HEADER OXIDOREDUCTASE 18-AUG-08 3E7G
TITLE STRUCTURE OF HUMAN INOSOX WITH INHIBITOR AR-C95791
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, INDUCIBLE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 82-505;
COMPND 5 SYNONYM: INDUCIBLE NO SYNTHASE, INDUCIBLE NOS, INOS, NOS
COMPND 6 TYPE II, HEPATOCYTE NOS, HEP-NOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI
KEYWDS NITRIC OXIDE, NOS, HEME, TETRAHYDROBIOPTERIN,
KEYWDS 2 OXIDOREDUCTASE, ALTERNATIVE SPLICING, CALCIUM, CALMODULIN-
KEYWDS 3 BINDING, FAD, FMN, IRON, METAL-BINDING, NADP,
KEYWDS 4 PHOSPHOPROTEIN, POLYMORPHISM, ZINC
EXPDTA X-RAY DIFFRACTION
AUTHOR E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,B.R.CRANE,
AUTHOR 2 G.ANDERSSON,G.ANDREWS,P.J.HAMLEY,P.R.MALLINDER,D.J.NICHOLLS,
AUTHOR 3 S.A.ST-GALLAY,A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,
AUTHOR 4 S.CONNOLLY,D.J.STUEH,A.ABERG,A.V.WALLACE,J.A.TAINER,
AUTHOR 5 E.D.GETZOFF
REVDAT 2 20-JAN-09 3E7G 1 JRNL VERSN
REVDAT 1 07-OCT-08 3E7G 0
JRNL AUTH E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,
JRNL AUTH 2 B.R.CRANE,G.ANDERSSON,G.ANDREWS,P.J.HAMLEY,
JRNL AUTH 3 P.R.MALLINDER,D.J.NICHOLLS,S.A.ST-GALLAY,
JRNL AUTH 4 A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,
JRNL AUTH 5 S.CONNOLLY,D.J.STUEHR,A.ABERG,A.V.WALLACE,
JRNL AUTH 6 J.A.TAINER,E.D.GETZOFF
JRNL TITL ANCHORED PLASTICITY OPENS DOORS FOR SELECTIVE
JRNL TITL 2 INHIBITOR DESIGN IN NITRIC OXIDE SYNTHASE.
JRNL REF NAT.CHEM.BIOL. V. 4 700 2008
JRNL REFN ISSN 1552-4450
JRNL PMID 18849972
JRNL DOI 10.1038/NCHEMBIO.115
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 0.9
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 262227.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 125869
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) : 0.182
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6396
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 15110
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 818
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 318
REMARK 3 SOLVENT ATOMS : 504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.42000
REMARK 3 B22 (A**2) : 10.94000
REMARK 3 B33 (A**2) : -1.51000
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 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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.95
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 53.18
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 : PROTEIN_REP.TOP
REMARK 3 PARAMETER FILE 2 : TOPH19X.HEME
REMARK 3 PARAMETER FILE 3 : A1.TOP
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : PARAM19X.HEME
REMARK 3 TOPOLOGY FILE 3 : A1.PAR
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3E7G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 141544
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 51.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32700
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM SULFATE, HEPES, LITHIUM
REMARK 280 ACETATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 300K
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 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 45.10300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 95.57050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.33550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 95.57050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.10300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.33550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
