HEADER OXIDOREDUCTASE/TRANSFERASE 14-DEC-99 1DWV
TITLE MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
TITLE 2 N-HYDROXYARGININE AND 4-AMINO TETRAHYDROBIOPTERIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: OXYGENASE DOMAIN 65-498;
COMPND 5 SYNONYM: INDUCIBLE NOS TYPE II, MAC-NOS;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: MURINE INDUCIBLE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 CELL: MACROPHAGE;
SOURCE 6 PLASMID: PCWORI;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS OXIDOREDUCTASE TRANSFERASE COMPLEX, COMPLEX
KEYWDS 2 (OXIDOREDUCTASE/TRANSFERASE), NITRIC OXIDE MONOOXYGENASE,
KEYWDS 3 HEME, DIMER, INTERMEDIATE, PTERIN,
KEYWDS 4 4-AMINO-TETRAHYDROBIOPTERIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.CRANE,A.S.ARVAI,E.D.GETZOFF,D.J.STUEHR,J.A.TAINER
REVDAT 5 16-JUN-09 1DWV 1 REMARK KEYWDS
REVDAT 4 24-FEB-09 1DWV 1 VERSN
REVDAT 3 04-MAY-00 1DWV 1 JRNL
REVDAT 2 10-APR-00 1DWV 1 REMARK
REVDAT 1 06-FEB-00 1DWV 0
JRNL AUTH B.R.CRANE,A.S.ARVAI,S.GHOSH,E.D.GETZOFF,D.J.STUEHR,
JRNL AUTH 2 J.A.TAINER
JRNL TITL STRUCTURES OF THE N(OMEGA)-HYDROXY-L-ARGININE
JRNL TITL 2 COMPLEX OF INDUCIBLE NITRIC OXIDE SYNTHASE
JRNL TITL 3 OXYGENASE DIMER WITH ACTIVE ANDINACTIVE PTERINS
JRNL REF BIOCHEMISTRY V. 39 4608 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10769116
JRNL DOI 10.1021/BI992409A
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.R.CRANE,R.A.ROSENFELD,A.S.ARVAI,D.K.GHOSH,
REMARK 1 AUTH 2 S.GHOSH,J.A.TAINER,D.J.STUEHR,E.D.GETZOFF
REMARK 1 TITL N-TERMINAL DOMAIN SWAPPING AND METAL ION BINDING
REMARK 1 TITL 2 IN NITRIC OXIDE SYNTHASE DIMERIZATION
REMARK 1 REF EMBO J. V. 18 6271 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 10562539
REMARK 1 DOI 10.1093/EMBOJ/18.22.6271
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.K.GHOSH,B.R.CRANE,S.GHOSH,D.WOLAN,R.GACHHUI,
REMARK 1 AUTH 2 C.CROOKS,A.PRESTA,J.A.TAINER,E.D.GETZOFF,D.J.STUEHR
REMARK 1 TITL INDUCIBLE NITRIC OXIDE SYNTHASE: ROLE OF THE
REMARK 1 TITL 2 N-TERMINAL BETA-HAIRPIN HOOK AND PTERIN-BINDING
REMARK 1 TITL 3 SEGMENT IN DIMERIZATION AND TETRAHYDROBIOPTERIN
REMARK 1 TITL 4 INTERACTION
REMARK 1 REF EMBO J. V. 18 6260 1999
REMARK 1 REFN ISSN 0261-4189
REMARK 1 PMID 10562538
REMARK 1 DOI 10.1093/EMBOJ/18.22.6260
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,D.K.GHOSH,C.WU,E.D.GETZOFF,
REMARK 1 AUTH 2 D.J.STUEHR,J.A.TAINER
REMARK 1 TITL STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 1 TITL 2 WITH PTERIN AND SUBSTRATE
REMARK 1 REF SCIENCE V. 279 2121 1998
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 9516116
REMARK 1 DOI 10.1126/SCIENCE.279.5359.2121
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.R.CRANE,A.S.ARVAI,R.GACHHUI,C.WU,D.K.GHOSH,
REMARK 1 AUTH 2 E.D.GETZOFF,D.J.STUEHR,J.A.TAINER
REMARK 1 TITL THE STRUCTURE OF NITRIC OXIDE SYNTHASE OXYGENASE
REMARK 1 TITL 2 DOMAIN AND INHIBITOR COMPLEXES
REMARK 1 REF SCIENCE V. 278 425 1997
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 9334294
REMARK 1 DOI 10.1126/SCIENCE.278.5337.425
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3560711.67
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.000000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.1
REMARK 3 NUMBER OF REFLECTIONS : 58616
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 SET) : 0.247
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2952
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.6
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7493
REMARK 3 BIN R VALUE (WORKING SET) : 0.369
REMARK 3 BIN FREE R VALUE : 0.363
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 395
