HEADER OXIDOREDUCTASE 10-JUN-09 3HSO
TITLE TERNARY STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE WITH NHA AND NO
TITLE 2 BOUND(1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 297-718;
COMPND 5 SYNONYM: BNOS, NOS TYPE I, NEURONAL NOS, N-NOS, NNOS, CONSTITUTIVE
COMPND 6 NOS, NC-NOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: NOS1, BNOS;
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 HEME ENZYME DIATOMIC LIGAND, ALTERNATIVE
KEYWDS 2 SPLICING, CALMODULIN-BINDING, CELL MEMBRANE, CELL PROJECTION, FAD,
KEYWDS 3 FMN, HEME, IRON, MEMBRANE, METAL-BINDING, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DOUKOV,H.LI,M.SOLTIS,T.L.POULOS
REVDAT 4 06-SEP-23 3HSO 1 REMARK LINK
REVDAT 3 24-JUL-19 3HSO 1 REMARK
REVDAT 2 17-NOV-09 3HSO 1 JRNL
REVDAT 1 20-OCT-09 3HSO 0
JRNL AUTH T.DOUKOV,H.LI,M.SOLTIS,T.L.POULOS
JRNL TITL SINGLE CRYSTAL STRUCTURAL AND ABSORPTION SPECTRAL
JRNL TITL 2 CHARACTERIZATIONS OF NITRIC OXIDE SYNTHASE COMPLEXED WITH
JRNL TITL 3 N(OMEGA)-HYDROXY-L-ARGININE AND DIATOMIC LIGANDS.
JRNL REF BIOCHEMISTRY V. 48 10246 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19791770
JRNL DOI 10.1021/BI9009743
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 59468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2983
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.1611 - 5.5654 0.87 2668 157 0.1745 0.1907
REMARK 3 2 5.5654 - 4.4183 0.91 2668 152 0.1411 0.1689
REMARK 3 3 4.4183 - 3.8601 0.92 2669 152 0.1349 0.2112
REMARK 3 4 3.8601 - 3.5072 0.93 2681 133 0.1373 0.2065
REMARK 3 5 3.5072 - 3.2559 0.94 2694 146 0.1462 0.1865
REMARK 3 6 3.2559 - 3.0640 0.95 2728 127 0.1578 0.2068
REMARK 3 7 3.0640 - 2.9105 0.95 2705 144 0.1643 0.2235
REMARK 3 8 2.9105 - 2.7839 0.95 2725 155 0.1623 0.2489
REMARK 3 9 2.7839 - 2.6767 0.96 2704 153 0.1692 0.2142
REMARK 3 10 2.6767 - 2.5843 0.97 2752 123 0.1769 0.2364
REMARK 3 11 2.5843 - 2.5035 0.97 2759 145 0.1684 0.2011
REMARK 3 12 2.5035 - 2.4320 0.96 2725 128 0.1780 0.2466
REMARK 3 13 2.4320 - 2.3680 0.97 2753 142 0.1882 0.2534
REMARK 3 14 2.3680 - 2.3102 0.96 2738 139 0.2060 0.2816
REMARK 3 15 2.3102 - 2.2577 0.98 2717 150 0.2020 0.2595
REMARK 3 16 2.2577 - 2.2096 0.96 2730 139 0.2172 0.3047
REMARK 3 17 2.2096 - 2.1654 0.97 2710 155 0.2248 0.3118
REMARK 3 18 2.1654 - 2.1246 0.95 2714 137 0.2395 0.3066
REMARK 3 19 2.1246 - 2.0866 0.95 2646 136 0.2667 0.3469
REMARK 3 20 2.0866 - 2.0512 0.92 2590 131 0.2881 0.3584
REMARK 3 21 2.0512 - 2.0200 0.86 2409 139 0.3034 0.3264
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 61.22
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 7156
REMARK 3 ANGLE : 1.424 9755
REMARK 3 CHIRALITY : 0.102 1014
REMARK 3 PLANARITY : 0.007 1242
REMARK 3 DIHEDRAL : 18.674 2603
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0531 4.9269 59.8539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1216 T22: 0.1154
REMARK 3 T33: 0.1015 T12: -0.0524
REMARK 3 T13: -0.0036 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: -0.3119 L22: 0.2768
REMARK 3 L33: 2.3639 L12: -0.1298
REMARK 3 L13: -0.4007 L23: -0.1238
REMARK 3 S TENSOR
REMARK 3 S11: -0.0823 S12: 0.1230 S13: -0.0037
REMARK 3 S21: -0.0054 S22: -0.0485 S23: 0.0167
REMARK 3 S31: 0.1148 S32: -0.2672 S33: -0.0012
