HEADER OXIDOREDUCTASE 25-AUG-08 3EAH
TITLE STRUCTURE OF INHIBITED HUMAN ENOS OXYGENASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, ENDOTHELIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NOS TYPE III, ENDOTHELIAL NOS, CNOS, ENOS, NOSIII, EC-NOS,
COMPND 5 CONSTITUTIVE NOS;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: NOS3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE, NOS, HEME, TETRAHYDROBIOPTERIN, OXIDOREDUCTASE
KEYWDS 2 CALMODULIN-BINDING, FAD, FMN, IRON, METAL-BINDING, NADP,
KEYWDS 3 OXIDOREDUCTASE, POLYMORPHISM, ZINC
EXPDTA X-RAY DIFFRACTION
AUTHOR E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,B.R.CRANE,G.ANDERSSON,
AUTHOR 2 G.ANDREWS,P.J.HAMLEY,P.R.MALLINDER,D.J.NICHOLLS,S.A.ST-GALLAY,
AUTHOR 3 A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,S.CONNOLLY,D.J.STUEHR,
AUTHOR 4 A.ABERG,A.V.WALLACE,J.A.TAINER,E.D.GETZOFF
REVDAT 5 21-FEB-24 3EAH 1 REMARK LINK
REVDAT 4 09-JUN-09 3EAH 1 REVDAT
REVDAT 3 24-FEB-09 3EAH 1 VERSN
REVDAT 2 13-JAN-09 3EAH 1 JRNL
REVDAT 1 07-OCT-08 3EAH 0
JRNL AUTH E.D.GARCIN,A.S.ARVAI,R.J.ROSENFELD,M.D.KROEGER,B.R.CRANE,
JRNL AUTH 2 G.ANDERSSON,G.ANDREWS,P.J.HAMLEY,P.R.MALLINDER,D.J.NICHOLLS,
JRNL AUTH 3 S.A.ST-GALLAY,A.C.TINKER,N.P.GENSMANTEL,A.METE,D.R.CHESHIRE,
JRNL AUTH 4 S.CONNOLLY,D.J.STUEHR,A.ABERG,A.V.WALLACE,J.A.TAINER,
JRNL AUTH 5 E.D.GETZOFF
JRNL TITL ANCHORED PLASTICITY OPENS DOORS FOR SELECTIVE INHIBITOR
JRNL TITL 2 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 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1984817.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 36303
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) : 0.213
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1803
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5706
REMARK 3 BIN R VALUE (WORKING SET) : 0.3130
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 292
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6328
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 143
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.41000
REMARK 3 B22 (A**2) : 1.74000
REMARK 3 B33 (A**2) : -11.15000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.37
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) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.870
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) : 1.050 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.760 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.650 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.480 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 30.55
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.PARAM
REMARK 3 PARAMETER FILE 2 : PARA.INP
REMARK 3 PARAMETER FILE 3 : A15.PARA
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : TOPO.INP
REMARK 3 TOPOLOGY FILE 3 : A15.TOPO
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EAH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049079.