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 188
REMARK 3 SOLVENT ATOMS : 425
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -18.35
REMARK 3 B22 (A**2) : -18.35
REMARK 3 B33 (A**2) : 36.71
REMARK 3 B12 (A**2) : -4.90
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.48
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.4
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.25
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.48 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.50 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.06 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.03 ; 2.50
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : 0.04 ; 100
REMARK 3 GROUP 1 B-FACTOR (A**2) : 2.1 ; 0.95
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19X.HEME
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.
REMARK 3 TOPOLOGY FILE 2 : TOPH19X.H
REMARK 3 TOPOLOGY FILE 3 : TOPH19X.4AM
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DWV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-99.
REMARK 100 THE PDBE ID CODE IS EBI-4465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-98
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 : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58616
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: CNS 0.4, X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.0
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.0
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.06667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.13333
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 57.10000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 95.16667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 19.03333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 38.06667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 76.13333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 95.16667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 57.10000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 19.03333
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 300
REMARK 300 DETAILS:BIOLOGICAL_UNIT: INOS OXYGENASE DOMAIN ACTIVE
REMARK 300 AS A DIMER
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -224.6 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 212.98000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 57.10000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.36 KCAL/MOL
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 319.47000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 184.44609
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 190.33333
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 ZN ZN A 903 LIES ON A SPECIAL POSITION.
REMARK 375 ZN ZN B 903 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2181 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2079 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2166 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2185 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2186 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 EACH NOS DIMER IS COVALENTLY LINKED BY A TETRATHIOLATE ZINC
REMARK 400 CENTER THAT RESIDES ON THE MOLECULAR SYMMETRY AXIS.
REMARK 400
REMARK 400 4-AMINO TETRAHYDROBIOPTERIN IS BOUND IN A PROTONATED
REMARK 400 QUINONOID FORM
REMARK 400
REMARK 400 NOH-L-ARGININE (HAR) IS LIKELY PROTONATED ON N OMEGA AT THE
REMARK 400 PH 6.0 OF THESE CRYSTALS
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 PRO A 123 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLY A 365 N - CA - C ANGL. DEV. = -15.3 DEGREES
