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HEADER OXYGEN STORAGE/TRANSPORT 13-DEC-04 1Y8I TITLE HORSE METHEMOGLOBIN LOW SALT, PH 7.0 (98% RELATIVE HUMIDITY) COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAINS; COMPND 3 CHAIN: A, C; COMPND 4 SYNONYM: SLOW AND FAST; COMPND 5 OTHER_DETAILS: PH 7.0 AQUOMET STRUCTURE; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEMOGLOBIN BETA CHAIN; COMPND 8 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 3 ORGANISM_COMMON: HORSE; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: EQUUS CABALLUS; SOURCE 6 ORGANISM_COMMON: HORSE KEYWDS AQUO METHEMOGLOBIN, QUARTERNARY ASSOCIATION, ALLOSTERIC KEYWDS 2 TRANSITION, PROTEIN HYDRATION EXPDTA X-RAY DIFFRACTION AUTHOR R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN REVDAT 1 26-JUL-05 1Y8I 0 JRNL AUTH R.SANKARANARAYANAN,B.K.BISWAL,M.VIJAYAN JRNL TITL A NEW RELAXED STATE IN HORSE METHEMOGLOBIN JRNL TITL 2 CHARACTERIZED BY CRYSTALLOGRAPHIC STUDIES. JRNL REF PROTEINS V. 60 547 2005 JRNL REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN REMARK 1 TITL STRUCTURE OF HUMAN METHAEMOGLOBIN: THE VARIATION REMARK 1 TITL 2 OF A THEME REMARK 1 REF CURR.SCI. V. 81 1100 2001 REMARK 1 REFN ASTM CUSCAM II ISSN 0011-3891 REMARK 1 REFERENCE 2 REMARK 1 AUTH B.K.BISWAL,M.VIJAYAN REMARK 1 TITL STRUCTURES OF HUMAN OXY- AND DEOXYHAEMOGLOBIN AT REMARK 1 TITL 2 DIFFERENT LEVELS OF HUMIDITY: VARIABILITY IN THE T REMARK 1 TITL 3 STATE REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 58 1155 2002 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 2.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.4 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 231708.250 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8 REMARK 3 NUMBER OF REFLECTIONS : 17215 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 SET) : 0.167 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800 REMARK 3 FREE R VALUE TEST SET COUNT : 999 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007 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) : 2.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2500 REMARK 3 BIN R VALUE (WORKING SET) : 0.2240 REMARK 3 BIN FREE R VALUE : 0.2670 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 6.20 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 166 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4406 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 304 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.50 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.91000 REMARK 3 B22 (A**2) : 7.11000 REMARK 3 B33 (A**2) : -3.20000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26 REMARK 3 ESD FROM SIGMAA (A) : 0.23 REMARK 3 LOW RESOLUTION CUTOFF (A) : 20.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.36 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.12 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED 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 : 0.28 REMARK 3 BSOL : 48.25 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : TOPH19X.HEME REMARK 3 TOPOLOGY FILE 3 : WATER.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1Y8I 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 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB031249. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-AUG-2002 REMARK 200 TEMPERATURE (KELVIN) : 293.0 REMARK 200 PH : 7.00 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 RU200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : OSMIC MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE 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 : 18160 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.14300 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) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.47400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: HORSE METHEMOGLOBIN, PDB ENTRY 2MHB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 44.