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
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: 5340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 82
REMARK 465 GLU A 504
REMARK 465 LYS A 505
REMARK 465 PRO B 82
REMARK 465 GLU B 504
REMARK 465 LYS B 505
REMARK 465 PRO C 82
REMARK 465 PRO D 82
REMARK 465 GLU D 504
REMARK 465 LYS D 505
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 503 CG OD1 OD2
REMARK 470 ARG B 83 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 503 CG OD1 OD2
REMARK 470 ARG C 83 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 83 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 503 CG OD1 OD2
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 ALA A 157 150.60 -39.23
REMARK 500 SER A 251 -91.33 -112.54
REMARK 500 CYS A 367 64.05 -157.22
REMARK 500 ARG A 388 -132.32 -114.64
REMARK 500 CYS A 457 97.67 -169.77
REMARK 500 LEU A 485 -160.72 -102.10
REMARK 500 THR B 121 74.78 -117.79
REMARK 500 ALA B 157 151.92 -48.26
REMARK 500 SER B 251 -94.12 -104.76
REMARK 500 LYS B 335 -60.27 -123.10
REMARK 500 CYS B 367 63.58 -156.87
REMARK 500 ARG B 388 -137.35 -118.47
REMARK 500 ASN B 390 60.39 36.30
REMARK 500 THR B 403 11.43 -67.50
REMARK 500 ARG B 454 21.84 -145.20
REMARK 500 CYS B 457 96.93 -160.43
REMARK 500 LEU B 485 -163.40 -105.93
REMARK 500 HIS C 84 149.36 -171.42
REMARK 500 THR C 121 72.91 -115.85
REMARK 500 SER C 251 -94.53 -100.66
REMARK 500 TYR C 299 29.05 48.54
REMARK 500 LYS C 335 -50.38 -125.12
REMARK 500 CYS C 367 59.79 -156.05
REMARK 500 ARG C 388 -133.56 -122.35
REMARK 500 ASN C 390 63.70 32.48
REMARK 500 CYS C 457 91.63 -164.21
REMARK 500 LEU C 485 -166.32 -102.85
REMARK 500 ASP C 503 -147.39 -138.22
REMARK 500 GLU C 504 73.79 -110.47
REMARK 500 HIS D 84 136.87 164.05
REMARK 500 ALA D 104 165.40 -46.35
REMARK 500 THR D 121 74.13 -119.55
REMARK 500 ALA D 157 145.84 -35.34
REMARK 500 ASN D 236 47.76 37.70
REMARK 500 SER D 251 -90.58 -103.44
REMARK 500 CYS D 367 65.94 -154.53
REMARK 500 ARG D 388 -133.14 -121.23
REMARK 500 ASN D 390 63.94 37.09
REMARK 500 ARG D 454 15.10 -141.94
REMARK 500 CYS D 457 93.52 -172.08
REMARK 500 LEU D 485 -165.21 -103.44
REMARK 500 GLN D 502 32.10 -99.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR D 451 0.07 SIDE_CHAIN
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D7101 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH D7109 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH D7118 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A4124 DISTANCE = 5.29 ANGSTROMS
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 A3001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 110 SG
REMARK 620 2 CYS A 115 SG 105.4
REMARK 620 3 CYS B 110 SG 126.6 110.1
REMARK 620 4 CYS B 115 SG 97.1 106.0 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C3002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 110 SG
REMARK 620 2 CYS C 115 SG 108.1
REMARK 620 3 CYS D 110 SG 127.5 105.3
REMARK 620 4 CYS D 115 SG 107.3 102.7 103.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A3001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 901
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 902
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 A 906