REMARK 500 ARG B 80 NE - CZ - NH2 ANGL. DEV. = 3.0 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 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 SER A 100 -63.63 -17.83
REMARK 500 ASN A 115 68.25 -114.82
REMARK 500 ARG A 197 -6.31 -55.85
REMARK 500 ILE A 234 134.58 -34.31
REMARK 500 SER A 245 -80.73 -94.50
REMARK 500 THR A 270 -166.58 -69.35
REMARK 500 LYS A 329 -38.43 -142.89
REMARK 500 CYS A 361 70.46 -157.15
REMARK 500 ARG A 382 -140.61 -115.18
REMARK 500 CYS A 451 107.90 -164.41
REMARK 500 LEU A 479 -162.32 -100.35
REMARK 500 SER B 100 -72.81 -13.52
REMARK 500 ARG B 197 -6.91 -59.49
REMARK 500 SER B 245 -87.43 -101.32
REMARK 500 THR B 270 -174.34 -68.88
REMARK 500 LYS B 329 -37.25 -137.81
REMARK 500 CYS B 361 72.19 -157.99
REMARK 500 ARG B 382 -129.99 -115.27
REMARK 500 CYS B 451 103.73 -161.45
REMARK 500 LEU B 479 -161.66 -102.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 CYS B 378 23.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
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 ZN A 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 104 SG
REMARK 620 2 CYS A 109 SG 97.3
REMARK 620 3 CYS A 104 SG 111.4 124.7
REMARK 620 4 CYS A 109 SG 124.6 103.3 97.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 903 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 104 SG
REMARK 620 2 CYS B 104 SG 127.6
REMARK 620 3 CYS B 109 SG 111.6 98.7
REMARK 620 4 CYS B 109 SG 100.5 111.8 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 194 SG
REMARK 620 2 HEM A 901 NA 105.0
REMARK 620 3 HEM A 901 NB 92.1 90.9
REMARK 620 4 HEM A 901 NC 94.8 160.2 88.7
REMARK 620 5 HEM A 901 ND 99.0 86.3 168.9 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEM B 901 NB
REMARK 620 2 HEM B 901 NC 88.7
REMARK 620 3 HEM B 901 NA 90.5 164.0
REMARK 620 4 CYS B 194 SG 92.3 89.0 106.9
REMARK 620 5 HEM B 901 ND 169.4 89.5 88.4 98.1
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: KABSCH AND SANDER
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AB A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAR A 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4AB B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAR B 909
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DWW RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 N-HYDROXYARGININE AND DIHYDROBIOPTERIN
REMARK 900 RELATED ID: 1DWX RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 N-HYDROXYARGININE AND TETRAHYDROBIOPTERIN
REMARK 900 RELATED ID: 1QOM RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 (DELTA 65) WITH SWAPPED N-TERMINAL HOOK
REMARK 900 RELATED ID: 1NOC RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN
REMARK 900 (DELTA 114) COMPLEXED WITH TYPE I E. COLI CHLORAMPHENICOL
REMARK 900 ACETYL TRANSFERASE AND IMIDAZOLE
REMARK 900 RELATED ID: 1NOS RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN
REMARK 900 (DELTA 114), IMIDAZOLE COMPLEX
REMARK 900 RELATED ID: 2NOS RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DOMAIN
REMARK 900 (DELTA 114), AMINOGUANIDINE COMPLEX
REMARK 900 RELATED ID: 1NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 (DELTA 65) WITH TETRAHYDROBIOPTERIN AND SUBSTRATE
REMARK 900 L-ARGININE
REMARK 900 RELATED ID: 2NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 (DELTA 65) WITH TETRAHYDROBIOPTERIN AND WATER BOUND IN
REMARK 900 ACTIVE CENTER
REMARK 900 RELATED ID: 3NOD RELATED DB: PDB
REMARK 900 MURINE INDUCIBLE NITRIC OXIDE SYNTHASE OXYGENASE DIMER
REMARK 900 (DELTA 65) WITH TETRAHYDROBIOPTERIN AND PRODUCT ANALOGUE
REMARK 900 L-THIOCITRULLINE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 PROTEIN WAS EXPRESSED WITH A COOH-TERMINAL HIS6 TAG.
