HEADER OXIDOREDUCTASE 10-JUN-09 3HSN
TITLE TERNARY STRUCTURE OF NEURONAL NITRIC OXIDE SYNTHASE WITH NHA AND CO
TITLE 2 BOUND
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, CALMODULIN-
KEYWDS 2 BINDING, CELL MEMBRANE, CELL PROJECTION, FAD, FMN, HEME, IRON,
KEYWDS 3 MEMBRANE, METAL-BINDING, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.DOUKOV,H.LI,M.SOLTIS,T.L.POULOS
REVDAT 5 06-SEP-23 3HSN 1 REMARK LINK
REVDAT 4 24-JUL-19 3HSN 1 REMARK
REVDAT 3 13-JUL-11 3HSN 1 VERSN
REVDAT 2 17-NOV-09 3HSN 1 JRNL
REVDAT 1 20-OCT-09 3HSN 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. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 73249
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3717
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 44.1025 - 5.7172 0.97 2803 161 0.1760 0.2004
REMARK 3 2 5.7172 - 4.5394 0.99 2705 152 0.1446 0.1627
REMARK 3 3 4.5394 - 3.9660 0.98 2655 151 0.1264 0.1816
REMARK 3 4 3.9660 - 3.6036 0.99 2640 146 0.1330 0.1733
REMARK 3 5 3.6036 - 3.3454 0.99 2675 144 0.1377 0.1730
REMARK 3 6 3.3454 - 3.1482 0.99 2643 132 0.1547 0.1651
REMARK 3 7 3.1482 - 2.9906 0.99 2645 120 0.1654 0.2522
REMARK 3 8 2.9906 - 2.8604 0.99 2599 166 0.1584 0.2258
REMARK 3 9 2.8604 - 2.7503 0.99 2613 137 0.1578 0.2069
REMARK 3 10 2.7503 - 2.6554 0.99 2655 141 0.1635 0.2006
REMARK 3 11 2.6554 - 2.5724 0.99 2655 107 0.1633 0.1890
REMARK 3 12 2.5724 - 2.4989 0.99 2599 143 0.1591 0.2165
REMARK 3 13 2.4989 - 2.4331 0.99 2661 139 0.1705 0.1951
REMARK 3 14 2.4331 - 2.3737 0.99 2567 133 0.1690 0.2304
REMARK 3 15 2.3737 - 2.3198 0.98 2622 136 0.1724 0.2331
REMARK 3 16 2.3198 - 2.2704 0.98 2529 147 0.1803 0.2452
REMARK 3 17 2.2704 - 2.2250 0.98 2617 130 0.1900 0.2508
REMARK 3 18 2.2250 - 2.1830 0.97 2530 139 0.1927 0.2413
REMARK 3 19 2.1830 - 2.1440 0.97 2534 134 0.1982 0.2709
REMARK 3 20 2.1440 - 2.1077 0.96 2533 132 0.2094 0.2580
REMARK 3 21 2.1077 - 2.0737 0.95 2465 134 0.2054 0.2582
REMARK 3 22 2.0737 - 2.0418 0.94 2460 162 0.2057 0.2563
REMARK 3 23 2.0418 - 2.0118 0.94 2439 126 0.2140 0.2574
REMARK 3 24 2.0118 - 1.9834 0.94 2510 121 0.2374 0.2889
REMARK 3 25 1.9834 - 1.9566 0.92 2400 139 0.2484 0.3022
REMARK 3 26 1.9566 - 1.9312 0.93 2444 116 0.2724 0.3362
REMARK 3 27 1.9312 - 1.9100 0.88 2334 129 0.2853 0.3454
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 : 0.39
REMARK 3 B_SOL : 60.55
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.40
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 : 0.011 7146
REMARK 3 ANGLE : 1.380 9720
REMARK 3 CHIRALITY : 0.088 1007
REMARK 3 PLANARITY : 0.006 1231
REMARK 3 DIHEDRAL : 18.913 2589
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): 12.0977 4.9136 59.9481
REMARK 3 T TENSOR
REMARK 3 T11: 0.0604 T22: 0.0950
REMARK 3 T33: 0.1059 T12: -0.0191
REMARK 3 T13: -0.0003 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 0.1205 L22: 0.4597
REMARK 3 L33: 3.3787 L12: -0.0199
REMARK 3 L13: -0.3373 L23: -0.1308
REMARK 3 S TENSOR
REMARK 3 S11: -0.0543 S12: 0.0821 S13: -0.0129
REMARK 3 S21: 0.0133 S22: -0.0341 S23: 0.0005
REMARK 3 S31: -0.0173 S32: -0.2783 S33: 0.0002
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 3HSN 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_1000053533.