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M PHOSPHATE BUFFER, 30% PEG REMARK 280 3350, PH 7.0, LIQUID DIFFUSION, TEMPERATURE 293K 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 31.39900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.07950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.45350 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.07950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.39900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.45350 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 FE HEM B 147 O HOH 901 2.13 REMARK 500 FE HEM A 142 O HOH 900 2.14 REMARK 500 FE HEM C 142 O HOH 902 2.14 REMARK 500 FE HEM D 147 O HOH 903 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 MET C 32 SD MET C 32 CE 0.100 REMARK 500 LYS D 95 CB LYS D 95 CG 0.048 REMARK 500 LYS D 95 CG LYS D 95 CD 0.052 REMARK 500 LYS D 95 CD LYS D 95 CE 0.044 REMARK 500 LYS D 144 CB LYS D 144 CG -0.042 REMARK 500 LYS D 144 CE LYS D 144 NZ 0.055 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. = -8.7 DEGREES REMARK 500 PRO B 36 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 ASP B 79 C - N - CA ANGL. DEV. = -9.0 DEGREES REMARK 500 ASP C 47 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 LYS C 139 N - CA - C ANGL. DEV. =-14.1 DEGREES REMARK 500 TYR C 140 N - CA - C ANGL. DEV. = 20.1 DEGREES REMARK 500 ARG C 141 N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 TYR C 140 CA - C - N ANGL. DEV. = -8.9 DEGREES REMARK 500 ARG C 141 C - N - CA ANGL. DEV. = 10.5 DEGREES REMARK 500 ASN D 19 N - CA - C ANGL. DEV. = -7.9 DEGREES REMARK 500 LYS D 95 CD - CE - NZ ANGL. DEV. = 9.6 DEGREES REMARK 500 TYR D 145 N - CA - C ANGL. DEV. = -7.8 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 198 DISTANCE = 9.72 ANGSTROMS REMARK 525 HOH 222 DISTANCE = 5.64 ANGSTROMS REMARK 525 HOH 270 DISTANCE = 6.16 ANGSTROMS REMARK 525 HOH 278 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH 284 DISTANCE = 5.43 ANGSTROMS REMARK 525 HOH 286 DISTANCE = 5.20 ANGSTROMS REMARK 525 HOH 300 DISTANCE = 8.98 ANGSTROMS REMARK 525 HOH 303 DISTANCE = 10.89 ANGSTROMS REMARK 525 HOH 308 DISTANCE = 5.90 ANGSTROMS REMARK 525 HOH 320 DISTANCE = 5.41 ANGSTROMS REMARK 525 HOH 330 DISTANCE = 6.73 ANGSTROMS REMARK 525 HOH 333 DISTANCE = 11.09 ANGSTROMS REMARK 525 HOH 354 DISTANCE = 7.07 ANGSTROMS REMARK 525 HOH 355 DISTANCE = 5.26 ANGSTROMS REMARK 525 HOH 361 DISTANCE = 6.15 ANGSTROMS REMARK 525 HOH 362 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH 363 DISTANCE = 9.99 ANGSTROMS REMARK 525 HOH 371 DISTANCE = 6.27 ANGSTROMS REMARK 525 HOH 374 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH 377 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH 387 DISTANCE = 5.51 ANGSTROMS REMARK 525 HOH 420 DISTANCE = 8.22 ANGSTROMS REMARK 525 HOH 421 DISTANCE = 8.77 ANGSTROMS REMARK 525 HOH 426 DISTANCE = 7.25 ANGSTROMS REMARK 525 HOH 436 DISTANCE = 5.45 ANGSTROMS REMARK 525 HOH 442 DISTANCE = 8.56 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JY7 RELATED DB: PDB REMARK 900 RELATED ID: 1LFQ RELATED DB: PDB REMARK 900 RELATED ID: 1Y8H RELATED DB: PDB REMARK 900 RELATED ID: 1Y8K RELATED DB: PDB DBREF 1Y8I A 1 141 UNP P01958 HBA_HORSE 1 141 DBREF 1Y8I C 1 141 UNP P01958 HBA_HORSE 1 141 DBREF 1Y8I B 1 146 UNP P02062 HBB_HORSE 1 146 DBREF 1Y8I D 1 146 UNP P02062 HBB_HORSE 1 146 SEQADV 1Y8I ASP A 82 UNP P01958 ASN 82 CONFLICT SEQADV 1Y8I ASN A 85 UNP P01958 ASP 85 CONFLICT SEQADV 1Y8I ASP C 82 UNP P01958 ASN 82 CONFLICT SEQADV 1Y8I ASN C 85 UNP P01958 ASP 85 CONFLICT SEQRES 1 A 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA SEQRES 3 A 141 GLU ALA LEU GLU ARG MET PHE LEU GLY 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 ALA HIS GLY LYS LYS VAL GLY ASP ALA SEQRES 6 A 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY SEQRES 7 A 141 ALA LEU SER ASP LEU SER ASN LEU HIS ALA HIS LYS LEU SEQRES 8 A 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 A 141 LEU LEU SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER SEQRES 11 A 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA SEQRES 2 B 146 LEU TRP ASP LYS VAL ASN GLU GLU GLU VAL GLY GLY GLU SEQRES 3 B 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 B 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER ASN PRO GLY SEQRES 5 B 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 B 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU SEQRES 7 B 146 ASP ASN LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU SEQRES 8 B 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 B 146 LEU LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG HIS SEQRES 10 B 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER TYR SEQRES 11 B 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS SEQRES 12 B 146 LYS TYR HIS SEQRES 1 C 141 VAL LEU SER ALA ALA ASP LYS THR ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP SER LYS VAL GLY GLY HIS ALA GLY GLU TYR GLY ALA SEQRES 3 C 141 GLU ALA LEU GLU ARG MET PHE LEU GLY 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 ALA HIS GLY LYS LYS VAL GLY ASP ALA SEQRES 6 C 141 LEU THR LEU ALA VAL GLY HIS LEU ASP ASP LEU PRO GLY SEQRES 7 C 141 ALA LEU SER ASP LEU SER ASN LEU HIS ALA HIS LYS LEU SEQRES 8 C 141 ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS SEQRES 9 C 141 LEU LEU SER THR LEU ALA VAL HIS LEU PRO ASN ASP PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU SER SEQRES 11 C 141 SER VAL SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 146 VAL GLN LEU SER GLY GLU GLU LYS ALA ALA VAL LEU ALA SEQRES 2 D 146 LEU TRP ASP LYS VAL ASN GLU GLU GLU VAL GLY GLY GLU SEQRES 3 D 146 ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN SEQRES 4 D 146 ARG PHE PHE ASP SER PHE GLY ASP LEU SER ASN PRO GLY SEQRES 5 D 146 ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS SEQRES 6 D 146 LYS VAL LEU HIS SER PHE GLY GLU GLY VAL HIS HIS LEU SEQRES 7 D 146 ASP ASN LEU LYS GLY THR PHE ALA ALA LEU SER GLU LEU SEQRES 8 D 146 HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG SEQRES 9 D 146 LEU LEU GLY ASN VAL LEU VAL VAL VAL LEU ALA ARG HIS SEQRES 10 D 146 PHE GLY LYS ASP PHE THR PRO GLU LEU GLN ALA SER TYR SEQRES 11 D 146 GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS SEQRES 12 D 146 LYS TYR HIS HET HEM A 142 43 HET HEM B 147 43 HET HEM C 142 43 HET HEM D 147 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) FORMUL 9 HOH *304(H2 O) HELIX 1 1 SER A 3 GLY A 18 1 16 HELIX 2 2 HIS A 20 PHE A 36 1 17 HELIX 3 3 PRO A 37 PHE A 43 5 7 HELIX 4 4 SER A 52 GLY A 71 1 20 HELIX 5 5 ASP A 75 LEU A 80 1 6 HELIX 6 6 LEU A 80 HIS A 89 1 10 HELIX 7 7 PRO A 95 LEU A 113 1 19 HELIX 8 8 THR A 118 SER A 138 1 21 HELIX 9 9 SER B 4 LYS B 17 1 14 HELIX 10 10 GLU B 22 TYR B 35 1 14 HELIX 11 11 PRO B 36 GLY B 46 5 11 HELIX 12 12 ASN B 50 ASN B 57 1 8 HELIX 13 13 ASN B 57 HIS B 77 1 21 HELIX 14 14 ASN B 80 PHE B 85 1 6 HELIX 15 15 PHE B 85 LYS B 95 1 11 HELIX 16 16 PRO B 100 GLY B 119 1 20 HELIX 17 17 LYS B 120 PHE B 122 5 3 HELIX 18 18 THR B 123 ALA B 142 1 20 HELIX 19 19 SER C 3 GLY C 18 1 16 HELIX 20 20 HIS C 20 PHE C 36 1 17 HELIX 21 21 PRO C 37 PHE C 43 5 7 HELIX 22 22 SER C 52 HIS C 72 1 21 HELIX 23 23 ASP C 75 LEU C 80 1 6 HELIX 24 24 LEU C 80 HIS C 89 1 10 HELIX 25 25 PRO C 95 LEU C 113 1 19 HELIX 26 26 THR C 118 SER C 138 1 21 HELIX 27 27 SER D 4 ASP D 16 1 13 HELIX 28 28 ASN D 19 TYR D 35 1 17 HELIX 29 29 PRO D 36 GLY D 46 5 11 HELIX 30 30 ASN D 50 ASN D 57 1 8 HELIX 31 31 ASN D 57 HIS D 76 1 20 HELIX 32 32 ASN D 80 ASP D 94 1 15 HELIX 33 33 PRO D 100 GLY D 119 1 20 HELIX 34 34 LYS D 120 PHE D 122 5 3 HELIX 35 35 THR D 123 ALA D 142 1 20 HELIX 36 36 HIS D 143 HIS D 146 5 4 LINK NE2 HIS A 87 FE HEM A 142 LINK NE2 HIS C 87 FE HEM C 142 LINK NE2 HIS B 92 FE HEM B 147 LINK NE2 HIS D 92 FE HEM D 147 CRYST1 62.798 80.907 112.159 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 0.015924 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012360 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008916 0.00000