DBREF 1DWV A 77 496 UNP P29477 NOS2_MOUSE 77 496
DBREF 1DWV B 77 496 UNP P29477 NOS2_MOUSE 77 496
SEQRES 1 A 420 GLN TYR VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE
SEQRES 2 A 420 LEU HIS ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE
SEQRES 3 A 420 THR CYS LYS SER LYS SER CYS LEU GLY SER ILE MET ASN
SEQRES 4 A 420 PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR
SEQRES 5 A 420 PRO LEU GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE
SEQRES 6 A 420 ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU
SEQRES 7 A 420 GLU HIS LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE
SEQRES 8 A 420 GLU THR THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU
SEQRES 9 A 420 ILE PHE ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG
SEQRES 10 A 420 CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE
SEQRES 11 A 420 ASP ALA ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN
SEQRES 12 A 420 HIS ILE CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY
SEQRES 13 A 420 ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER
SEQRES 14 A 420 ASP GLY LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU
SEQRES 15 A 420 ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE
SEQRES 16 A 420 ARG GLY ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS
SEQRES 17 A 420 ILE ASP LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP
SEQRES 18 A 420 VAL LEU PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO
SEQRES 19 A 420 GLU VAL PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL
SEQRES 20 A 420 THR MET GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU
SEQRES 21 A 420 GLY LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET
SEQRES 22 A 420 LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO
SEQRES 23 A 420 PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG
SEQRES 24 A 420 ASP PHE CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU
SEQRES 25 A 420 VAL GLY ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA
SEQRES 26 A 420 SER LEU TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL
SEQRES 27 A 420 ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE
SEQRES 28 A 420 MET ASP HIS HIS THR ALA SER GLU SER PHE MET LYS HIS
SEQRES 29 A 420 MET GLN ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA
SEQRES 30 A 420 ASP TRP ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE
SEQRES 31 A 420 THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU
SEQRES 32 A 420 SER PRO PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR
SEQRES 33 A 420 HIS ILE TRP GLN
SEQRES 1 B 420 GLN TYR VAL ARG ILE LYS ASN TRP GLY SER GLY GLU ILE
SEQRES 2 B 420 LEU HIS ASP THR LEU HIS HIS LYS ALA THR SER ASP PHE
SEQRES 3 B 420 THR CYS LYS SER LYS SER CYS LEU GLY SER ILE MET ASN
SEQRES 4 B 420 PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO THR
SEQRES 5 B 420 PRO LEU GLU GLU LEU LEU PRO HIS ALA ILE GLU PHE ILE
