HEADER OXYGEN STORAGE/TRANSPORT 12-AUG-98 1M6C TITLE V68N MYOGLOBIN WITH CO COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (MYOGLOBIN); COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA; SOURCE 3 ORGANISM_COMMON: PIG; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PLCII KEYWDS OXYGEN STORAGE, MYOGLOBIN, CO EXPDTA X-RAY DIFFRACTION AUTHOR G.N.MURSHUDOV,S.KRZYWDA,A.M.BRZOZOWSKI,M.JASKOLSKI, AUTHOR 2 E.E.SCOTT,S.A.KLIZAS,Q.H.GIBSON,J.S.OLSON,A.J.WILKINSON REVDAT 3 01-APR-03 1M6C 1 JRNL REVDAT 2 29-DEC-99 1M6C 4 HEADER COMPND REMARK JRNL REVDAT 2 2 4 ATOM SOURCE SEQRES REVDAT 1 19-AUG-98 1M6C 0 JRNL AUTH S.KRZYWDA,G.N.MURSHUDOV,A.M.BRZOZOWSKI,M.JASKOLSKI, JRNL AUTH 2 E.E.SCOTT,S.A.KLIZAS,Q.H.GIBSON,J.S.OLSON, JRNL AUTH 3 A.J.WILKINSON JRNL TITL STABILIZING BOUND O2 IN MYOGLOBIN BY VALINE68 JRNL TITL 2 (E11) TO ASPARAGINE SUBSTITUTION. JRNL REF BIOCHEMISTRY V. 37 15896 1998 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 3 NUMBER OF REFLECTIONS : 35786 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) : 0.192 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1788 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2472 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 90 REMARK 3 SOLVENT ATOMS : 487 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.28000 REMARK 3 B22 (A**2) : 2.44000 REMARK 3 B33 (A**2) : -4.18000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 1.08000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.019 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.037 ; 0.040 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.042 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.014 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.164 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.192 ; 0.300 REMARK 3 MULTIPLE TORSION (A) : 0.274 ; 0.300 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) : 3.700 ; 7.000 REMARK 3 STAGGERED (DEGREES) : 16.200; 15.000 REMARK 3 TRANSVERSE (DEGREES) : 42.400; 20.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.346 ; 4.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.419 ; 6.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.696 ; 4.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.303 ; 6.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1M6C 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 RCSB . REMARK 100 THE RCSB ID CODE IS RCSB008354. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 150.0 REMARK 200 PH : 7.10 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 : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : CCP4 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35786 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 24.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.05800 REMARK 200 R SYM (I) : 0.05800 REMARK 200 FOR THE DATA SET : 22.3000 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER REMARK 200 SOFTWARE USED: CCP4 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 64.