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HSO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053534.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL1-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : 0.03700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : 0.25600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB CODE 1LZX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, MES, AMMONIUM ACETATE, SDS,
REMARK 280 GSH, PH 5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 278K
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 25.91500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.32000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.22000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.32000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.91500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.22000
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: 10200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 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 CYS A 297
REMARK 465 PRO A 298
REMARK 465 SER A 339
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 THR A 342
REMARK 465 ARG A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 GLU A 346
REMARK 465 ASP A 347
REMARK 465 SER B 339
REMARK 465 GLN B 340
REMARK 465 HIS B 341
REMARK 465 THR B 342
REMARK 465 ARG B 343
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 432 CB CYS B 432 SG 0.118
REMARK 500
REMARK 500 REMARK: NULL
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 ARG B 669 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 392 -5.92 65.58
REMARK 500 THR A 466 -83.65 -116.18
REMARK 500 PHE A 517 50.83 -143.31
REMARK 500 CYS A 582 55.56 -151.99
REMARK 500 ARG A 603 -130.64 -114.42
REMARK 500 SER B 392 -14.17 82.27
REMARK 500 THR B 466 -83.81 -114.11
REMARK 500 CYS B 582 55.84 -157.23
REMARK 500 VAL B 595 -63.99 -91.38
REMARK 500 ARG B 603 -135.33 -119.06
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 900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 114.6
REMARK 620 3 CYS B 326 SG 122.2 98.9
REMARK 620 4 CYS B 331 SG 105.0 99.9 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 750 NA 91.0
REMARK 620 3 HEM A 750 NB 88.2 86.7
REMARK 620 4 HEM A 750 NC 90.1 178.5 92.2
REMARK 620 5 HEM A 750 ND 94.2 90.4 176.3 90.6
REMARK 620 6 NO A 752 N 175.8 93.2 92.6 85.7 85.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 750 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 750 NA 94.0
REMARK 620 3 HEM B 750 NB 91.9 89.3
REMARK 620 4 HEM B 750 NC 91.2 174.3 92.8
REMARK 620 5 HEM B 750 ND 91.9 89.1 175.9 88.4
REMARK 620 6 NO B 752 N 171.2 92.6 94.0 82.1 82.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAR A 770
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 860
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO B 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 1760
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAR B 1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1860
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HSN RELATED DB: PDB
REMARK 900 RELATED ID: 3HSP RELATED DB: PDB
DBREF 3HSO A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 3HSO B 297 718 UNP P29476 NOS1_RAT 297 718
