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HEADER OXYGEN STORAGE/TRANSPORT 21-JUL-04 1WMU TITLE CRYSTAL STRUCTURE OF HEMOGLOBIN D FROM THE ALDABRA GIANT TITLE 2 TORTOISE, GEOCHELONE GIGANTEA, AT 1.65 A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN D ALPHA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HEMOGLOBIN ALPHA-D CHAIN; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN A AND D BETA CHAIN; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: HEMOGLOBIN BETA CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ALDABRACHELYS ELEPHANTINA; SOURCE 3 ORGANISM_COMMON: ALDABRA GIANT TORTOISE; SOURCE 4 TISSUE: RED BLOOD CELL; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: ALDABRACHELYS ELEPHANTINA; SOURCE 7 ORGANISM_COMMON: ALDABRA GIANT TORTOISE; SOURCE 8 TISSUE: RED BLOOD CELL KEYWDS HEMOGLOBIN D, REPTILIA, THE ALDABRA GIANT TORTOISE, KEYWDS 2 GEOCHELONE GIGANTEA EXPDTA X-RAY DIFFRACTION AUTHOR T.KUWADA,T.HASEGAWA,I.SATOH,K.ISHIKAWA,F.SHISHIKURA REVDAT 1 03-AUG-04 1WMU 0 JRNL AUTH T.KUWADA,T.HASEGAWA,I.SATOH,K.ISHIKAWA,F.SHISHIKURA JRNL TITL CRYSTAL STRUCTURE OF HEMOGLOBIN D FROM THE ALDABRA JRNL TITL 2 GIANT TORTOISE, GEOCHELONE GIGANTEA, AT 1.65 A JRNL TITL 3 RESOLUTION JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.65 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNX 2000.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN,MOLECULAR REMARK 3 : SIMULATIONS (BADGER,BERARD,KUMAR,SZALMA, REMARK 3 : YIP,DZAKULA) REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.48 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1422458.080 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.6 REMARK 3 NUMBER OF REFLECTIONS : 39799 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.220 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 4000 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 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 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.00 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5699 REMARK 3 BIN R VALUE (WORKING SET) : 0.3650 REMARK 3 BIN FREE R VALUE : 0.3850 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 629 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2292 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 86 REMARK 3 SOLVENT ATOMS : 510 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.20 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.62000 REMARK 3 B22 (A**2) : 8.26000 REMARK 3 B33 (A**2) : -4.64000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.13000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21 REMARK 3 ESD FROM SIGMAA (A) : 0.20 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 16.40 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.70 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.32 REMARK 3 BSOL : 51.23 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : ION.PARAM REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : HEM.PARAM REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : ION.TOP REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : HEM.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WMU 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 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB023756. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-DEC-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 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 FR-E+ SUPERBRIGHT REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : CONFOCAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39802 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650 REMARK 200 RESOLUTION RANGE LOW (A) : 40.480 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7 REMARK 200 DATA REDUNDANCY : 7.390 REMARK 200 R MERGE (I) : 0.03100 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) : 1.65 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6 REMARK 200 DATA REDUNDANCY IN SHELL : 7.14 REMARK 200 R MERGE FOR SHELL (I) : 0.21100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 5.