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HEADER OXYGEN TRANSPORT 01-OCT-79 1HDS TITLE MACROMOLECULAR STRUCTURE REFINEMENT BY RESTRAINED LEAST- TITLE 2 SQUARES AND INTERACTIVE GRAPHICS AS APPLIED TO SICKLING TITLE 3 DEER TYPE III HEMOGLOBIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN S (DEOXY) (ALPHA CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HEMOGLOBIN S (DEOXY) (BETA CHAIN); COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ODOCOILEUS VIRGINIANUS; SOURCE 3 MOL_ID: 2; SOURCE 4 ORGANISM_SCIENTIFIC: ODOCOILEUS VIRGINIANUS KEYWDS OXYGEN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR E.L.AMMA,R.L.GIRLING REVDAT 8 30-SEP-83 1HDS 1 REVDAT REVDAT 7 13-JUN-83 1HDS 1 REMARK REVDAT 6 02-MAR-82 1HDS 1 REMARK REVDAT 5 15-SEP-81 1HDS 1 REMARK REVDAT 4 01-OCT-80 1HDS 1 REMARK REVDAT 3 13-JUN-80 1HDS 1 SEQRES REVDAT 2 05-MAR-80 1HDS 1 REMARK REVDAT 1 07-DEC-79 1HDS 0 JRNL AUTH R.L.GIRLING,T.E.HOUSTON,W.C.SCHMIDTJUNIOR,E.L.AMMA JRNL TITL MACROMOLECULAR STRUCTURE REFINEMENT BY RESTRAINED JRNL TITL 2 LEAST-SQUARES AND INTERACTIVE GRAPHICS AS APPLIED JRNL TITL 3 TO SICKLING DEER TYPE III HEMOGLOBIN JRNL REF ACTA CRYSTALLOGR.,SECT.A V. 36 43 1980 JRNL REFN ASTM ACACEQ DK ISSN 0108-7673 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.L.GIRLING,W.C.SCHMIDTJUNIOR,T.E.HOUSTON,E.L.AMMA, REMARK 1 AUTH 2 T.H.J.HUISMAN REMARK 1 TITL MOLECULAR PACKING AND INTERMOLECULAR CONTACTS OF REMARK 1 TITL 2 SICKLING DEER TYPE III HEMOGLOBIN REMARK 1 REF J.MOL.BIOL. V. 131 417 1979 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH W.C.SCHMIDTJUNIOR,R.L.GIRLING,E.L.AMMA REMARK 1 TITL APPLICATION OF A RESTRAINED LEAST-SQUARES REMARK 1 TITL 2 REFINEMENT PROCEDURE TO SICKLING DEER HEMOGLOBIN REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 33 3618 1977 REMARK 1 REFN ASTM ASBSDK DK ISSN 0108-7681 REMARK 1 REFERENCE 3 REMARK 1 AUTH W.C.SCHMIDTJUNIOR,R.L.GIRLING,T.E.HOUSTON, REMARK 1 AUTH 2 G.D.SPROUL,E.L.AMMA,T.H.J.HUISMAN REMARK 1 TITL THE STRUCTURE OF SICKLING DEER TYPE III HEMOGLOBIN REMARK 1 TITL 2 BY MOLECULAR REPLACEMENT REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 33 335 1977 REMARK 1 REFN ASTM ASBSDK DK ISSN 0108-7681 REMARK 1 REFERENCE 4 REMARK 1 EDIT M.O.DAYHOFF REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 214 1978 REMARK 1 REF 2 AND STRUCTURE,SUPPLEMENT 3 REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER REMARK 1 PUBL 2 SPRING,MD. REMARK 1 REFN ISSN 0-912466-07-3 REMARK 2 REMARK 2 RESOLUTION. 1.98 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NULL REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 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 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 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4384 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 172 REMARK 3 SOLVENT ATOMS : 0 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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1HDS 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: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 