SEQRES 6 B 420 ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE GLU
SEQRES 7 B 420 GLU HIS LEU ALA ARG LEU GLU ALA VAL THR LYS GLU ILE
SEQRES 8 B 420 GLU THR THR GLY THR TYR GLN LEU THR LEU ASP GLU LEU
SEQRES 9 B 420 ILE PHE ALA THR LYS MET ALA TRP ARG ASN ALA PRO ARG
SEQRES 10 B 420 CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL PHE
SEQRES 11 B 420 ASP ALA ARG ASN CYS SER THR ALA GLN GLU MET PHE GLN
SEQRES 12 B 420 HIS ILE CYS ARG HIS ILE LEU TYR ALA THR ASN ASN GLY
SEQRES 13 B 420 ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG SER
SEQRES 14 B 420 ASP GLY LYS HIS ASP PHE ARG LEU TRP ASN SER GLN LEU
SEQRES 15 B 420 ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY THR ILE
SEQRES 16 B 420 ARG GLY ASP ALA ALA THR LEU GLU PHE THR GLN LEU CYS
SEQRES 17 B 420 ILE ASP LEU GLY TRP LYS PRO ARG TYR GLY ARG PHE ASP
SEQRES 18 B 420 VAL LEU PRO LEU VAL LEU GLN ALA ASP GLY GLN ASP PRO
SEQRES 19 B 420 GLU VAL PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU VAL
SEQRES 20 B 420 THR MET GLU HIS PRO LYS TYR GLU TRP PHE GLN GLU LEU
SEQRES 21 B 420 GLY LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN MET
SEQRES 22 B 420 LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO ALA CYS PRO
SEQRES 23 B 420 PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL ARG
SEQRES 24 B 420 ASP PHE CYS ASP THR GLN ARG TYR ASN ILE LEU GLU GLU
SEQRES 25 B 420 VAL GLY ARG ARG MET GLY LEU GLU THR HIS THR LEU ALA
SEQRES 26 B 420 SER LEU TRP LYS ASP ARG ALA VAL THR GLU ILE ASN VAL
SEQRES 27 B 420 ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR ILE
SEQRES 28 B 420 MET ASP HIS HIS THR ALA SER GLU SER PHE MET LYS HIS
SEQRES 29 B 420 MET GLN ASN GLU TYR ARG ALA ARG GLY GLY CYS PRO ALA
SEQRES 30 B 420 ASP TRP ILE TRP LEU VAL PRO PRO VAL SER GLY SER ILE
SEQRES 31 B 420 THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL LEU
SEQRES 32 B 420 SER PRO PHE TYR TYR TYR GLN ILE GLU PRO TRP LYS THR
SEQRES 33 B 420 HIS ILE TRP GLN
HET ZN A 903 1
HET SO4 A 904 5
HET SO4 A 905 5
HET SO4 A 906 5
HET SO4 A 907 5
HET ZN B 903 1
HET SO4 B 904 5
HET SO4 B 905 5
HET SO4 B 906 5
HET SO4 B 907 5
HET HEM A 901 43
HET 4AB A 902 17
HET HAR A 909 13
HET HEM B 901 43
HET 4AB B 902 17
HET HAR B 909 13
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 4AB 2,4-DIAMINO-6-[2,3-DIHYDROXY-PROP-3-YL]-5,6,
HETNAM 2 4AB 7,8-TETRAHYDROPTERIDINE
HETNAM HAR N-OMEGA-HYDROXY-L-ARGININE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 8(O4 S 2-)
FORMUL 13 HEM 2(C34 H32 FE N4 O4)
FORMUL 14 4AB 2(C9 H16 N6 O2)
FORMUL 15 HAR 2(C6 H14 N4 O3)
FORMUL 19 HOH *425(H2 O1)
HELIX 1 1 THR A 93 ALA A 98 5 6
HELIX 2 2 PRO A 116 LEU A 119 5 4
HELIX 3 3 PRO A 129 GLY A 146 1 18
HELIX 4 4 LYS A 152 GLY A 171 1 20
HELIX 5 5 THR A 176 ASN A 190 1 15
HELIX 6 6 GLY A 196 TRP A 200 5 5
HELIX 7 7 THR A 213 ASN A 230 1 18
HELIX 8 8 ASN A 231 ASN A 233 5 3