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B1901
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B1902
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 B1906
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C3002
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C2901
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B C2902
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 C2906
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D3901
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B D3902
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT2 D3906
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E65 RELATED DB: PDB
REMARK 900 RELATED ID: 3E67 RELATED DB: PDB
REMARK 900 RELATED ID: 3E68 RELATED DB: PDB
REMARK 900 RELATED ID: 3E6L RELATED DB: PDB
REMARK 900 RELATED ID: 3E6N RELATED DB: PDB
REMARK 900 RELATED ID: 3E6O RELATED DB: PDB
REMARK 900 RELATED ID: 3E6T RELATED DB: PDB
DBREF 3E7G A 82 505 UNP P35228 NOS2A_HUMAN 82 505
DBREF 3E7G B 82 505 UNP P35228 NOS2A_HUMAN 82 505
DBREF 3E7G C 82 505 UNP P35228 NOS2A_HUMAN 82 505
DBREF 3E7G D 82 505 UNP P35228 NOS2A_HUMAN 82 505
SEQRES 1 A 424 PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET
SEQRES 2 A 424 THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE
SEQRES 3 A 424 LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET
SEQRES 4 A 424 THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO
SEQRES 5 A 424 THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE
SEQRES 6 A 424 VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE
SEQRES 7 A 424 GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU
SEQRES 8 A 424 ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU
SEQRES 9 A 424 LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 A 424 ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL
SEQRES 11 A 424 PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE
SEQRES 12 A 424 GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN
SEQRES 13 A 424 GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 A 424 SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN
SEQRES 15 A 424 LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER
SEQRES 16 A 424 ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU
SEQRES 17 A 424 CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE
SEQRES 18 A 424 ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP
SEQRES 19 A 424 PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU
SEQRES 20 A 424 VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU
SEQRES 21 A 424 LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN
SEQRES 22 A 424 MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS
SEQRES 23 A 424 PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 424 ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU
SEQRES 25 A 424 GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU
SEQRES 26 A 424 ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN
SEQRES 27 A 424 ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR
SEQRES 28 A 424 ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS
SEQRES 29 A 424 TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO
SEQRES 30 A 424 ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER
SEQRES 31 A 424 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL
SEQRES 32 A 424 LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS
SEQRES 33 A 424 THR HIS VAL TRP GLN ASP GLU LYS
SEQRES 1 B 424 PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET
SEQRES 2 B 424 THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE
SEQRES 3 B 424 LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET
SEQRES 4 B 424 THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO
SEQRES 5 B 424 THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE
SEQRES 6 B 424 VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE
SEQRES 7 B 424 GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU
SEQRES 8 B 424 ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU
SEQRES 9 B 424 LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 B 424 ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL
SEQRES 11 B 424 PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE
SEQRES 12 B 424 GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN
SEQRES 13 B 424 GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 B 424 SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN
SEQRES 15 B 424 LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER
SEQRES 16 B 424 ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU
SEQRES 17 B 424 CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE
SEQRES 18 B 424 ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP
SEQRES 19 B 424 PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU
SEQRES 20 B 424 VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU
SEQRES 21 B 424 LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN
SEQRES 22 B 424 MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS
SEQRES 23 B 424 PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 424 ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU
SEQRES 25 B 424 GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU
SEQRES 26 B 424 ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN
SEQRES 27 B 424 ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR
SEQRES 28 B 424 ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS
SEQRES 29 B 424 TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO
SEQRES 30 B 424 ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER
SEQRES 31 B 424 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL
SEQRES 32 B 424 LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS
SEQRES 33 B 424 THR HIS VAL TRP GLN ASP GLU LYS
SEQRES 1 C 424 PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET
SEQRES 2 C 424 THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE
SEQRES 3 C 424 LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET
SEQRES 4 C 424 THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO
SEQRES 5 C 424 THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE
SEQRES 6 C 424 VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE
SEQRES 7 C 424 GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU
SEQRES 8 C 424 ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU
SEQRES 9 C 424 LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 C 424 ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL
SEQRES 11 C 424 PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE
SEQRES 12 C 424 GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN
SEQRES 13 C 424 GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 C 424 SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN
SEQRES 15 C 424 LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER
SEQRES 16 C 424 ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU
SEQRES 17 C 424 CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE
SEQRES 18 C 424 ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP
SEQRES 19 C 424 PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU
SEQRES 20 C 424 VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU
SEQRES 21 C 424 LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN
SEQRES 22 C 424 MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS
SEQRES 23 C 424 PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 C 424 ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU
SEQRES 25 C 424 GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU
SEQRES 26 C 424 ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN
SEQRES 27 C 424 ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR
SEQRES 28 C 424 ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS
SEQRES 29 C 424 TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO
SEQRES 30 C 424 ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER
SEQRES 31 C 424 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL
SEQRES 32 C 424 LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS
SEQRES 33 C 424 THR HIS VAL TRP GLN ASP GLU LYS
SEQRES 1 D 424 PRO ARG HIS VAL ARG ILE LYS ASN TRP GLY SER GLY MET
SEQRES 2 D 424 THR PHE GLN ASP THR LEU HIS HIS LYS ALA LYS GLY ILE
SEQRES 3 D 424 LEU THR CYS ARG SER LYS SER CYS LEU GLY SER ILE MET
SEQRES 4 D 424 THR PRO LYS SER LEU THR ARG GLY PRO ARG ASP LYS PRO
SEQRES 5 D 424 THR PRO PRO ASP GLU LEU LEU PRO GLN ALA ILE GLU PHE
SEQRES 6 D 424 VAL ASN GLN TYR TYR GLY SER PHE LYS GLU ALA LYS ILE
SEQRES 7 D 424 GLU GLU HIS LEU ALA ARG VAL GLU ALA VAL THR LYS GLU
SEQRES 8 D 424 ILE GLU THR THR GLY THR TYR GLN LEU THR GLY ASP GLU
SEQRES 9 D 424 LEU ILE PHE ALA THR LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 D 424 ARG CYS ILE GLY ARG ILE GLN TRP SER ASN LEU GLN VAL
SEQRES 11 D 424 PHE ASP ALA ARG SER CYS SER THR ALA ARG GLU MET PHE
SEQRES 12 D 424 GLU HIS ILE CYS ARG HIS VAL ARG TYR SER THR ASN ASN
SEQRES 13 D 424 GLY ASN ILE ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 D 424 SER ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN ALA GLN
SEQRES 15 D 424 LEU ILE ARG TYR ALA GLY TYR GLN MET PRO ASP GLY SER
SEQRES 16 D 424 ILE ARG GLY ASP PRO ALA ASN VAL GLU PHE THR GLN LEU
SEQRES 17 D 424 CYS ILE ASP LEU GLY TRP LYS PRO LYS TYR GLY ARG PHE
SEQRES 18 D 424 ASP VAL VAL PRO LEU VAL LEU GLN ALA ASN GLY ARG ASP
SEQRES 19 D 424 PRO GLU LEU PHE GLU ILE PRO PRO ASP LEU VAL LEU GLU
SEQRES 20 D 424 VAL ALA MET GLU HIS PRO LYS TYR GLU TRP PHE ARG GLU
SEQRES 21 D 424 LEU GLU LEU LYS TRP TYR ALA LEU PRO ALA VAL ALA ASN
SEQRES 22 D 424 MET LEU LEU GLU VAL GLY GLY LEU GLU PHE PRO GLY CYS
SEQRES 23 D 424 PRO PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 D 424 ARG ASP PHE CYS ASP VAL GLN ARG TYR ASN ILE LEU GLU
SEQRES 25 D 424 GLU VAL GLY ARG ARG MET GLY LEU GLU THR HIS LYS LEU
SEQRES 26 D 424 ALA SER LEU TRP LYS ASP GLN ALA VAL VAL GLU ILE ASN
SEQRES 27 D 424 ILE ALA VAL LEU HIS SER PHE GLN LYS GLN ASN VAL THR
SEQRES 28 D 424 ILE MET ASP HIS HIS SER ALA ALA GLU SER PHE MET LYS
SEQRES 29 D 424 TYR MET GLN ASN GLU TYR ARG SER ARG GLY GLY CYS PRO
SEQRES 30 D 424 ALA ASP TRP ILE TRP LEU VAL PRO PRO MET SER GLY SER