SEQRES 1 A 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 A 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 A 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 A 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 A 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 A 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 A 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 422 THR HIS VAL TRP LYS GLY
SEQRES 1 B 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 B 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 B 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 B 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 B 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 B 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 B 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 422 THR HIS VAL TRP LYS GLY
HET HEM A 750 43
HET NO A 752 2
HET H4B A 760 17
HET HAR A 770 13
HET ACT A 860 4
HET ZN A 900 1
HET HEM B 750 43
HET NO B 752 2
HET H4B B1760 17
HET HAR B1770 13
HET ACT B1860 4
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM NO NITRIC OXIDE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM HAR N-OMEGA-HYDROXY-L-ARGININE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETSYN HEM HEME
HETSYN NO NITROGEN MONOXIDE
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 NO 2(N O)
FORMUL 5 H4B 2(C9 H15 N5 O3)
FORMUL 6 HAR 2(C6 H14 N4 O3)
FORMUL 7 ACT 2(C2 H3 O2 1-)
FORMUL 8 ZN ZN 2+
FORMUL 14 HOH *441(H2 O)
HELIX 1 1 THR A 315 SER A 320 5 6
HELIX 2 2 THR A 350 ILE A 369 1 20
HELIX 3 3 SER A 374 SER A 392 1 19
HELIX 4 4 LYS A 397 ASN A 411 1 15
HELIX 5 5 GLY A 417 TRP A 421 5 5
HELIX 6 6 THR A 434 ASN A 451 1 18
HELIX 7 7 LYS A 452 ASN A 454 5 3
HELIX 8 8 ASN A 498 GLN A 508 1 11
HELIX 9 9 PRO A 537 VAL A 541 5 5
HELIX 10 10 PHE A 551 GLY A 558 5 8
HELIX 11 11 MET A 589 VAL A 595 1 7
HELIX 12 12 VAL A 595 ASP A 600 1 6
HELIX 13 13 ILE A 606 ASP A 615 1 10
HELIX 14 14 LYS A 620 SER A 623 5 4
HELIX 15 15 LEU A 624 ASP A 644 1 21
HELIX 16 16 ASP A 650 GLY A 670 1 21
HELIX 17 17 ASP A 675 VAL A 680 1 6
HELIX 18 18 SER A 684 GLN A 693 5 10
HELIX 19 19 ASP A 709 THR A 713 5 5
HELIX 20 20 THR B 315 SER B 320 5 6
HELIX 21 21 THR B 350 ILE B 369 1 20
HELIX 22 22 SER B 374 SER B 392 1 19
HELIX 23 23 LYS B 397 ASN B 411 1 15
HELIX 24 24 GLY B 417 TRP B 421 5 5
HELIX 25 25 THR B 434 ASN B 451 1 18
HELIX 26 26 LYS B 452 ASN B 454 5 3
HELIX 27 27 ASN B 498 GLY B 509 1 12
HELIX 28 28 PRO B 537 VAL B 541 5 5
HELIX 29 29 TRP B 553 GLY B 558 5 6
HELIX 30 30 GLY B 590 VAL B 595 1 6
HELIX 31 31 VAL B 595 ASP B 600 1 6
HELIX 32 32 ILE B 606 ASP B 615 1 10
HELIX 33 33 LYS B 620 SER B 623 5 4
HELIX 34 34 LEU B 624 ASP B 644 1 21
HELIX 35 35 ASP B 650 GLY B 670 1 21
HELIX 36 36 ASP B 675 VAL B 680 1 6
HELIX 37 37 SER B 684 GLN B 693 5 10
HELIX 38 38 ASP B 709 THR B 713 5 5
SHEET 1 A 2 LEU A 301 LYS A 304 0
SHEET 2 A 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 B 3 GLN A 425 ASP A 428 0
SHEET 2 B 3 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 B 3 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 1 C 3 ARG A 473 VAL A 474 0
SHEET 2 C 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 C 3 GLU A 532 PHE A 534 -1 O PHE A 534 N LEU A 522
SHEET 1 D 2 GLY A 484 LYS A 486 0
SHEET 2 D 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 E 2 GLU A 543 PRO A 545 0
SHEET 2 E 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 F 3 LEU A 577 PHE A 579 0
SHEET 2 F 3 LEU A 571 ILE A 574 -1 N LEU A 572 O PHE A 579