81.75000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.41500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.75000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.41500 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 DBREF 1HDS A 1 141 UNP P01972 HBA_ODOVI 1 141 DBREF 1HDS B 1 145 UNP P02074 HBB_ODOVI 1 145 DBREF 1HDS C 1 141 UNP P01972 HBA_ODOVI 1 141 DBREF 1HDS D 1 145 UNP P02074 HBB_ODOVI 1 145 SEQADV 1HDS ASN A 6 UNP P01972 ASP 6 CONFLICT SEQADV 1HDS GLN A 27 UNP P01972 GLU 27 CONFLICT SEQADV 1HDS GLN A 30 UNP P01972 GLU 30 CONFLICT SEQADV 1HDS GLN A 55 UNP P01972 VAL 55 CONFLICT SEQADV 1HDS GLN A 60 UNP P01972 GLU 60 CONFLICT SEQADV 1HDS GLN A 70 UNP P01972 VAL 70 CONFLICT SEQADV 1HDS ASN A 74 UNP P01972 ASP 74 CONFLICT SEQADV 1HDS ASN A 82 UNP P01972 ASP 82 CONFLICT SEQADV 1HDS ASN A 85 UNP P01972 ASP 85 CONFLICT SEQADV 1HDS ASN A 94 UNP P01972 ASP 94 CONFLICT SEQADV 1HDS SER A 104 UNP P01972 THR 104 CONFLICT SEQADV 1HDS THR A 115 UNP P01972 SER 115 CONFLICT SEQADV 1HDS ASN A 116 UNP P01972 ASP 116 CONFLICT SEQADV 1HDS ASN A 124 UNP P01972 SER 124 CONFLICT SEQADV 1HDS ASN A 126 UNP P01972 ASP 126 CONFLICT SEQADV 1HDS ASP A 132 UNP P01972 VAL 132 CONFLICT SEQADV 1HDS ASP B 18 UNP P02074 ASN 18 CONFLICT SEQADV 1HDS GLN B 25 UNP P02074 GLU 25 CONFLICT SEQADV 1HDS GLN B 42 UNP P02074 GLU 42 CONFLICT SEQADV 1HDS ASN B 46 UNP P02074 ASP 46 CONFLICT SEQADV 1HDS ASN B 55 UNP P02074 GLY 55 CONFLICT SEQADV 1HDS THR B 71 UNP P02074 SER 71 CONFLICT SEQADV 1HDS GLN B 72 UNP P02074 GLU 72 CONFLICT SEQADV 1HDS GLN B 86 UNP P02074 GLU 86 CONFLICT SEQADV 1HDS GLY B 89 UNP P02074 GLU 89 CONFLICT SEQADV 1HDS ASN B 98 UNP P02074 ASP 98 CONFLICT SEQADV 1HDS GLN B 100 UNP P02074 GLU 100 CONFLICT SEQADV 1HDS ALA B 110 UNP P02074 VAL 110 CONFLICT SEQADV 1HDS LEU B 111 UNP P02074 VAL 111 CONFLICT SEQADV 1HDS VAL B 113 UNP P02074 LEU 113 CONFLICT SEQADV 1HDS GLN B 120 UNP P02074 GLU 120 CONFLICT SEQADV 1HDS ASN B 124 UNP P02074 LEU 124 CONFLICT SEQADV 1HDS LEU B 128 UNP P02074 ASP 128 CONFLICT SEQADV 1HDS LYS B 143 UNP P02074 ARG 143 CONFLICT SEQADV 1HDS ASN C 6 UNP P01972 ASP 6 CONFLICT SEQADV 1HDS GLN C 27 UNP P01972 GLU 27 CONFLICT SEQADV 1HDS GLN C 30 UNP P01972 GLU 30 CONFLICT SEQADV 1HDS GLN C 55 UNP P01972 VAL 55 CONFLICT SEQADV 1HDS GLN C 60 UNP P01972 GLU 60 CONFLICT SEQADV 1HDS GLN C 70 UNP P01972 VAL 70 CONFLICT SEQADV 1HDS ASN C 74 UNP P01972 ASP 74 CONFLICT SEQADV 1HDS ASN C 82 UNP P01972 ASP 82 CONFLICT SEQADV 1HDS ASN C 85 UNP P01972 ASP 85 CONFLICT SEQADV 1HDS ASN C 94 UNP P01972 ASP 94 CONFLICT SEQADV 1HDS SER C 104 UNP P01972 THR 104 CONFLICT SEQADV 1HDS THR C 115 UNP P01972 SER 115 CONFLICT SEQADV 1HDS ASN C 116 UNP P01972 ASP 116 CONFLICT SEQADV 1HDS ASN C 124 UNP P01972 SER 124 CONFLICT SEQADV 1HDS ASN C 126 UNP P01972 ASP 126 CONFLICT SEQADV 1HDS ASP C 132 UNP P01972 VAL 132 CONFLICT SEQADV 1HDS ASP D 18 UNP P02074 ASN 18 CONFLICT SEQADV 1HDS GLN D 25 UNP P02074 GLU 25 CONFLICT SEQADV 1HDS GLN D 42 UNP P02074 GLU 42 