SEQRES 31 D 424 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR VAL
SEQRES 32 D 424 LEU SER PRO PHE TYR TYR TYR GLN VAL GLU ALA TRP LYS
SEQRES 33 D 424 THR HIS VAL TRP GLN ASP GLU LYS
HET ZN A3001 1
HET HEM A 901 43
HET H4B A 902 17
HET AT2 A 906 19
HET HEM B1901 43
HET H4B B1902 17
HET AT2 B1906 19
HET ZN C3002 1
HET HEM C2901 43
HET H4B C2902 17
HET AT2 C2906 19
HET HEM D3901 43
HET H4B D3902 17
HET AT2 D3906 19
HETNAM ZN ZINC ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM AT2 ETHYL 4-[(4-METHYLPYRIDIN-2-YL)AMINO]PIPERIDINE-1-
HETNAM 2 AT2 CARBOXYLATE
HETSYN HEM HEME
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 HEM 4(C34 H32 FE N4 O4)
FORMUL 7 H4B 4(C9 H15 N5 O3)
FORMUL 8 AT2 4(C14 H21 N3 O2)
FORMUL 19 HOH *504(H2 O)
HELIX 1 1 THR A 99 ALA A 104 5 6
HELIX 2 2 PRO A 122 THR A 126 5 5
HELIX 3 3 PRO A 135 SER A 153 1 19
HELIX 4 4 LYS A 158 THR A 176 1 19
HELIX 5 5 THR A 182 ASN A 196 1 15
HELIX 6 6 GLY A 202 TRP A 206 5 5
HELIX 7 7 THR A 219 ASN A 236 1 18
HELIX 8 8 ASN A 237 ASN A 239 5 3
HELIX 9 9 ASN A 283 LEU A 293 1 11
HELIX 10 10 PRO A 322 VAL A 326 5 5
HELIX 11 11 TYR A 336 GLU A 343 5 8
HELIX 12 12 MET A 374 VAL A 380 1 7
HELIX 13 13 VAL A 380 ASP A 385 1 6
HELIX 14 14 ILE A 391 GLY A 400 1 10
HELIX 15 15 LYS A 405 SER A 408 5 4
HELIX 16 16 LEU A 409 GLN A 429 1 21
HELIX 17 17 ASP A 435 GLY A 455 1 21
HELIX 18 18 ASP A 460 VAL A 465 1 6
HELIX 19 19 SER A 469 GLN A 478 5 10
HELIX 20 20 GLU A 494 HIS A 499 1 6
HELIX 21 21 THR B 99 ALA B 104 5 6
HELIX 22 22 PRO B 122 THR B 126 5 5
HELIX 23 23 PRO B 135 SER B 153 1 19
HELIX 24 24 LYS B 158 GLY B 177 1 20
HELIX 25 25 THR B 182 ASN B 196 1 15
HELIX 26 26 GLY B 202 TRP B 206 5 5
HELIX 27 27 THR B 219 ASN B 236 1 18
HELIX 28 28 ASN B 237 ASN B 239 5 3
HELIX 29 29 ASN B 283 LEU B 293 1 11
HELIX 30 30 PRO B 322 VAL B 326 5 5
HELIX 31 31 TYR B 336 GLU B 343 5 8
HELIX 32 32 MET B 374 VAL B 380 1 7
HELIX 33 33 VAL B 380 ASP B 385 1 6
HELIX 34 34 ILE B 391 MET B 399 1 9
HELIX 35 35 LYS B 405 SER B 408 5 4
HELIX 36 36 LEU B 409 GLN B 429 1 21
HELIX 37 37 ASP B 435 GLY B 455 1 21
HELIX 38 38 ASP B 460 VAL B 465 1 6
HELIX 39 39 SER B 469 GLN B 478 5 10
HELIX 40 40 GLU B 494 HIS B 499 1 6
HELIX 41 41 THR C 99 ALA C 104 5 6
HELIX 42 42 PRO C 122 THR C 126 5 5
HELIX 43 43 PRO C 135 GLY C 152 1 18
HELIX 44 44 LYS C 158 GLY C 177 1 20
HELIX 45 45 THR C 182 ASN C 196 1 15
HELIX 46 46 GLY C 202 TRP C 206 5 5
HELIX 47 47 THR C 219 ASN C 236 1 18
HELIX 48 48 ASN C 237 ASN C 239 5 3
HELIX 49 49 ASN C 283 LEU C 293 1 11
HELIX 50 50 PRO C 322 VAL C 326 5 5
HELIX 51 51 TYR C 336 GLU C 343 5 8
HELIX 52 52 MET C 374 VAL C 380 1 7
HELIX 53 53 VAL C 380 ASP C 385 1 6
HELIX 54 54 ILE C 391 MET C 399 1 9
HELIX 55 55 LYS C 405 SER C 408 5 4
HELIX 56 56 LEU C 409 GLN C 429 1 21
HELIX 57 57 ASP C 435 GLY C 455 1 21
HELIX 58 58 ASP C 460 VAL C 465 1 6
HELIX 59 59 SER C 469 GLN C 478 5 10
HELIX 60 60 GLU C 494 THR C 498 5 5
HELIX 61 61 THR D 99 LYS D 103 5 5
HELIX 62 62 PRO D 122 THR D 126 5 5
HELIX 63 63 PRO D 135 GLY D 152 1 18
HELIX 64 64 LYS D 158 GLY D 177 1 20
HELIX 65 65 THR D 182 ASN D 196 1 15
HELIX 66 66 GLY D 202 TRP D 206 5 5
HELIX 67 67 THR D 219 ASN D 236 1 18
HELIX 68 68 ASN D 237 ASN D 239 5 3
HELIX 69 69 ASN D 283 LEU D 293 1 11
HELIX 70 70 PRO D 322 VAL D 326 5 5
HELIX 71 71 TYR D 336 GLU D 343 5 8
HELIX 72 72 MET D 374 VAL D 380 1 7