HELIX 9 9 THR A 277 LEU A 287 1 11
HELIX 10 10 PHE A 333 GLY A 337 5 5
HELIX 11 11 GLY A 369 VAL A 374 1 6
HELIX 12 12 VAL A 374 ASP A 379 1 6
HELIX 13 13 ILE A 385 MET A 393 1 9
HELIX 14 14 THR A 399 SER A 402 5 4
HELIX 15 15 LEU A 403 GLN A 423 1 21
HELIX 16 16 ASP A 429 GLY A 449 1 21
HELIX 17 17 ASP A 454 VAL A 459 1 6
HELIX 18 18 SER A 463 THR A 467 5 5
HELIX 19 19 PRO A 468 HIS A 471 5 4
HELIX 20 20 GLU A 488 THR A 492 5 5
HELIX 21 21 THR B 93 ALA B 98 5 6
HELIX 22 22 PRO B 116 LEU B 119 5 4
HELIX 23 23 PRO B 129 GLY B 146 1 18
HELIX 24 24 LYS B 152 GLY B 171 1 20
HELIX 25 25 THR B 176 ASN B 190 1 15
HELIX 26 26 GLY B 196 TRP B 200 5 5
HELIX 27 27 THR B 213 ASN B 230 1 18
HELIX 28 28 ASN B 231 ASN B 233 5 3
HELIX 29 29 THR B 277 LEU B 287 1 11
HELIX 30 30 PRO B 316 VAL B 320 5 5
HELIX 31 31 PHE B 333 GLY B 337 5 5
HELIX 32 32 GLY B 369 VAL B 374 1 6
HELIX 33 33 ILE B 385 ARG B 392 1 8
HELIX 34 34 THR B 399 SER B 402 5 4
HELIX 35 35 LEU B 403 GLN B 423 1 21
HELIX 36 36 ASP B 429 GLY B 449 1 21
HELIX 37 37 ASP B 454 VAL B 459 1 6
HELIX 38 38 SER B 463 THR B 467 5 5
HELIX 39 39 THR B 467 HIS B 471 5 5
HELIX 40 40 GLU B 488 THR B 492 5 5
SHEET 1 AA 2 VAL A 79 LYS A 82 0
SHEET 2 AA 2 ILE A 89 ASP A 92 -1 O LEU A 90 N ILE A 81
SHEET 1 AB 4 GLN A 204 ASP A 207 0
SHEET 2 AB 4 ALA A 237 VAL A 240 1 O ILE A 238 N PHE A 206
SHEET 3 AB 4 PHE A 363 ASN A 364 -1 O ASN A 364 N ALA A 237
SHEET 4 AB 4 ALA A 345 VAL A 346 -1 O VAL A 346 N PHE A 363
SHEET 1 AC 3 ARG A 252 LEU A 253 0
SHEET 2 AC 3 LEU A 301 GLN A 304 -1 O GLN A 304 N ARG A 252
SHEET 3 AC 3 GLU A 311 PHE A 313 -1 O GLU A 311 N LEU A 303
SHEET 1 AD 2 GLY A 263 TYR A 264 0
SHEET 2 AD 2 ARG A 272 GLY A 273 -1 O ARG A 272 N TYR A 264
SHEET 1 AE 2 GLU A 322 THR A 324 0
SHEET 2 AE 2 LYS A 339 TYR A 341 -1 O TRP A 340 N VAL A 323
SHEET 1 AF 3 LEU A 356 PHE A 358 0
SHEET 2 AF 3 LEU A 350 VAL A 353 -1 O LEU A 351 N PHE A 358
SHEET 3 AF 3 PHE A 482 TYR A 484 -1 O PHE A 482 N GLU A 352
SHEET 1 AG 2 TYR A 367 MET A 368 0
SHEET 2 AG 2 ILE A 427 MET A 428 1 N MET A 428 O TYR A 367
SHEET 1 BA 2 VAL B 79 LYS B 82 0
SHEET 2 BA 2 ILE B 89 ASP B 92 -1 O LEU B 90 N ILE B 81
SHEET 1 BB 4 GLN B 204 ASP B 207 0
SHEET 2 BB 4 ALA B 237 VAL B 240 1 O ILE B 238 N PHE B 206
SHEET 3 BB 4 PHE B 363 ASN B 364 -1 O ASN B 364 N ALA B 237
SHEET 4 BB 4 ALA B 345 VAL B 346 -1 O VAL B 346 N PHE B 363
SHEET 1 BC 3 ARG B 252 LEU B 253 0
SHEET 2 BC 3 LEU B 301 GLN B 304 -1 O GLN B 304 N ARG B 252
SHEET 3 BC 3 GLU B 311 PHE B 313 -1 O GLU B 311 N LEU B 303
SHEET 1 BD 2 GLY B 263 GLN B 265 0
SHEET 2 BD 2 ILE B 271 GLY B 273 -1 O ARG B 272 N TYR B 264
SHEET 1 BE 2 GLU B 322 THR B 324 0
SHEET 2 BE 2 LYS B 339 TYR B 341 -1 O TRP B 340 N VAL B 323
SHEET 1 BF 3 LEU B 356 PHE B 358 0
SHEET 2 BF 3 LEU B 350 VAL B 353 -1 O LEU B 351 N PHE B 358
SHEET 3 BF 3 PHE B 482 TYR B 484 -1 O PHE B 482 N GLU B 352
SHEET 1 BG 2 TYR B 367 MET B 368 0