CONFLICT SEQADV 1HDS ASN D 46 UNP P02074 ASP 46 CONFLICT SEQADV 1HDS ASN D 55 UNP P02074 GLY 55 CONFLICT SEQADV 1HDS THR D 71 UNP P02074 SER 71 CONFLICT SEQADV 1HDS GLN D 72 UNP P02074 GLU 72 CONFLICT SEQADV 1HDS GLN D 86 UNP P02074 GLU 86 CONFLICT SEQADV 1HDS GLY D 89 UNP P02074 GLU 89 CONFLICT SEQADV 1HDS ASN D 98 UNP P02074 ASP 98 CONFLICT SEQADV 1HDS GLN D 100 UNP P02074 GLU 100 CONFLICT SEQADV 1HDS ALA D 110 UNP P02074 VAL 110 CONFLICT SEQADV 1HDS LEU D 111 UNP P02074 VAL 111 CONFLICT SEQADV 1HDS VAL D 113 UNP P02074 LEU 113 CONFLICT SEQADV 1HDS GLN D 120 UNP P02074 GLU 120 CONFLICT SEQADV 1HDS ASN D 124 UNP P02074 LEU 124 CONFLICT SEQADV 1HDS LEU D 128 UNP P02074 ASP 128 CONFLICT SEQADV 1HDS LYS D 143 UNP P02074 ARG 143 CONFLICT SEQRES 1 A 141 VAL LEU SER ALA ALA ASN LYS SER ASN VAL LYS ALA ALA SEQRES 2 A 141 TRP GLY LYS VAL GLY GLY ASN ALA PRO ALA TYR GLY ALA SEQRES 3 A 141 GLN ALA LEU GLN 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 GLN LYS ALA HIS GLY GLN LYS VAL ALA ASN ALA SEQRES 6 A 141 LEU THR LYS ALA GLN GLY HIS LEU ASN ASP LEU PRO GLY SEQRES 7 A 141 THR LEU SER ASN LEU SER ASN LEU HIS ALA HIS LYS LEU SEQRES 8 A 141 ARG VAL ASN PRO VAL ASN PHE LYS LEU LEU SER HIS SER SEQRES 9 A 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO THR ASN PHE SEQRES 10 A 141 THR PRO ALA VAL HIS ALA ASN LEU ASN LYS PHE LEU ALA SEQRES 11 A 141 ASN ASP SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 B 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR GLY PHE SEQRES 2 B 145 TRP GLY LYS VAL ASP VAL ASP VAL VAL GLY ALA GLN ALA SEQRES 3 B 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 B 145 PHE PHE GLN HIS PHE GLY ASN LEU SER SER ALA GLY ALA SEQRES 5 B 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS ARG SEQRES 6 B 145 VAL LEU ASP ALA PHE THR GLN GLY LEU LYS HIS LEU ASP SEQRES 7 B 145 ASP LEU LYS GLY ALA PHE ALA GLN LEU SER GLY LEU HIS SEQRES 8 B 145 CYS ASN LYS LEU HIS VAL ASN PRO GLN ASN PHE ARG LEU SEQRES 9 B 145 LEU GLY ASN VAL LEU ALA LEU VAL VAL ALA ARG ASN PHE SEQRES 10 B 145 GLY GLY GLN PHE THR PRO ASN VAL GLN ALA LEU PHE GLN SEQRES 11 B 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS LYS SEQRES 12 B 145 TYR HIS SEQRES 1 C 141 VAL LEU SER ALA ALA ASN LYS SER ASN VAL LYS ALA ALA SEQRES 2 C 141 TRP GLY LYS VAL GLY GLY ASN ALA PRO ALA TYR GLY ALA SEQRES 3 C 141 GLN ALA LEU GLN 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 GLN LYS ALA HIS GLY GLN LYS VAL ALA ASN ALA SEQRES 6 C 141 LEU THR LYS ALA GLN GLY HIS LEU ASN ASP LEU PRO GLY SEQRES 7 C 141 THR LEU SER ASN LEU SER ASN LEU HIS ALA HIS LYS LEU SEQRES 8 C 141 ARG VAL ASN PRO VAL ASN PHE LYS LEU LEU SER HIS SER SEQRES 9 C 141 LEU LEU VAL THR LEU ALA SER HIS LEU PRO THR ASN PHE SEQRES 10 C 141 THR PRO ALA VAL HIS ALA ASN LEU ASN LYS PHE LEU ALA SEQRES 11 C 141 ASN ASP SER THR VAL LEU THR SER LYS TYR ARG SEQRES 1 D 145 MET LEU THR ALA GLU GLU LYS ALA ALA VAL THR GLY PHE SEQRES 2 D 145 TRP GLY LYS VAL ASP VAL ASP VAL VAL GLY ALA GLN ALA SEQRES 3 D 145 LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN ARG SEQRES 4 D 145 PHE PHE GLN HIS PHE GLY ASN LEU SER SER ALA GLY ALA SEQRES 5 D 145 VAL MET ASN ASN PRO LYS VAL LYS ALA HIS GLY LYS ARG SEQRES 6 D 145 VAL LEU ASP ALA PHE THR GLN GLY LEU LYS HIS LEU ASP SEQRES 7 D 145 ASP LEU LYS GLY ALA PHE ALA GLN LEU SER GLY LEU HIS SEQRES 8 D 145 CYS ASN LYS LEU HIS VAL ASN PRO GLN ASN PHE ARG LEU SEQRES 9 D 145 LEU GLY ASN VAL LEU ALA LEU VAL VAL ALA ARG ASN PHE SEQRES 10 D 145 GLY GLY GLN PHE THR PRO ASN VAL GLN ALA LEU PHE GLN SEQRES 11 D 145 LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS LYS SEQRES 12 D 145 TYR HIS FTNOTE 1 THE CHIRALITY OF THIS RESIDUE APPEARS TO BE IN ERROR AND FTNOTE 1 WILL BE CORRECTED IN SUBSEQUENT REFINEMENT CYCLES. HET HEM A 1 43 HET HEM B 1 43 HET HEM C 1 43 HET HEM D 1 43 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 HEM 4(C34 H32 FE N4 O4) HELIX 1 1 SER A 3 GLY A 15 1 13 HELIX 2 2 ALA A 21 LEU A 29 1 9 HELIX 3 3 THR A 39 PHE A 43 5 5 HELIX 4 4 ALA A 53 GLN A 70 1 18 HELIX 5 5 ASP A 75 LEU A 80 1 6 HELIX 6 6 LEU A 83 HIS A 89 1 7 HELIX 7 7 ASN A 94 VAL A 96 5 3 HELIX 8 8 ASN A 97 LEU A 113 1 17 HELIX 9 9 THR A 118 LEU A 136 1 19 HELIX 10 10 GLU B 5 TRP B 14 1 10 HELIX 11 11 VAL B 21 LEU B 31 1 11 HELIX 12 12 PHE B 40 PHE B 44 5 5 HELIX 13 13 SER B 49 ASN B 56 1 8 HELIX 14 14 PRO B 57 VAL B 66 1 10 HELIX 15 15 GLN B 86 LYS B 94 1 9 HELIX 16 16 ASN B 98 GLY B 118 1 21 HELIX 17 17 THR B 122 LYS B 143 1 22 HELIX 18 18 ALA C 5 GLY C 18 1 14 HELIX 19 19 ALA C 21 GLN C 30 1 10 HELIX 20 20 GLN C 30 PHE C 36 1 7 HELIX 21 21 PRO C 37 PHE C 43 5 7 HELIX 22 22 SER C 52 GLN C 70 1 19 HELIX 23 23 ASP C 75 LEU C 80 1 6 HELIX 24 24 SER C 84 HIS C 89 1 6 HELIX 25 25 ASN C 94 VAL C 96 5 3 HELIX 26 26 ASN C 97 LEU C 113 1 17 HELIX 27 27 THR C 118 SER C 138 1 21 HELIX 28 28 LYS C 139 ARG C 141 5 3 HELIX 29 29 ASP D 20 TYR D 34 1 15 HELIX 30 30 PRO D 35 PHE D 41 5 7 HELIX 31 31 ALA D 50 ASN D 56 1 7 HELIX 32 32 PRO D 57 THR D 71 1 15 HELIX 33 33 ASP D 79 PHE D 84 1 6 HELIX 34 34 GLY D 89 LYS D 94 1 6 HELIX 35 35 ASN D 98 LEU D 111 1 14 HELIX 36 36 VAL D 113 GLY D 118 1 6 HELIX 37 37 GLY D 119 PHE D 121 5 3 HELIX 38 38 THR D 122 LYS D 131 1 10 HELIX 39 39 LYS D 131 LEU D 140 1 10 CISPEP 1 ALA A 88 HIS A 89 0 -25.73 CISPEP 2 LEU B 77 ASP B 78 0 3.00 CISPEP 3 ASP B 79 LEU B 80 0 -0.18 CISPEP 4 LEU B 80 LYS B 81 0 16.18 CISPEP 5 ALA B 85 GLN B 86 0 -7.20 CISPEP 6 PHE B 121 THR B 122 0 3.80 CISPEP 7 LEU C 48 SER C 49 0 9.47 CISPEP 8 SER C 49 HIS C 50 0 12.77 CISPEP 9 GLN C 70 GLY C 71 0 23.82 CISPEP 10 ASN C 85 LEU C 86 0 -26.51 CISPEP 11 LEU C 109 ALA C 110 0 -25.29 CISPEP 12 ALA D 4 GLU D 5 0 -25.50 CISPEP 13 LYS D 7 ALA D 8 0 15.91 CISPEP 14 THR D 11 GLY D 12 0 -2.67 CISPEP 15 ALA D 50 GLY D 51 0 -5.49 CISPEP 16 PHE D 70 THR D 71 0 9.98 CISPEP 17 LEU D 77 ASP D 78 0 25.86 CRYST1 163.500 70.830 65.950 90.00 94.15 90.00 C 1 2 1 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 0.006116 0.000000 0.000444 0.00000 SCALE2 0.000000 0.014118 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015203 0.00000