SHEET 3 F 3 SER A 703 GLU A 705 -1 O SER A 703 N GLU A 573
SHEET 1 G 2 LEU B 301 LYS B 304 0
SHEET 2 G 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 H 4 GLN B 425 ASP B 428 0
SHEET 2 H 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 H 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 H 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 I 3 ARG B 473 VAL B 474 0
SHEET 2 I 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 I 3 GLU B 532 PHE B 534 -1 O GLU B 532 N LEU B 524
SHEET 1 J 2 GLY B 484 LYS B 486 0
SHEET 2 J 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 K 2 GLU B 543 PRO B 545 0
SHEET 2 K 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 L 3 LEU B 577 PHE B 579 0
SHEET 2 L 3 LEU B 571 ILE B 574 -1 N LEU B 572 O PHE B 579
SHEET 3 L 3 SER B 703 GLU B 705 -1 O SER B 703 N GLU B 573
SHEET 1 M 2 TYR B 588 MET B 589 0
SHEET 2 M 2 ILE B 648 VAL B 649 1 O VAL B 649 N TYR B 588
LINK SG CYS A 326 ZN ZN A 900 1555 1555 2.37
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.39
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.38
LINK FE HEM A 750 N NO A 752 1555 1555 1.80
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.51
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.57
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.40
LINK FE HEM B 750 N NO B 752 1555 1555 1.80
CISPEP 1 THR A 701 PRO A 702 0 -0.80
CISPEP 2 THR B 701 PRO B 702 0 -2.52
SITE 1 AC1 20 TRP A 409 CYS A 415 VAL A 416 SER A 457
SITE 2 AC1 20 PHE A 584 SER A 585 TRP A 587 GLU A 592
SITE 3 AC1 20 TRP A 678 PHE A 704 TYR A 706 NO A 752
SITE 4 AC1 20 H4B A 760 HAR A 770 ACT A 860 HOH A 906
SITE 5 AC1 20 HOH A 950 HOH A 966 HOH A 975 HOH A1011
SITE 1 AC2 3 PHE A 584 HEM A 750 HAR A 770
SITE 1 AC3 14 SER A 334 ARG A 596 VAL A 677 TRP A 678
SITE 2 AC3 14 HEM A 750 HOH A 921 HOH A 944 HOH A 945
SITE 3 AC3 14 HOH A 950 HOH A 996 TRP B 676 PHE B 691
SITE 4 AC3 14 HIS B 692 GLU B 694
SITE 1 AC4 13 GLN A 478 TYR A 562 PRO A 565 GLY A 586
SITE 2 AC4 13 TRP A 587 TYR A 588 GLU A 592 ASP A 597
SITE 3 AC4 13 HEM A 750 NO A 752 HOH A 913 HOH A 940
SITE 4 AC4 13 HOH A1056
SITE 1 AC5 5 TRP A 587 VAL A 649 SER A 657 HEM A 750
SITE 2 AC5 5 HOH A1017
SITE 1 AC6 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC7 20 TRP B 409 CYS B 415 SER B 457 PHE B 584
SITE 2 AC7 20 SER B 585 GLY B 586 TRP B 587 GLU B 592
SITE 3 AC7 20 TRP B 678 PHE B 704 TYR B 706 NO B 752
SITE 4 AC7 20 HOH B 920 HOH B 926 HOH B 979 HOH B1058
SITE 5 AC7 20 HOH B1092 HOH B1099 H4B B1760 HAR B1770
SITE 1 AC8 3 PHE B 584 HEM B 750 HAR B1770
SITE 1 AC9 14 TRP A 676 PHE A 691 HIS A 692 HOH A 964
SITE 2 AC9 14 SER B 334 MET B 336 ARG B 596 VAL B 677
SITE 3 AC9 14 TRP B 678 HEM B 750 HOH B 936 HOH B 979
SITE 4 AC9 14 HOH B 998 HOH B1100
SITE 1 BC1 15 GLN B 478 TYR B 562 PRO B 565 VAL B 567
SITE 2 BC1 15 GLY B 586 TRP B 587 TYR B 588 GLU B 592
SITE 3 BC1 15 ASP B 597 HEM B 750 NO B 752 HOH B 913
SITE 4 BC1 15 HOH B 967 HOH B 997 HOH B1098
SITE 1 BC2 6 TRP B 587 VAL B 649 HOH B 960 HOH B 987
SITE 2 BC2 6 HOH B 995 HOH B1060
CRYST1 51.830 110.440 164.640 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 0.019294 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009055 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006074 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