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 : 6.0
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.080
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 : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 35.54500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.05000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.05000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.54500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.07500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 9730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -197.0 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 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 35
REMARK 465 LYS A 36
REMARK 465 PRO A 74A
REMARK 465 ARG A 74B
REMARK 465 LYS A 74C
REMARK 465 LEU A 74D
REMARK 465 GLN A 74E
REMARK 465 GLY A 74F
REMARK 465 ARG A 74G
REMARK 465 PRO A 74H
REMARK 465 SER A 74I
REMARK 465 PRO A 74J
REMARK 465 GLY A 74K
REMARK 465 PRO A 74L
REMARK 465 PRO A 74M
REMARK 465 ALA A 74N
REMARK 465 LYS A 447
REMARK 465 GLY A 448
REMARK 465 SER A 449
REMARK 465 ALA A 450
REMARK 465 ALA A 451
REMARK 465 LYS A 452
REMARK 465 GLY A 453
REMARK 465 THR A 454
REMARK 465 GLY A 455
REMARK 465 ILE A 456
REMARK 465 THR A 457
REMARK 465 ARG A 458
REMARK 465 PRO B 35
REMARK 465 ARG B 75A
REMARK 465 LYS B 75B
REMARK 465 LEU B 75C
REMARK 465 GLN B 75D
REMARK 465 GLY B 75E
REMARK 465 ARG B 75F
REMARK 465 PRO B 75G
REMARK 465 SER B 75H
REMARK 465 PRO B 75I
REMARK 465 GLY B 75J
REMARK 465 PRO B 75K
REMARK 465 PRO B 75L
REMARK 465 ALA B 75M
REMARK 465 LYS B 447
REMARK 465 GLY B 448
REMARK 465 SER B 449
REMARK 465 ALA B 450
REMARK 465 ALA B 451
REMARK 465 LYS B 452
REMARK 465 GLY B 453
REMARK 465 THR B 454
REMARK 465 GLY B 455
REMARK 465 ILE B 456
REMARK 465 THR B 457
REMARK 465 ARG B 458
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 GLN A 58 CG CD OE1 NE2
REMARK 470 GLN A 59 CG CD OE1 NE2
REMARK 470 ARG A 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 GLN A 88 CG CD OE1 NE2
REMARK 470 GLN A 110 CG CD OE1 NE2
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 GLN B 56 CG CD OE1 NE2
REMARK 470 GLN B 58 CG CD OE1 NE2
REMARK 470 GLN B 59 CG CD OE1 NE2
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 GLN B 88 CG CD OE1 NE2
REMARK 470 ARG B 354 CG CD NE CZ NH1 NH2
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 DISTANCE
REMARK 500 OH TYR A 441 O2D HEC A 861 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 113 O HOH A 1906 3545 1.89
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 51 95.24 -69.04
REMARK 500 ARG A 106 23.39 -146.56
REMARK 500 ASN A 186 53.58 39.94
REMARK 500 ARG A 187 8.76 56.67
REMARK 500 ARG A 204 137.18 -176.51
REMARK 500 ASP A 224 13.15 146.69
REMARK 500 ASN A 249 22.47 -149.25
REMARK 500 THR A 285 -32.60 -131.97
REMARK 500 ALA A 317 73.18 -152.47
REMARK 500 SER A 325 -38.12 -39.94
REMARK 500 ARG A 338 -130.88 -119.68
REMARK 500 ILE A 383 148.45 -173.40
REMARK 500 CYS A 407 114.40 -169.64
REMARK 500 PRO A 417 -5.19 -59.89