SHEET 2 BG 2 ILE B 427 MET B 428 1 N MET B 428 O TYR B 367
LINK FE HEM A 901 SG CYS A 194 1555 1555 2.39
LINK ZN ZN A 903 SG CYS A 109 1555 1555 2.24
LINK ZN ZN A 903 SG CYS A 104 1555 1555 2.22
LINK ZN ZN A 903 SG CYS A 109 1555 11655 2.23
LINK ZN ZN A 903 SG CYS A 104 1555 11655 2.23
LINK FE HEM B 901 SG CYS B 194 1555 1555 2.43
LINK ZN ZN B 903 SG CYS B 109 1555 9766 2.25
LINK ZN ZN B 903 SG CYS B 109 1555 1555 2.28
LINK ZN ZN B 903 SG CYS B 104 1555 9766 2.25
LINK ZN ZN B 903 SG CYS B 104 1555 1555 2.23
CISPEP 1 SER A 480 PRO A 481 0 -0.08
CISPEP 2 SER B 480 PRO B 481 0 0.89
SITE 1 AC1 2 CYS A 104 CYS A 109
SITE 1 AC2 3 ARG A 80 HIS A 91 HOH A2207
SITE 1 AC3 2 LYS A 82 ILE A 89
SITE 1 AC4 1 LEU A 177
SITE 1 AC5 3 LYS A 97 GLN A 143 ARG A 448
SITE 1 AC6 2 CYS B 104 CYS B 109
SITE 1 AC7 4 THR B 176 LEU B 177 HOH B2214 HOH B2215
SITE 1 AC8 5 LEU B 94 LYS B 97 GLN B 143 ARG B 448
SITE 2 AC8 5 HOH B2216
SITE 1 AC9 3 ARG B 80 LYS B 82 ILE B 89
SITE 1 BC1 3 ARG B 80 ILE B 89 HIS B 91
SITE 1 BC2 19 TRP A 188 ARG A 193 CYS A 194 SER A 236
SITE 2 BC2 19 PHE A 363 ASN A 364 GLY A 365 TRP A 366
SITE 3 BC2 19 GLU A 371 TRP A 457 TYR A 485 4AB A 902
SITE 4 BC2 19 HAR A 909 HOH A2198 HOH A2199 HOH A2200
SITE 5 BC2 19 HOH A2201 HOH A2202 HOH A2203
SITE 1 BC3 12 SER A 112 ARG A 375 TRP A 455 ILE A 456
SITE 2 BC3 12 TRP A 457 PHE A 470 HIS A 471 HEM A 901
SITE 3 BC3 12 HOH A2178 HOH A2203 HOH A2205 HOH A2206
SITE 1 BC4 11 GLN A 257 TYR A 341 PRO A 344 GLY A 365
SITE 2 BC4 11 TRP A 366 TYR A 367 GLU A 371 ASP A 376
SITE 3 BC4 11 HEM A 901 HOH A2208 HOH A2209
SITE 1 BC5 19 TRP B 188 ARG B 193 CYS B 194 SER B 236
SITE 2 BC5 19 PHE B 363 ASN B 364 GLY B 365 TRP B 366
SITE 3 BC5 19 GLU B 371 TRP B 457 TYR B 485 4AB B 902
SITE 4 BC5 19 HAR B 909 HOH B2205 HOH B2206 HOH B2207
SITE 5 BC5 19 HOH B2208 HOH B2209 HOH B2210
SITE 1 BC6 13 SER B 112 ARG B 375 TRP B 455 ILE B 456
SITE 2 BC6 13 TRP B 457 PHE B 470 HIS B 471 GLU B 473
SITE 3 BC6 13 HEM B 901 HOH B2183 HOH B2209 HOH B2211
SITE 4 BC6 13 HOH B2213
SITE 1 BC7 10 GLN B 257 TYR B 341 PRO B 344 GLY B 365
SITE 2 BC7 10 TRP B 366 TYR B 367 GLU B 371 ASP B 376
SITE 3 BC7 10 HEM B 901 HOH B2152
CRYST1 212.980 212.980 114.200 90.00 90.00 120.00 P 61 2 2 24
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 0.004695 0.002711 0.000000 0.00000
SCALE2 0.000000 0.005422 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008756 0.00000
MTRIX1 1 -0.863870 -0.503700 -0.003907 291.42731 1
MTRIX2 1 -0.503715 0.863838 0.007455 78.08660 1
MTRIX3 1 0.000380 0.008408 -0.999965 122.68790 1
MTRIX1 2 -0.866206 -0.499593 -0.009731 291.86951 1
MTRIX2 2 -0.499653 0.866210 0.005100 77.41970 1
MTRIX3 2 0.005881 0.009280 -0.999940 122.75170 1
MTRIX1 3 -0.862943 -0.505143 -0.012623 292.31000 1
MTRIX2 3 -0.505258 0.862926 0.008542 78.31740 1
MTRIX3 3 0.006578 0.013749 -0.999884 121.16290 1
(ATOM LINES ARE NOT SHOWN.)
END