HELIX 73 73 VAL D 380 ASP D 385 1 6
HELIX 74 74 ILE D 391 MET D 399 1 9
HELIX 75 75 LYS D 405 SER D 408 5 4
HELIX 76 76 LEU D 409 GLN D 429 1 21
HELIX 77 77 ASP D 435 GLY D 455 1 21
HELIX 78 78 ASP D 460 VAL D 465 1 6
HELIX 79 79 SER D 469 GLN D 478 5 10
HELIX 80 80 GLU D 494 THR D 498 5 5
SHEET 1 A 2 VAL A 85 LYS A 88 0
SHEET 2 A 2 THR A 95 ASP A 98 -1 O PHE A 96 N ILE A 87
SHEET 1 B 4 GLN A 210 ASP A 213 0
SHEET 2 B 4 ALA A 243 VAL A 246 1 O ILE A 244 N PHE A 212
SHEET 3 B 4 PHE A 369 ASN A 370 -1 O ASN A 370 N ALA A 243
SHEET 4 B 4 ALA A 351 VAL A 352 -1 N VAL A 352 O PHE A 369
SHEET 1 C 3 ARG A 258 VAL A 259 0
SHEET 2 C 3 LEU A 307 GLN A 310 -1 O GLN A 310 N ARG A 258
SHEET 3 C 3 GLU A 317 PHE A 319 -1 O PHE A 319 N LEU A 307
SHEET 1 D 2 GLY A 269 GLN A 271 0
SHEET 2 D 2 ILE A 277 GLY A 279 -1 O ARG A 278 N TYR A 270
SHEET 1 E 2 GLU A 328 ALA A 330 0
SHEET 2 E 2 LYS A 345 TYR A 347 -1 O TRP A 346 N VAL A 329
SHEET 1 F 3 LEU A 362 PHE A 364 0
SHEET 2 F 3 LEU A 356 VAL A 359 -1 N LEU A 357 O PHE A 364
SHEET 3 F 3 PHE A 488 TYR A 490 -1 O TYR A 490 N LEU A 356
SHEET 1 G 2 VAL B 85 LYS B 88 0
SHEET 2 G 2 THR B 95 ASP B 98 -1 O PHE B 96 N ILE B 87
SHEET 1 H 4 GLN B 210 ASP B 213 0
SHEET 2 H 4 ALA B 243 VAL B 246 1 O ILE B 244 N PHE B 212
SHEET 3 H 4 PHE B 369 ASN B 370 -1 O ASN B 370 N ALA B 243
SHEET 4 H 4 ALA B 351 VAL B 352 -1 N VAL B 352 O PHE B 369
SHEET 1 I 3 ARG B 258 VAL B 259 0
SHEET 2 I 3 LEU B 307 GLN B 310 -1 O GLN B 310 N ARG B 258
SHEET 3 I 3 GLU B 317 PHE B 319 -1 O PHE B 319 N LEU B 307
SHEET 1 J 2 GLY B 269 GLN B 271 0
SHEET 2 J 2 ILE B 277 GLY B 279 -1 O ARG B 278 N TYR B 270
SHEET 1 K 2 GLU B 328 ALA B 330 0
SHEET 2 K 2 LYS B 345 TYR B 347 -1 O TRP B 346 N VAL B 329
SHEET 1 L 3 LEU B 362 PHE B 364 0
SHEET 2 L 3 LEU B 356 VAL B 359 -1 N VAL B 359 O LEU B 362
SHEET 3 L 3 PHE B 488 TYR B 490 -1 O TYR B 490 N LEU B 356
SHEET 1 M 2 VAL C 85 LYS C 88 0
SHEET 2 M 2 THR C 95 ASP C 98 -1 O ASP C 98 N VAL C 85
SHEET 1 N 4 GLN C 210 ASP C 213 0
SHEET 2 N 4 ALA C 243 VAL C 246 1 O ILE C 244 N PHE C 212
SHEET 3 N 4 PHE C 369 ASN C 370 -1 O ASN C 370 N ALA C 243
SHEET 4 N 4 ALA C 351 VAL C 352 -1 N VAL C 352 O PHE C 369
SHEET 1 O 3 ARG C 258 VAL C 259 0
SHEET 2 O 3 LEU C 307 GLN C 310 -1 O GLN C 310 N ARG C 258
SHEET 3 O 3 GLU C 317 PHE C 319 -1 O PHE C 319 N LEU C 307
SHEET 1 P 2 GLY C 269 GLN C 271 0
SHEET 2 P 2 ILE C 277 GLY C 279 -1 O ARG C 278 N TYR C 270
SHEET 1 Q 2 GLU C 328 ALA C 330 0
SHEET 2 Q 2 LYS C 345 TYR C 347 -1 O TRP C 346 N VAL C 329
SHEET 1 R 3 LEU C 362 PHE C 364 0
SHEET 2 R 3 LEU C 356 VAL C 359 -1 N LEU C 357 O PHE C 364
SHEET 3 R 3 PHE C 488 TYR C 490 -1 O TYR C 490 N LEU C 356
SHEET 1 S 2 VAL D 85 LYS D 88 0
SHEET 2 S 2 THR D 95 ASP D 98 -1 O ASP D 98 N VAL D 85
SHEET 1 T 4 GLN D 210 ASP D 213 0
SHEET 2 T 4 ALA D 243 VAL D 246 1 O ILE D 244 N PHE D 212
SHEET 3 T 4 PHE D 369 ASN D 370 -1 O ASN D 370 N ALA D 243
SHEET 4 T 4 ALA D 351 VAL D 352 -1 N VAL D 352 O PHE D 369
SHEET 1 U 3 ARG D 258 VAL D 259 0
SHEET 2 U 3 LEU D 307 GLN D 310 -1 O GLN D 310 N ARG D 258
SHEET 3 U 3 GLU D 317 PHE D 319 -1 O PHE D 319 N LEU D 307
SHEET 1 V 2 GLY D 269 GLN D 271 0
SHEET 2 V 2 ILE D 277 GLY D 279 -1 O ARG D 278 N TYR D 270
SHEET 1 W 2 GLU D 328 ALA D 330 0
SHEET 2 W 2 LYS D 345 TYR D 347 -1 O TRP D 346 N VAL D 329
SHEET 1 X 3 LEU D 362 PHE D 364 0