REMARK 500 ARG B 187 16.11 58.78
REMARK 500 ARG B 204 138.23 171.43
REMARK 500 ASP B 224 6.00 152.01
REMARK 500 SER B 226 172.46 -59.40
REMARK 500 HIS B 243 38.51 -99.00
REMARK 500 ASN B 249 17.01 -148.77
REMARK 500 ALA B 317 69.03 -168.46
REMARK 500 ARG B 338 -141.23 -122.96
REMARK 500 ASN B 340 68.23 25.83
REMARK 500 SER B 357 -7.51 -59.39
REMARK 500 SER B 421 4.14 -66.94
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 ZN A 862 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 63 SG
REMARK 620 2 CYS A 68 SG 105.1
REMARK 620 3 CYS B 63 SG 123.7 103.8
REMARK 620 4 CYS B 68 SG 107.2 107.3 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 861 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 150 SG
REMARK 620 2 HEC A 861 NA 95.5
REMARK 620 3 HEC A 861 NB 85.7 89.9
REMARK 620 4 HEC A 861 NC 90.8 173.7 90.1
REMARK 620 5 HEC A 861 ND 98.4 94.6 173.5 84.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B1861 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 150 SG
REMARK 620 2 HEC B1861 NA 95.5
REMARK 620 3 HEC B1861 NB 92.5 91.8
REMARK 620 4 HEC B1861 NC 89.6 174.9 88.7
REMARK 620 5 HEC B1861 ND 90.2 94.2 173.2 85.1
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 HEC A 861
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 862
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 327 A 864
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 866
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1865
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1866
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A1867
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 865
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 867
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 327 B1864
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
REMARK 900 RELATED ID: 3E7G RELATED DB: PDB
REMARK 900 RELATED ID: 3E7I RELATED DB: PDB
REMARK 900 RELATED ID: 3E7M RELATED DB: PDB
REMARK 900 RELATED ID: 3E7S RELATED DB: PDB
REMARK 900 RELATED ID: 3E7T RELATED DB: PDB
REMARK 900 RELATED ID: 3EAI RELATED DB: PDB
REMARK 900 RELATED ID: 3EBD RELATED DB: PDB
REMARK 900 RELATED ID: 3EBF RELATED DB: PDB
REMARK 900 RELATED ID: 3EJ8 RELATED DB: PDB
DBREF 3EAH A 35 458 UNP P29474 NOS3_HUMAN 66 492
DBREF 3EAH B 35 458 UNP P29474 NOS3_HUMAN 66 492
SEQRES 1 A 427 PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER
SEQRES 2 A 427 ILE THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP
SEQRES 3 A 427 GLY PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL
SEQRES 4 A 427 PHE PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO
SEQRES 5 A 427 PRO ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE
SEQRES 6 A 427 ILE ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER
SEQRES 7 A 427 GLN ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU
SEQRES 8 A 427 VAL ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU
SEQRES 9 A 427 LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 A 427 ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL
SEQRES 11 A 427 PHE ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE
SEQRES 12 A 427 THR TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG
SEQRES 13 A 427 GLY ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 A 427 CYS PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN
SEQRES 15 A 427 LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER
SEQRES 16 A 427 VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU
SEQRES 17 A 427 CYS ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE
SEQRES 18 A 427 ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO
SEQRES 19 A 427 PRO GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 427 VAL PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA
SEQRES 21 A 427 LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN
SEQRES 22 A 427 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA
SEQRES 23 A 427 PRO PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR
SEQRES 24 A 427 ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU
SEQRES 25 A 427 ASP VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR
SEQRES 26 A 427 SER SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN
SEQRES 27 A 427 VAL ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR
SEQRES 28 A 427 ILE VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS
SEQRES 29 A 427 HIS LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO
SEQRES 30 A 427 ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER
SEQRES 31 A 427 LEU THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE
SEQRES 32 A 427 LEU SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP LYS
SEQRES 33 A 427 GLY SER ALA ALA LYS GLY THR GLY ILE THR ARG
SEQRES 1 B 427 PRO LYS PHE PRO ARG VAL LYS ASN TRP GLU VAL GLY SER
SEQRES 2 B 427 ILE THR TYR ASP THR LEU SER ALA GLN ALA GLN GLN ASP
SEQRES 3 B 427 GLY PRO CYS THR PRO ARG ARG CYS LEU GLY SER LEU VAL
SEQRES 4 B 427 PHE PRO ARG LYS LEU GLN GLY ARG PRO SER PRO GLY PRO
SEQRES 5 B 427 PRO ALA PRO GLU GLN LEU LEU SER GLN ALA ARG ASP PHE
SEQRES 6 B 427 ILE ASN GLN TYR TYR SER SER ILE LYS ARG SER GLY SER
SEQRES 7 B 427 GLN ALA HIS GLU GLN ARG LEU GLN GLU VAL GLU ALA GLU
SEQRES 8 B 427 VAL ALA ALA THR GLY THR TYR GLN LEU ARG GLU SER GLU
SEQRES 9 B 427 LEU VAL PHE GLY ALA LYS GLN ALA TRP ARG ASN ALA PRO
SEQRES 10 B 427 ARG CYS VAL GLY ARG ILE GLN TRP GLY LYS LEU GLN VAL
SEQRES 11 B 427 PHE ASP ALA ARG ASP CYS ARG SER ALA GLN GLU MET PHE
SEQRES 12 B 427 THR TYR ILE CYS ASN HIS ILE LYS TYR ALA THR ASN ARG
SEQRES 13 B 427 GLY ASN LEU ARG SER ALA ILE THR VAL PHE PRO GLN ARG
SEQRES 14 B 427 CYS PRO GLY ARG GLY ASP PHE ARG ILE TRP ASN SER GLN
SEQRES 15 B 427 LEU VAL ARG TYR ALA GLY TYR ARG GLN GLN ASP GLY SER
SEQRES 16 B 427 VAL ARG GLY ASP PRO ALA ASN VAL GLU ILE THR GLU LEU
SEQRES 17 B 427 CYS ILE GLN HIS GLY TRP THR PRO GLY ASN GLY ARG PHE
SEQRES 18 B 427 ASP VAL LEU PRO LEU LEU LEU GLN ALA PRO ASP GLU PRO
SEQRES 19 B 427 PRO GLU LEU PHE LEU LEU PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 427 VAL PRO LEU GLU HIS PRO THR LEU GLU TRP PHE ALA ALA
