[Scop | Full Entry | Seq (local cached copy) | More Options ]
HEADER OXYGEN STORAGE/TRANSPORT 08-NOV-05 2D5X
TITLE CRYSTAL STRUCTURE OF CARBONMONOXY HORSE HEMOGLOBIN
TITLE 2 COMPLEXED WITH L35
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMOGLOBIN ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEMOGLOBIN ALPHA CHAIN, ALPHA-GLOBIN;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HEMOGLOBIN BETA SUBUNIT;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: HEMOGLOBIN BETA CHAIN, BETA-GLOBIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 TISSUE: RED CELL;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 7 ORGANISM_COMMON: HORSE;
SOURCE 8 TISSUE: RED CELL
KEYWDS HEMOGLOBIN, L35, ALLOSTERIC EFFECTOR, CRYSTAL STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YOKOYAMA,S.NEYA,A.TSUNESHIGE,T.YONETANI,S.Y.PARK,J.R.TAME
REVDAT 1 07-MAR-06 2D5X 0
JRNL AUTH T.YOKOYAMA,S.NEYA,A.TSUNESHIGE,T.YONETANI,S.Y.PARK,
JRNL AUTH 2 J.R.TAME
JRNL TITL R-STATE HAEMOGLOBIN WITH LOW OXYGEN AFFINITY:
JRNL TITL 2 CRYSTAL STRUCTURES OF DEOXY HUMAN AND CARBONMONOXY
JRNL TITL 3 HORSE HAEMOGLOBIN BOUND TO THE EFFECTOR MOLECULE
JRNL TITL 4 L35
JRNL REF J.MOL.BIOL. V. 356 790 2006
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 43215
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2284
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2001
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2567
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.32000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : 0.82000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.265
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2416 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3301 ; 1.250 ; 2.074
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 4.506 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 95 ;34.164 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 364 ;13.865 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;15.187 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 347 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1838 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1245 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1671 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 185 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 53 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.153 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1426 ; 0.655 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2267 ; 1.238 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1004 ; 2.005 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1034 ; 3.169 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D5X 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 (2007-05-01)
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ .
REMARK 100 THE RCSB ID CODE IS RCSB025026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 56.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15800
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG1000, 50MM LICL, 50MM MES,
REMARK 280 0.5MM L35, PH 6.0, BATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 43.50800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.50800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.16850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.72100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.16850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.72100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.50800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.16850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.72100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 43.50800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.16850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.72100
REMARK 290 SMTRY3 8 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 107.44200
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 87.01600
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 C CMO 1148 1.68
REMARK 500 FE HEM A 142 C CMO 1143 1.70
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2D5Z RELATED DB: PDB
REMARK 900 CARBONMONOXY HUMAN HEMOGLOBIN COMPLEXED WITH L35
REMARK 900 RELATED ID: 2D60 RELATED DB: PDB
REMARK 900 CARBONMONOXY HUMAN HEMOGLOBIN COMPLEXED WITH L35
DBREF 2D5X A 1 141 UNP P01958 HBA_HORSE 1 141
DBREF 2D5X B 1 146 UNP P02062 HBB_HORSE 1 146
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 ASN 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 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
HET HEM A 142 43
HET CMO 1143 2
HET HEM B 147 43
HET CMO 1148 2
HET L35 1200 25
HET L35 1201 25
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CMO CARBON MONOXIDE
HETNAM L35 2-[4-({[(3,5-DICHLOROPHENYL)AMINO]CARBONYL}AMINO)
HETNAM 2 L35 PHENOXY]-2-METHYLPROPANOIC ACID
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 CMO 2(C O)
FORMUL 7 L35 2(C17 H16 CL2 N2 O4)
FORMUL 9 HOH *224(H2 O)
HELIX 1 1 SER A 3 VAL A 17 1 15
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 HIS A 72 ASP A 74 5 3
HELIX 6 6 ASP A 75 LEU A 80 1 6
HELIX 7 7 LEU A 80 LYS A 90 1 11
HELIX 8 8 ASP A 94 LEU A 113 1 20
HELIX 9 9 THR A 118 THR A 137 1 20
HELIX 10 10 SER B 4 ASP B 16 1 13
HELIX 11 11 ASN B 19 TYR B 35 1 17
HELIX 12 12 PRO B 36 GLY B 46 5 11
HELIX 13 13 ASN B 50 ASN B 57 1 8
HELIX 14 14 ASN B 57 HIS B 76 1 20
HELIX 15 15 HIS B 77 ASP B 79 5 3
HELIX 16 16 ASN B 80 LYS B 95 1 16
HELIX 17 17 PRO B 100 GLY B 119 1 20
HELIX 18 18 LYS B 120 PHE B 122 5 3
HELIX 19 19 THR B 123 ALA B 142 1 20
HELIX 20 20 HIS B 143 HIS B 146 5 4
LINK NE2 HIS A 87 FE HEM A 142
LINK NE2 HIS B 92 FE HEM B 147
CRYST1 62.337 107.442 87.016 90.00 90.00 90.00 C 2 2 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 0.016042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011492 0.00000