SHEET 2 X 3 LEU D 356 VAL D 359 -1 N LEU D 357 O PHE D 364
SHEET 3 X 3 PHE D 488 TYR D 490 -1 O TYR D 490 N LEU D 356
LINK SG CYS A 110 ZN ZN A3001 1555 1555 2.76
LINK SG CYS A 115 ZN ZN A3001 1555 1555 2.69
LINK SG CYS A 200 FE HEM A 901 1555 1555 2.58
LINK SG CYS B 110 ZN ZN A3001 1555 1555 2.65
LINK SG CYS B 115 ZN ZN A3001 1555 1555 2.70
LINK SG CYS B 200 FE HEM B1901 1555 1555 2.52
LINK SG CYS C 110 ZN ZN C3002 1555 1555 2.80
LINK SG CYS C 115 ZN ZN C3002 1555 1555 2.63
LINK SG CYS C 200 FE HEM C2901 1555 1555 2.53
LINK SG CYS D 110 ZN ZN C3002 1555 1555 2.73
LINK SG CYS D 115 ZN ZN C3002 1555 1555 2.66
LINK SG CYS D 200 FE HEM D3901 1555 1555 2.58
CISPEP 1 SER A 486 PRO A 487 0 0.12
CISPEP 2 SER B 486 PRO B 487 0 0.02
CISPEP 3 SER C 486 PRO C 487 0 -0.14
CISPEP 4 SER D 486 PRO D 487 0 0.08
SITE 1 AC1 4 CYS A 110 CYS A 115 CYS B 110 CYS B 115
SITE 1 AC2 18 TRP A 194 ARG A 199 CYS A 200 SER A 242
SITE 2 AC2 18 PHE A 369 ASN A 370 TRP A 372 GLU A 377
SITE 3 AC2 18 TRP A 463 TYR A 489 TYR A 491 H4B A 902
SITE 4 AC2 18 AT2 A 906 HOH A4015 HOH A4023 HOH A4048
SITE 5 AC2 18 HOH A4116 HOH A4121
SITE 1 AC3 10 SER A 118 MET A 120 ARG A 381 ILE A 462
SITE 2 AC3 10 TRP A 463 HEM A 901 HOH A4072 HOH A4123
SITE 3 AC3 10 PHE B 476 HIS B 477
SITE 1 AC4 12 GLN A 263 ARG A 266 TYR A 347 PRO A 350
SITE 2 AC4 12 PHE A 369 GLY A 371 TRP A 372 TYR A 373
SITE 3 AC4 12 GLU A 377 ASP A 382 ARG A 388 HEM A 901
SITE 1 AC5 19 TRP B 194 ARG B 199 CYS B 200 SER B 242
SITE 2 AC5 19 PHE B 369 ASN B 370 TRP B 372 GLU B 377
SITE 3 AC5 19 TRP B 463 TYR B 489 TYR B 491 H4B B1902
SITE 4 AC5 19 AT2 B1906 HOH B5026 HOH B5051 HOH B5061
SITE 5 AC5 19 HOH B5075 HOH B5093 HOH B5110
SITE 1 AC6 10 PHE A 476 HIS A 477 GLN A 478 SER B 118
SITE 2 AC6 10 MET B 120 ARG B 381 ILE B 462 TRP B 463
SITE 3 AC6 10 HEM B1901 HOH B5093
SITE 1 AC7 11 GLN B 263 ARG B 266 TYR B 347 PRO B 350
SITE 2 AC7 11 GLY B 371 TRP B 372 TYR B 373 GLU B 377
SITE 3 AC7 11 ASP B 382 ARG B 388 HEM B1901
SITE 1 AC8 4 CYS C 110 CYS C 115 CYS D 110 CYS D 115
SITE 1 AC9 19 TRP C 194 ARG C 199 CYS C 200 SER C 242
SITE 2 AC9 19 PHE C 369 ASN C 370 TRP C 372 GLU C 377
SITE 3 AC9 19 TRP C 463 TYR C 489 TYR C 491 H4B C2902
SITE 4 AC9 19 AT2 C2906 HOH C6014 HOH C6047 HOH C6050
SITE 5 AC9 19 HOH C6079 HOH C6080 HOH C6131
SITE 1 BC1 11 SER C 118 MET C 120 ARG C 381 ILE C 462
SITE 2 BC1 11 TRP C 463 HEM C2901 HOH C6033 HOH C6087
SITE 3 BC1 11 HOH C6131 PHE D 476 GLN D 478
SITE 1 BC2 11 GLN C 263 ARG C 266 TYR C 347 PHE C 369
SITE 2 BC2 11 GLY C 371 TRP C 372 TYR C 373 GLU C 377
SITE 3 BC2 11 ASP C 382 ARG C 388 HEM C2901
SITE 1 BC3 18 TRP D 194 ARG D 199 CYS D 200 SER D 242
SITE 2 BC3 18 PHE D 369 ASN D 370 TRP D 372 GLU D 377
SITE 3 BC3 18 TRP D 463 TYR D 489 TYR D 491 H4B D3902
SITE 4 BC3 18 AT2 D3906 HOH D7024 HOH D7044 HOH D7048
SITE 5 BC3 18 HOH D7088 HOH D7091
SITE 1 BC4 12 PHE C 476 HIS C 477 GLU C 479 SER D 118
SITE 2 BC4 12 MET D 120 ARG D 381 ILE D 462 TRP D 463
SITE 3 BC4 12 HEM D3901 HOH D7035 HOH D7092 HOH D7106
SITE 1 BC5 11 GLN D 263 ARG D 266 TYR D 347 PRO D 350
SITE 2 BC5 11 GLY D 371 TRP D 372 TYR D 373 GLU D 377
SITE 3 BC5 11 ASP D 382 ARG D 388 HEM D3901
CRYST1 90.206 158.671 191.141 90.00 90.00 90.00 P 21 21 21 16
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 0.011086 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005232 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