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 PHOSPHATE BUFFER PH 7.1 10 MG/ REMARK 280 ML PROTEIN REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,1/2+Y,-Z REMARK 290 3555 1/2+X,1/2+Y,1/2+Z REMARK 290 4555 1/2-X,Y,1/2-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 21.15000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.08130 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.15000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.73178 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.08130 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 45.73178 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 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 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 OE2 GLU B 27 O HOH 90 0.96 REMARK 500 O HOH 148 O HOH 191 1.45 REMARK 500 O HOH 101 O HOH 202 1.49 REMARK 500 CD GLU B 27 O HOH 90 1.66 REMARK 500 O HOH 290 O HOH 307 1.67 REMARK 500 O HOH 373 O HOH 464 1.76 REMARK 500 O HOH 315 O HOH 400 1.81 REMARK 500 OE1 GLN B 128 O HOH 148 1.83 REMARK 500 OE1 GLN B 128 O HOH 116 1.85 REMARK 500 O HOH 283 O HOH 492 1.86 REMARK 500 O HOH 127 O HOH 300 2.02 REMARK 500 OE1 GLU B 18 O HOH 70 2.09 REMARK 500 O HOH 251 O HOH 323 2.12 REMARK 500 O HOH 165 O HOH 194 2.14 REMARK 500 O HOH 20 O HOH 214 2.16 REMARK 500 O HOH 17 O HOH 236 2.19 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 CE1 HIS B 48 O HOH 367 1554 0.77 REMARK 500 OE1 GLN A 128 O HOH 157 2656 0.84 REMARK 500 ND1 HIS B 48 O HOH 367 1554 0.91 REMARK 500 CD GLN A 128 O HOH 157 2656 1.10 REMARK 500 OE1 GLN A 128 O HOH 93 2656 1.12 REMARK 500 NE2 GLN A 128 O HOH 57 2656 1.50 REMARK 500 CD GLN A 128 O HOH 93 2656 1.64 REMARK 500 CD2 HIS B 48 O HOH 219 1554 1.69 REMARK 500 CG GLN A 128 O HOH 93 2656 1.83 REMARK 500 OE1 GLU B 109 O HOH 183 2645 1.83 REMARK 500 NE2 GLN A 128 O HOH 93 2656 1.86 REMARK 500 CD GLN A 128 O HOH 93 2656 2.00 REMARK 500 NE2 HIS B 48 O HOH 367 1554 2.02 REMARK 500 CD GLU B 109 O HOH 183 2645 2.02 REMARK 500 OE1 GLU B 83 O HOH 393 4555 2.08 REMARK 500 CG GLN A 128 O HOH 157 2656 2.11 REMARK 500 O HOH 21 O HOH 373 2656 2.12 REMARK 500 NE2 GLN A 128 O HOH 157 2656 2.13 REMARK 500 CG HIS B 48 O HOH 367 1554 2.18 REMARK 500 NZ LYS A 16 O HOH 351 2646 2.19 REMARK 500 O HOH 102 O HOH 468 2645 2.19 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 LYS B 98 CD LYS B 98 CE 0.284 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 LYS B 16 CG - CD - CE ANGL. DEV. = 25.9 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 186 DISTANCE = 6.30 ANGSTROMS REMARK 525 HOH 265 DISTANCE = 5.01 ANGSTROMS REMARK 525 HOH 277 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH 290 DISTANCE = 5.67 ANGSTROMS REMARK 525 HOH 301 DISTANCE = 8.57 ANGSTROMS REMARK 525 HOH 303 DISTANCE = 9.54 ANGSTROMS REMARK 525 HOH 314 DISTANCE = 6.28 ANGSTROMS REMARK 525 HOH 342 DISTANCE = 7.49 ANGSTROMS REMARK 525 HOH 348 DISTANCE = 6.84 ANGSTROMS REMARK 525 HOH 373 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH 386 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 389 DISTANCE = 8.85 ANGSTROMS REMARK 525 HOH 393 DISTANCE = 6.85 ANGSTROMS REMARK 525 HOH 425 DISTANCE = 10.09 ANGSTROMS REMARK 525 HOH 455 DISTANCE = 8.44 ANGSTROMS REMARK 525 HOH 460 DISTANCE = 7.46 ANGSTROMS REMARK 525 HOH 463 DISTANCE = 7.31 ANGSTROMS REMARK 525 HOH 468 DISTANCE = 6.23 ANGSTROMS REMARK 525 HOH 490 DISTANCE = 8.61 ANGSTROMS REMARK 525 HOH 503 DISTANCE = 5.52 ANGSTROMS