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HEADER OXYGEN STORAGE/TRANSPORT 11-SEP-00 1FSX TITLE THE X-RAY STRUCTURE DETERMINATION OF BOVINE CARBONMONOXY HB TITLE 2 AT 2.1 A RESOLUTION AND ITS RELATIONSHIP TO THE QUATERNARY TITLE 3 STRUCTURE OF OTHER HB CRYSTAL FORMS COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEMOGLOBIN ALPHA CHAIN; COMPND 3 CHAIN: A, C; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: HEMOGLOBIN BETA CHAIN; COMPND 6 CHAIN: B, D SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 TISSUE: BLOOD; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 7 ORGANISM_COMMON: BOVINE; SOURCE 8 TISSUE: BLOOD KEYWDS HEMOGLOBIN TETRAMER, R-STATE, QUATERNARY STRUCTURE EXPDTA X-RAY DIFFRACTION AUTHOR M.K.SAFO,D.J.ABRAHAM REVDAT 2 01-APR-03 1FSX 1 JRNL REVDAT 1 06-JUN-01 1FSX 0 JRNL AUTH M.K.SAFO,D.J.ABRAHAM JRNL TITL THE X-RAY STRUCTURE DETERMINATION OF BOVINE JRNL TITL 2 CARBONMONOXY HEMOGLOBIN AT 2.1 A RESOULTION AND JRNL TITL 3 ITS RELATIONSHIP TO THE QUATERNARY STRUCTURES OF JRNL TITL 4 OTHER HEMOGLOBIN CRYSTAL FROMS. JRNL REF PROTEIN SCI. V. 10 1091 2001 JRNL REFN ASTM PRCIEI US ISSN 0961-8368 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.843 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 32949 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1647 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 : 4386 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 180 REMARK 3 SOLVENT ATOMS : 136 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.40 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) : 0.013 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: 1. ANOMALOUS DATA USED FOR REMARK 3 REFINEMENT. 2. BULK SOLVENT CORRECTION DURING REFINEMENT REMARK 4 REMARK 4 1FSX 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 RCSB011873. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-APR-1993 REMARK 200 TEMPERATURE (KELVIN) : 298.0 REMARK 200 PH : 7.30 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 200 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32949 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 64.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.42000 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: NULL REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 46.80 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, SODIUM REMARK 280 PHOSPHATE, PYRIDINE, BENZENE, PH 7.3, LIQUID DIFFUSION, REMARK 280 TEMPERATURE 298.0K 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 39.70500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.70000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.31500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.70000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.70500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.31500 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 C CMO 747 FE HEM 748 1.74 REMARK 500 C CMO 142 FE HEM 143 1.80 REMARK 500 C CMO 347 FE HEM 348 1.80 REMARK 500 C CMO 542 FE HEM 543 1.81 REMARK 500 O THR C 537 O ARG C 541 1.97 REMARK 500 NE2 HIS A 87 FE HEM 143 2.04 REMARK 500 NE2 HIS D 692 FE HEM 748 2.06 REMARK 500 NE2 HIS C 487 FE HEM 543 2.11 REMARK 500 NE2 HIS B 292 FE HEM 348 2.14 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 B 255 SD MET B 255 CE -0.172 REMARK 500 CYS D 693 CB CYS D 693 SG 0.083 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 VAL A 1 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASP A 47 N - CA - C ANGL. DEV. =-15.2 DEGREES REMARK 500 SER A 138 N - CA - C ANGL. DEV. = 9.6 DEGREES REMARK 500 LEU B 278 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 LEU C 402 CA - CB - CG ANGL. DEV. = 8.5 DEGREES REMARK 500 ASP C 447 N - CA - C ANGL. DEV. =-13.8 DEGREES REMARK 500 TYR C 540 N - CA - C ANGL. DEV. = 16.0 DEGREES REMARK 500 TYR C 540 C - N - CA ANGL. DEV. = 12.6 DEGREES REMARK 500 PRO D 636 N - CA - C ANGL. DEV. = 9.2 DEGREES REMARK 500 SER D 649 N - CA - C ANGL. DEV. = 10.3 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU D 603 154.26 59.46 DBREF 1FSX A 1 141 UNP P01966 HBA_BOVIN 1 141 DBREF 1FSX C 401 541 UNP P01966 HBA_BOVIN 1 141 DBREF 1FSX B 202 346 UNP P02070 HBB_BOVIN 1 145 DBREF 1FSX D 602 746 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 CMO 142 2 HET HEM 143 43 HET CMO 347 2 HET HEM 348 43 HET CMO 542 2 HET HEM 543 43 HET CMO 747 2 HET HEM 748 43 HETNAM CMO CARBON MONOXIDE HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETSYN HEM HEME FORMUL 5 CMO 4(C O) FORMUL 6 HEM 4(C34 H32 FE N4 O4) FORMUL 13 HOH *136(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 HIS A 72 1 21 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 THR A 137 1 20 HELIX 9 9 THR B 204 GLY B 216 1 13 HELIX 10 10 LYS B 219 TYR B 235 1 17 HELIX 11 11 PRO B 236 PHE B 242 5 7 HELIX 12 12 PHE B 242 GLY B 246 5 5 HELIX 13 13 THR B 250 ASN B 256 1 7 HELIX 14 14 ASN B 257 LYS B 276 1 20 HELIX 15 15 ASP B 280 PHE B 285 1 6 HELIX 16 16 PHE B 285 ASP B 294 1 10 HELIX 17 17 PRO B 300 GLY B 319 1 20 HELIX 18 18 LYS B 320 PHE B 322 5 3 HELIX 19 19 THR B 323 HIS B 343 1 21 HELIX 20 20 SER C 403 GLY C 418 1 16 HELIX 21 21 HIS C 420 PHE C 436 1 17 HELIX 22 22 PRO C 437 PHE C 443 5 7 HELIX 23 23 SER C 452 GLU C 471 1 20 HELIX 24 24 ASP C 475 LEU C 480 1 6 HELIX 25 25 LEU C 480 HIS C 489 1 10 HELIX 26 26 PRO C 495 LEU C 513 1 19 HELIX 27 27 THR C 518 THR C 537 1 20 HELIX 28 28 THR D 604 GLY D 616 1 13 HELIX 29 29 LYS D 619 TYR D 635 1 17 HELIX 30 30 PRO D 636 GLU D 643 5 8 HELIX 31 31 PHE D 642 GLY D 646 5 5 HELIX 32 32 THR D 650 ASN D 656 1 7 HELIX 33 33 ASN D 657 MET D 675 1 19 HELIX 34 34 ASP D 680 PHE D 685 1 6 HELIX 35 35 PHE D 685 LYS D 695 1 11 HELIX 36 36 PRO D 700 GLY D 719 1 20 HELIX 37 37 LYS D 720 PHE D 722 5 3 HELIX 38 38 THR D 723 HIS D 743 1 21 HELIX 39 39 ARG D 744 HIS D 746 5 3 CRYST1 79.410 110.630 65.400 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 0.012593 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009039 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015291 0.00000