 19 CE2 SER C 52 GLU C 71 1 20 HELIX 20 CF2 LEU C 80 ALA C 88 1 9 HELIX 21 CG2 ASP C 94 HIS C 112 1 19 HELIX 22 CH2 THR C 118 SER C 138 1 21 HELIX 23 DA2 THR D 4 VAL D 18 1 15 HELIX 24 DB2 LYS D 19 VAL D 34 1 16 HELIX 25 DC2 TYR D 35 PHE D 41 1 7 HELIX 26 DD2 THR D 50 ASN D 56 1 7 HELIX 27 DE2 ASN D 57 LYS D 76 1 20 HELIX 28 DF2 PHE D 85 CYS D 93 1 9 HELIX 29 DG2 ASP D 99 ASN D 117 1 19 HELIX 30 DH2 THR D 123 HIS D 143 1 21 SITE 1 A1 1 HIS A 87 SITE 1 B1 1 HIS B 92 SITE 1 C1 1 HIS C 87 SITE 1 D1 1 HIS D 92 CRYST1 63.820 95.510 105.320 90.00 90.00 90.00 P 21 21 21 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 0.015669 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010470 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009495 0.00000 MTRIX1 1 -0.955772 0.281501 0.085119 23.80100 1 MTRIX2 1 0.281501 0.791944 0.541849 -7.12200 1 MTRIX3 1 0.085119 0.541849 -0.836165 11.18600 1