REMARK 525 HOH 504 DISTANCE = 7.84 ANGSTROMS REMARK 525 HOH 506 DISTANCE = 5.61 ANGSTROMS REMARK 525 HOH 510 DISTANCE = 5.79 ANGSTROMS REMARK 525 HOH 515 DISTANCE = 5.53 ANGSTROMS REMARK 525 HOH 526 DISTANCE = 8.52 ANGSTROMS DBREF 1M6C A 1 153 UNP P02189 MYG_PIG 2 154 DBREF 1M6C B 1 153 UNP P02189 MYG_PIG 2 154 SEQADV 1M6C ASN A 68 UNP P02189 VAL 68 ENGINEERED SEQADV 1M6C ASN B 68 UNP P02189 VAL 68 ENGINEERED SEQRES 1 A 153 GLY LEU SER ASP GLY GLU TRP GLN LEU VAL LEU ASN VAL SEQRES 2 A 153 TRP GLY LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN SEQRES 3 A 153 GLU VAL LEU ILE ARG LEU PHE LYS GLY HIS PRO GLU THR SEQRES 4 A 153 LEU GLU LYS PHE ASP LYS PHE LYS HIS LEU LYS SER GLU SEQRES 5 A 153 ASP GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY SEQRES 6 A 153 ASN THR ASN LEU THR ALA LEU GLY GLY ILE LEU LYS LYS SEQRES 7 A 153 LYS GLY HIS HIS GLU ALA GLU LEU THR PRO LEU ALA GLN SEQRES 8 A 153 SER HIS ALA THR LYS HIS LYS ILE PRO VAL LYS TYR LEU SEQRES 9 A 153 GLU PHE ILE SER GLU ALA ILE ILE GLN VAL LEU GLN SER SEQRES 10 A 153 LYS HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA SEQRES 11 A 153 MET SER LYS ALA LEU GLU LEU PHE ARG ASN ASP MET ALA SEQRES 12 A 153 ALA LYS TYR LYS GLU LEU GLY PHE GLN GLY SEQRES 1 B 153 GLY LEU SER ASP GLY GLU TRP GLN LEU VAL LEU ASN VAL SEQRES 2 B 153 TRP GLY LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN SEQRES 3 B 153 GLU VAL LEU ILE ARG LEU PHE LYS GLY HIS PRO GLU THR SEQRES 4 B 153 LEU GLU LYS PHE ASP LYS PHE LYS HIS LEU LYS SER GLU SEQRES 5 B 153 ASP GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY SEQRES 6 B 153 ASN THR ASN LEU THR ALA LEU GLY GLY ILE LEU LYS LYS SEQRES 7 B 153 LYS GLY HIS HIS GLU ALA GLU LEU THR PRO LEU ALA GLN SEQRES 8 B 153 SER HIS ALA THR LYS HIS LYS ILE PRO VAL LYS TYR LEU SEQRES 9 B 153 GLU PHE ILE SER GLU ALA ILE ILE GLN VAL LEU GLN SER SEQRES 10 B 153 LYS HIS PRO GLY ASP PHE GLY ALA ASP ALA GLN GLY ALA SEQRES 11 B 153 MET SER LYS ALA LEU GLU LEU PHE ARG ASN ASP MET ALA SEQRES 12 B 153 ALA LYS TYR LYS GLU LEU GLY PHE GLN GLY HET HEM A 154 43 HET CMO A 155 2 HET HEM B 154 43 HET CMO B 155 2 HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE HETNAM CMO CARBON MONOXIDE HETSYN HEM HEME FORMUL 3 HEM 2(C34 H32 FE N4 O4) FORMUL 4 CMO 2(C O) FORMUL 7 HOH *487(H2 O) HELIX 1 1 ASP A 4 GLY A 35 1 32 HELIX 2 2 PRO A 37 LYS A 42 5 6 HELIX 3 3 ASP A 44 PHE A 46 5 3 HELIX 4 4 GLU A 52 ALA A 57 1 6 HELIX 5 5 GLU A 59 LYS A 78 1 20 HELIX 6 6 GLU A 83 ALA A 94 1 12 HELIX 7 7 VAL A 101 LYS A 118 1 18 HELIX 8 8 ALA A 125 GLU A 148 1 24 HELIX 9 9 ASP B 4 GLY B 35 1 32 HELIX 10 10 PRO B 37 LYS B 42 1 6 HELIX 11 11 ASP B 44 PHE B 46 5 3 HELIX 12 12 GLU B 52 ALA B 57 1 6 HELIX 13 13 GLU B 59 LYS B 78 1 20 HELIX 14 14 GLU B 83 ALA B 94 1 12 HELIX 15 15 VAL B 101 LYS B 118 1 18 HELIX 16 16 PRO B 120 ASP B 122 5 3 HELIX 17 17 ALA B 125 LEU B 149 1 25 LINK FE HEM A 154 NE2 HIS A 93 LINK FE HEM B 154 NE2 HIS B 93 LINK FE HEM A 154 C CMO A 155 LINK FE HEM B 154 C CMO B 155 CRYST1 122.140 42.300 91.550 90.00 92.49 90.00 I 1 21 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 0.008187 0.000000 0.000356 0.00000 SCALE2 0.000000 0.023641 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010933 0.00000