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: CNX 2000.1 REMARK 200 STARTING MODEL: PDB ENTRY 1V75 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM TRIS-HCL, PH 7.5, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 56.12200 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.06900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 56.12200 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.06900 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 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, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 112.24400 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 FE HEM A 201 O HOH 1 1.99 REMARK 500 FE HEM B 201 O HOH 2 2.01 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 ASP A 47 N - CA - C ANGL. DEV. =-15.0 DEGREES REMARK 500 ASN B 19 N - CA - C ANGL. DEV. =-10.7 DEGREES REMARK 500 PRO B 36 N - CA - C ANGL. DEV. = 9.5 DEGREES REMARK 500 SER B 49 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 256 DISTANCE = 5.22 ANGSTROMS REMARK 525 HOH 262 DISTANCE = 6.55 ANGSTROMS REMARK 525 HOH 331 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH 332 DISTANCE = 5.42 ANGSTROMS REMARK 525 HOH 368 DISTANCE = 8.38 ANGSTROMS REMARK 525 HOH 442 DISTANCE = 5.10 ANGSTROMS REMARK 525 HOH 444 DISTANCE = 6.68 ANGSTROMS REMARK 525 HOH 450 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 456 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 466 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH 492 DISTANCE = 6.10 ANGSTROMS REMARK 525 HOH 493 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH 500 DISTANCE = 6.45 ANGSTROMS REMARK 525 HOH 503 DISTANCE = 9.56 ANGSTROMS REMARK 525 HOH 505 DISTANCE = 6.54 ANGSTROMS REMARK 525 HOH 509 DISTANCE = 7.96 ANGSTROMS REMARK 525 HOH 510 DISTANCE = 7.14 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1V75 RELATED DB: PDB REMARK 900 THE SAME PROTEIN CRYSTALLIZED USING PRECIPITANT DBREF 1WMU A 1 141 UNP P83134 HBAD_ALDEL 1 141 DBREF 1WMU B 1 146 UNP P83133 HBB_ALDEL 1 146 SEQRES 1 A 141 MET LEU THR GLU ASP ASP LYS GLN LEU ILE GLN HIS VAL SEQRES 2 A 141 TRP GLU LYS VAL LEU GLU HIS GLN GLU ASP PHE GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE ILE VAL TYR PRO SER THR SEQRES 4 A 141 LYS THR TYR PHE PRO HIS PHE ASP LEU HIS HIS ASP SER SEQRES 5 A 141 GLU GLN ILE ARG HIS HIS GLY LYS LYS VAL VAL GLY ALA SEQRES 6 A 141 LEU GLY ASP ALA VAL LYS HIS ILE ASP ASN LEU SER ALA SEQRES 7 A 141 THR LEU SER GLU LEU SER ASN LEU HIS ALA TYR ASN LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 A 141 PHE GLN VAL VAL LEU GLY ALA HIS LEU GLY ARG GLU TYR SEQRES 10 A 141 THR PRO GLN VAL GLN VAL ALA TYR ASP LYS PHE LEU ALA SEQRES 11 A 141 ALA VAL SER ALA VAL LEU ALA GLU LYS TYR ARG SEQRES 1 B 146 VAL HIS TRP THR SER GLU GLU LYS GLN TYR ILE THR SER SEQRES 2 B 146 LEU TRP ALA LYS VAL ASN VAL GLY GLU VAL GLY GLY GLU SEQRES 3 B 146 ALA LEU ALA ARG LEU LEU ILE VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE ALA SER PHE GLY ASN LEU SER SER ALA ASN SEQRES 5 B 146 ALA ILE LEU HIS ASN ALA LYS VAL LEU ALA HIS GLY GLN SEQRES 6 B 146 LYS VAL LEU THR SER PHE GLY GLU ALA VAL LYS ASN LEU SEQRES 7 B 146 ASP ASN ILE LYS LYS THR PHE ALA GLN LEU SER GLU LEU SEQRES 8 B 146 HIS CYS GLU LYS LEU HIS VAL ASP PRO GLU ASN PHE LYS SEQRES 9 B 146 LEU LEU GLY ASN ILE LEU ILE ILE VAL LEU ALA THR HIS SEQRES 10 B 146 PHE PRO LYS GLU PHE THR PRO ALA SER GLN ALA ALA TRP SEQRES 11 B 146 THR LYS LEU VAL ASN ALA VAL ALA HIS ALA LEU ALA LEU SEQRES 12 B 146 GLY TYR HIS HET HEM A 201 43 HET HEM B 201 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 5 HOH *510(H2 O) HELIX 1 1 THR A 3 LEU A 18 1 16 HELIX 2 2 HIS A 20 TYR A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 SER A 52 HIS A 72 1 21 HELIX 5 5 ASN A 75 LEU A 80 1 6 HELIX 6 6 LEU A 80 ASN A 90 1 11 HELIX 7 7 ASP A 94 GLY A 114 1 21 HELIX 8 8 ARG A 115 TYR A 117 5 3 HELIX 9 9 THR A 118 ALA A 137 1 20 HELIX 10 10 GLU A 138 ARG A 141 5 4 HELIX 11 11 THR B 4 ALA B 16 1 13 HELIX 12 12 ASN B 19 TYR B 35 1 17 HELIX 13 13 PRO B 36 GLY B 46 5 11 HELIX 14 14 SER B 50 HIS B 56 1 7 HELIX 15 15 ASN B 57 LYS B 76 1 20 HELIX 16 16 ASN B 77 ASP B 79 5 3 HELIX 17 17 ASN B 80 PHE B 85 1 6 HELIX 18 18 PHE B 85 LYS B 95 1 11 HELIX 19 19 PRO B 100 PHE B 118 1 19 HELIX 20 20 THR B 123 LEU B 143 1 21 LINK FE HEM A 201 NE2 HIS A 87 LINK FE HEM B 201 NE2 HIS B 92 CRYST1 112.244 62.138 53.926 90.00 109.98 90.00 C 1 2 1 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 0.008909 0.000000 0.003239 0.00000 SCALE2 0.000000 0.016093 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019732 0.00000