SEQRES 21 B 427 LEU GLY LEU ARG TRP TYR ALA LEU PRO ALA VAL SER ASN
SEQRES 22 B 427 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE PRO ALA ALA
SEQRES 23 B 427 PRO PHE SER GLY TRP TYR MET SER THR GLU ILE GLY THR
SEQRES 24 B 427 ARG ASN LEU CYS ASP PRO HIS ARG TYR ASN ILE LEU GLU
SEQRES 25 B 427 ASP VAL ALA VAL CYS MET ASP LEU ASP THR ARG THR THR
SEQRES 26 B 427 SER SER LEU TRP LYS ASP LYS ALA ALA VAL GLU ILE ASN
SEQRES 27 B 427 VAL ALA VAL LEU HIS SER TYR GLN LEU ALA LYS VAL THR
SEQRES 28 B 427 ILE VAL ASP HIS HIS ALA ALA THR ALA SER PHE MET LYS
SEQRES 29 B 427 HIS LEU GLU ASN GLU GLN LYS ALA ARG GLY GLY CYS PRO
SEQRES 30 B 427 ALA ASP TRP ALA TRP ILE VAL PRO PRO ILE SER GLY SER
SEQRES 31 B 427 LEU THR PRO VAL PHE HIS GLN GLU MET VAL ASN TYR PHE
SEQRES 32 B 427 LEU SER PRO ALA PHE ARG TYR GLN PRO ASP PRO TRP LYS
SEQRES 33 B 427 GLY SER ALA ALA LYS GLY THR GLY ILE THR ARG
HET HEC A 861 43
HET ZN A 862 1
HET 327 A 864 14
HET MPD A 866 8
HET CL A1865 1
HET MPD A1866 8
HET MPD A1867 8
HET CL B 865 1
HET MPD B 867 8
HET HEC B1861 43
HET 327 B1864 14
HETNAM HEC HEME C
HETNAM ZN ZINC ION
HETNAM 327 (3S,5E)-3-PROPYL-3,4-DIHYDROTHIENO[2,3-F][1,4]OXAZEPIN-
HETNAM 2 327 5(2H)-IMINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM CL CHLORIDE ION
FORMUL 3 HEC 2(C34 H34 FE N4 O4)
FORMUL 4 ZN ZN 2+
FORMUL 5 327 2(C10 H14 N2 O S)
FORMUL 6 MPD 4(C6 H14 O2)
FORMUL 7 CL 2(CL 1-)
FORMUL 14 HOH *143(H2 O)
HELIX 1 1 LEU A 53 ALA A 57 5 5
HELIX 2 2 PRO A 86 ILE A 104 1 19
HELIX 3 3 SER A 109 GLY A 127 1 19
HELIX 4 4 ARG A 132 ALA A 147 1 16
HELIX 5 5 GLY A 152 TRP A 156 5 5
HELIX 6 6 SER A 169 ASN A 186 1 18
HELIX 7 7 ARG A 187 ASN A 189 5 3
HELIX 8 8 ASN A 233 HIS A 243 1 11
HELIX 9 9 PRO A 272 VAL A 276 5 5
HELIX 10 10 LEU A 286 GLY A 293 5 8
HELIX 11 11 SER A 325 THR A 330 1 6
HELIX 12 12 THR A 330 ASP A 335 1 6
HELIX 13 13 ILE A 341 MET A 349 1 9
HELIX 14 14 THR A 355 SER A 358 5 4
HELIX 15 15 LEU A 359 ALA A 379 1 21
HELIX 16 16 ASP A 385 GLY A 405 1 21
HELIX 17 17 ASP A 410 VAL A 415 1 6
HELIX 18 18 SER A 419 GLN A 428 5 10
HELIX 19 19 LEU B 53 ALA B 57 5 5
HELIX 20 20 PRO B 86 ILE B 104 1 19
HELIX 21 21 SER B 109 GLY B 127 1 19
HELIX 22 22 ARG B 132 ALA B 147 1 16
HELIX 23 23 GLY B 152 LEU B 159 5 8
HELIX 24 24 SER B 169 ASN B 186 1 18
HELIX 25 25 ARG B 187 ASN B 189 5 3
HELIX 26 26 ASN B 233 HIS B 243 1 11
HELIX 27 27 PRO B 272 VAL B 276 5 5
HELIX 28 28 PHE B 289 GLY B 293 5 5
HELIX 29 29 SER B 325 THR B 330 1 6
HELIX 30 30 THR B 330 ASP B 335 1 6
HELIX 31 31 ILE B 341 MET B 349 1 9
HELIX 32 32 THR B 355 SER B 358 5 4
HELIX 33 33 LEU B 359 ALA B 379 1 21
HELIX 34 34 ASP B 385 GLY B 405 1 21
HELIX 35 35 ASP B 410 VAL B 415 1 6
HELIX 36 36 SER B 419 GLN B 428 5 10
SHEET 1 A 2 ARG A 39 LYS A 41 0
SHEET 2 A 2 ILE A 48 TYR A 50 -1 O THR A 49 N VAL A 40
SHEET 1 B 4 GLN A 160 ASP A 163 0
SHEET 2 B 4 ALA A 193 VAL A 196 1 O ILE A 194 N PHE A 162
SHEET 3 B 4 PHE A 319 SER A 320 -1 O SER A 320 N ALA A 193
