HEADER OXYGEN STORAGE/TRANSPORT 11-AUG-98 1MWD
TITLE WILD TYPE DEOXY MYOGLOBIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (MYOGLOBIN);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: MYOGLOBIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PLCII;
SOURCE 9 OTHER_DETAILS: RECOMBINANT PROTEIN EXPRESSED IN E.COLI
KEYWDS OXYGEN STORAGE, DEOXY MYOGLOBIN, OXYGEN STORAGE-TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.N.MURSHUDOV,S.KRZYWDA,A.M.BRZOZOWSKI,M.JASKOLSKI,E.E.SCOTT,
AUTHOR 2 A.A.KLIZAS,Q.H.GIBSON,J.S.OLSON,A.J.WILKINSON
REVDAT 5 14-FEB-24 1MWD 1 REMARK
REVDAT 4 24-FEB-09 1MWD 1 VERSN
REVDAT 3 01-APR-03 1MWD 1 JRNL
REVDAT 2 29-DEC-99 1MWD 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 19-AUG-98 1MWD 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,A.J.WILKINSON
JRNL TITL STABILIZING BOUND O2 IN MYOGLOBIN BY VALINE68 (E11) TO
JRNL TITL 2 ASPARAGINE SUBSTITUTION.
JRNL REF BIOCHEMISTRY V. 37 15896 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9843395
JRNL DOI 10.1021/BI9812470
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
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 : 41019
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) : 0.196
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2047
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2394
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 456
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.38000
REMARK 3 B22 (A**2) : 1.90000
REMARK 3 B33 (A**2) : -5.20000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.13000
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): 2.580
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.030 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.031 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.012 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.117 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.190 ; NULL
REMARK 3 MULTIPLE TORSION (A) : 0.275 ; NULL
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) : 3.800 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 16.400; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 41.600; 0.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.222 ; 4.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.180 ; 6.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.010 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.900 ; 6.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008364.
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
REMARK 200 PH : 7.1
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 : 42068
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 96.5
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
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 <I/SIGMA(I)> 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 (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 PHOSPHATE BUFFER 72-80% SATURATED
REMARK 280 AMMONIUM SULPHATE, PH 7.1
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,Y+1/2,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y,-Z+1/2
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 21.07000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.78550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.68842
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.78550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 45.68842
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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: 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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 4 CB - CG - OD1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 4 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 4 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 VAL B 13 CA - CB - CG1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 VAL B 13 CA - CB - CG2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG B 31 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 GLU B 83 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 HIS B 93 CE1 - NE2 - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 139 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TYR B 146 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 GLN B 152 N - CA - CB ANGL. DEV. = 16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 20 63.88 -167.02
REMARK 500 LYS A 79 62.19 38.23
REMARK 500 LYS A 79 -129.76 49.01
REMARK 500 THR A 95 -77.04 -93.61
REMARK 500 PHE A 123 70.76 -117.03
REMARK 500 ASP B 20 63.18 -165.68
REMARK 500 LYS B 79 -129.17 53.27
REMARK 500 HIS B 119 51.02 -141.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 154 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 93 NE2
REMARK 620 2 HEM A 154 NA 91.5
REMARK 620 3 HEM A 154 NB 92.9 88.7
REMARK 620 4 HEM A 154 NC 101.2 167.3 90.7
REMARK 620 5 HEM A 154 ND 99.4 87.3 167.1 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 154 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 93 NE2
REMARK 620 2 HEM B 154 NA 94.4
REMARK 620 3 HEM B 154 NB 92.7 91.1
REMARK 620 4 HEM B 154 NC 97.2 168.4 88.6
REMARK 620 5 HEM B 154 ND 99.6 90.4 167.5 87.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 154
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 154
DBREF 1MWD A 1 153 UNP P02189 MYG_PIG 2 154
DBREF 1MWD B 1 153 UNP P02189 MYG_PIG 2 154
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 VAL 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 VAL 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 HEM B 154 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 5 HOH *456(H2 O)
HELIX 1 1 ASP A 4 GLY A 35 1 32
HELIX 2 2 PRO A 37 LYS A 42 1 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 PRO A 120 ASP A 122 5 3
HELIX 9 9 ALA A 125 LEU A 149 1 25
HELIX 10 10 ASP B 4 GLY B 35 1 32
HELIX 11 11 PRO B 37 LYS B 42 5 6
HELIX 12 12 ASP B 44 PHE B 46 5 3
HELIX 13 13 GLU B 52 ALA B 57 1 6
HELIX 14 14 GLU B 59 LYS B 78 1 20
HELIX 15 15 GLU B 83 THR B 95 1 13
HELIX 16 16 VAL B 101 LYS B 118 1 18
HELIX 17 17 PRO B 120 ASP B 122 5 3
HELIX 18 18 ALA B 125 LEU B 149 1 25
LINK NE2 HIS A 93 FE HEM A 154 1555 1555 2.27
LINK NE2 HIS B 93 FE HEM B 154 1555 1555 2.28
SITE 1 AC1 16 LYS A 42 PHE A 43 HIS A 64 VAL A 68
SITE 2 AC1 16 ALA A 71 LEU A 89 SER A 92 HIS A 93
SITE 3 AC1 16 HIS A 97 ILE A 99 TYR A 103 HOH A 206
SITE 4 AC1 16 HOH A 208 HOH A 232 HOH A 270 HOH A 348
SITE 1 AC2 19 THR B 39 LYS B 42 PHE B 43 LYS B 45
SITE 2 AC2 19 HIS B 64 THR B 67 VAL B 68 ALA B 71
SITE 3 AC2 19 LEU B 89 SER B 92 HIS B 93 HIS B 97
SITE 4 AC2 19 ILE B 99 TYR B 103 HOH B 192 HOH B 194
SITE 5 AC2 19 HOH B 200 HOH B 214 HOH B 309
CRYST1 122.120 42.140 91.490 90.00 92.85 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 0.008189 0.000000 0.000408 0.00000
SCALE2 0.000000 0.023730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