SHEET 4 B 4 ALA A 301 VAL A 302 -1 N VAL A 302 O PHE A 319
SHEET 1 C 3 ARG A 208 ILE A 209 0
SHEET 2 C 3 LEU A 257 GLN A 260 -1 O GLN A 260 N ARG A 208
SHEET 3 C 3 GLU A 267 PHE A 269 -1 O PHE A 269 N LEU A 257
SHEET 1 D 2 GLY A 219 ARG A 221 0
SHEET 2 D 2 VAL A 227 GLY A 229 -1 O ARG A 228 N TYR A 220
SHEET 1 E 2 GLU A 278 PRO A 280 0
SHEET 2 E 2 ARG A 295 TYR A 297 -1 O TRP A 296 N VAL A 279
SHEET 1 F 3 LEU A 312 PHE A 314 0
SHEET 2 F 3 LEU A 306 ILE A 309 -1 N ILE A 309 O LEU A 312
SHEET 3 F 3 ALA A 438 ARG A 440 -1 O ARG A 440 N LEU A 306
SHEET 1 G 2 ARG B 39 LYS B 41 0
SHEET 2 G 2 ILE B 48 TYR B 50 -1 O THR B 49 N VAL B 40
SHEET 1 H 4 GLN B 160 ASP B 163 0
SHEET 2 H 4 ALA B 193 VAL B 196 1 O ILE B 194 N PHE B 162
SHEET 3 H 4 PHE B 319 SER B 320 -1 O SER B 320 N ALA B 193
SHEET 4 H 4 ALA B 301 VAL B 302 -1 N VAL B 302 O PHE B 319
SHEET 1 I 3 ARG B 208 ILE B 209 0
SHEET 2 I 3 LEU B 257 GLN B 260 -1 O GLN B 260 N ARG B 208
SHEET 3 I 3 GLU B 267 PHE B 269 -1 O GLU B 267 N LEU B 259
SHEET 1 J 2 GLY B 219 ARG B 221 0
SHEET 2 J 2 VAL B 227 GLY B 229 -1 O ARG B 228 N TYR B 220
SHEET 1 K 2 GLU B 278 PRO B 280 0
SHEET 2 K 2 ARG B 295 TYR B 297 -1 O TRP B 296 N VAL B 279
SHEET 1 L 3 LEU B 312 PHE B 314 0
SHEET 2 L 3 LEU B 306 ILE B 309 -1 N LEU B 307 O PHE B 314
SHEET 3 L 3 ALA B 438 ARG B 440 -1 O ARG B 440 N LEU B 306
LINK SG CYS A 63 ZN ZN A 862 1555 1555 2.28
LINK SG CYS A 68 ZN ZN A 862 1555 1555 2.36
LINK SG CYS A 150 FE HEC A 861 1555 1555 2.37
LINK ZN ZN A 862 SG CYS B 63 1555 1555 2.31
LINK ZN ZN A 862 SG CYS B 68 1555 1555 2.37
LINK SG CYS B 150 FE HEC B1861 1555 1555 2.60
CISPEP 1 SER A 436 PRO A 437 0 -0.18
CISPEP 2 SER B 436 PRO B 437 0 0.21
SITE 1 AC1 11 TRP A 144 ARG A 149 CYS A 150 VAL A 151
SITE 2 AC1 11 PHE A 319 TRP A 322 TRP A 413 PHE A 439
SITE 3 AC1 11 TYR A 441 327 A 864 MPD A1866
SITE 1 AC2 4 CYS A 63 CYS A 68 CYS B 63 CYS B 68
SITE 1 AC3 9 GLN A 213 PRO A 300 VAL A 302 SER A 320
SITE 2 AC3 9 GLY A 321 TRP A 322 GLU A 327 HEC A 861
SITE 3 AC3 9 CL A1865
SITE 1 AC4 8 TRP A 411 PHE A 426 HIS A 427 GLN A 428
SITE 2 AC4 8 SER B 71 VAL B 73 ALA B 412 TRP B 413
SITE 1 AC5 3 TYR A 323 ASN A 332 327 A 864
SITE 1 AC6 5 GLY A 152 TRP A 322 VAL A 384 SER A 392
SITE 2 AC6 5 HEC A 861
SITE 1 AC7 5 VAL A 73 ALA A 412 TRP A 413 PHE B 426
SITE 2 AC7 5 HIS B 427
SITE 1 AC8 3 TYR B 323 ASN B 332 327 B1864
SITE 1 AC9 6 ILE B 154 TRP B 322 VAL B 384 ALA B 389
SITE 2 AC9 6 SER B 392 HEC B1861
SITE 1 BC1 13 TRP B 144 ARG B 149 CYS B 150 VAL B 151
SITE 2 BC1 13 PHE B 319 TRP B 322 MET B 324 TRP B 413
SITE 3 BC1 13 PHE B 439 TYR B 441 MPD B 867 327 B1864
SITE 4 BC1 13 HOH B1925
SITE 1 BC2 9 GLN B 213 PRO B 300 VAL B 302 SER B 320
SITE 2 BC2 9 GLY B 321 TRP B 322 GLU B 327 CL B 865
SITE 3 BC2 9 HEC B1861
CRYST1 71.090 90.150 156.100 90.00 90.00 90.00 P 21 21 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 0.014067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011093 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006406 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