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 : MIRRORS
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 : 73350
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49600
REMARK 200 R SYM FOR SHELL (I) : 0.49600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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 ENTRY 1LZX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
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 26.08000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.52100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.42350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.52100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.08000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.42350
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: 11990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 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 CYS B 297
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: 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 FE HEM B 750 C CMO B 751 1.70
REMARK 500 FE HEM A 750 C CMO A 751 1.71
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 309 -0.66 59.59
REMARK 500 THR A 466 -85.18 -117.16
REMARK 500 CYS A 582 57.73 -152.16
REMARK 500 ARG A 603 -134.16 -111.03
REMARK 500 ASP B 309 12.06 59.81
REMARK 500 THR B 321 -56.27 -120.04
REMARK 500 SER B 392 -1.68 71.21
REMARK 500 THR B 466 -82.38 -116.86
REMARK 500 CYS B 582 54.40 -154.17
REMARK 500 ARG B 603 -132.44 -116.35
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 113.9
REMARK 620 3 CYS B 326 SG 118.7 103.2
REMARK 620 4 CYS B 331 SG 103.7 101.3 115.1
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 92.6
REMARK 620 3 HEM A 750 NB 90.8 87.2
REMARK 620 4 HEM A 750 NC 93.5 173.8 91.4
REMARK 620 5 HEM A 750 ND 97.6 89.6 171.1 90.9
REMARK 620 N 1 2 3 4
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 92.5
REMARK 620 3 HEM B 750 NB 92.0 88.6
REMARK 620 4 HEM B 750 NC 92.0 175.1 89.3
REMARK 620 5 HEM B 750 ND 94.9 91.3 173.0 90.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 751
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 GOL A 880
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 882
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 885
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 886
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO B 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 1760
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HAR B 1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 881
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 883
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 884
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3HSO RELATED DB: PDB
REMARK 900 RELATED ID: 3HSP RELATED DB: PDB
DBREF 3HSN A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 3HSN 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 CMO A 751 2
HET H4B A 760 17
HET HAR A 770 13
HET ACT A 860 4
HET ZN A 900 1
HET GOL A 880 6
HET GOL A 882 6
HET GOL A 885 6
HET GOL A 886 6
HET HEM B 750 43
HET CMO B 751 2
HET H4B B1760 17
HET HAR B1770 13
HET ACT B1860 4
HET GOL B 881 6
HET GOL B 883 6
HET GOL B 884 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CMO CARBON MONOXIDE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM HAR N-OMEGA-HYDROXY-L-ARGININE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 CMO 2(C 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 9 GOL 7(C3 H8 O3)
FORMUL 21 HOH *540(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 LEU A 424 5 8
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 GLY A 509 1 12
HELIX 9 9 PRO A 537 VAL A 541 5 5
HELIX 10 10 TRP A 553 GLY A 558 5 6
HELIX 11 11 GLY A 590 VAL A 595 1 6
HELIX 12 12 VAL A 595 ASP A 600 1 6
HELIX 13 13 ILE A 606 MET A 614 1 9
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 LEU B 424 5 8
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 GLN B 508 1 11
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 MET B 614 1 9
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 4 GLN A 425 ASP A 428 0
SHEET 2 B 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 B 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 B 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
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 TYR A 588 MET A 589 0
SHEET 2 G 2 ILE A 648 VAL A 649 1 O VAL A 649 N TYR A 588
SHEET 1 H 2 LEU B 301 LYS B 304 0
SHEET 2 H 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 I 4 GLN B 425 ASP B 428 0
SHEET 2 I 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 I 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 I 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 J 3 ARG B 473 VAL B 474 0
SHEET 2 J 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 J 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 K 2 GLY B 484 LYS B 486 0
SHEET 2 K 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 L 2 GLU B 543 PRO B 545 0
SHEET 2 L 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 M 3 LEU B 577 PHE B 579 0
SHEET 2 M 3 LEU B 571 ILE B 574 -1 N LEU B 572 O PHE B 579
SHEET 3 M 3 SER B 703 GLU B 705 -1 O GLU B 705 N LEU B 571
SHEET 1 N 2 TYR B 588 MET B 589 0
SHEET 2 N 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 2.33
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.43
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.41
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.39
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.45
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.45
CISPEP 1 THR A 701 PRO A 702 0 -3.41
CISPEP 2 THR B 701 PRO B 702 0 0.37
SITE 1 AC1 22 TRP A 409 ARG A 414 CYS A 415 VAL A 416
SITE 2 AC1 22 SER A 457 PHE A 584 SER A 585 GLY A 586
SITE 3 AC1 22 TRP A 587 GLU A 592 TRP A 678 PHE A 704
SITE 4 AC1 22 TYR A 706 CMO A 751 H4B A 760 HAR A 770
SITE 5 AC1 22 ACT A 860 HOH A 907 HOH A 909 HOH A 926
SITE 6 AC1 22 HOH A 942 HOH A 997
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 901 HOH A 909 HOH A 924
SITE 3 AC3 14 HOH A 946 HOH A1025 TRP B 676 PHE B 691
SITE 4 AC3 14 HIS B 692 GLU B 694
SITE 1 AC4 14 GLN A 478 TYR A 562 PRO A 565 VAL A 567
SITE 2 AC4 14 GLY A 586 TRP A 587 TYR A 588 GLU A 592
SITE 3 AC4 14 ASP A 597 HEM A 750 CMO A 751 HOH A 904
SITE 4 AC4 14 HOH A 908 HOH A1134
SITE 1 AC5 6 GLY A 417 TRP A 587 SER A 657 HEM A 750
SITE 2 AC5 6 HOH A1062 HOH A1121
SITE 1 AC6 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC7 3 LYS A 319 GLN A 364 ARG A 669
SITE 1 AC8 5 ILE A 402 LYS A 406 LEU A 424 GLN A 425
SITE 2 AC8 5 VAL A 426
SITE 1 AC9 6 THR A 492 LEU A 493 GLY A 494 ARG A 516
SITE 2 AC9 6 TYR A 604 GOL A 886
SITE 1 BC1 4 ASN A 605 GLU A 609 GOL A 885 HOH A 996
SITE 1 BC2 20 TRP B 409 ARG B 414 CYS B 415 PHE B 584
SITE 2 BC2 20 SER B 585 GLY B 586 TRP B 587 GLU B 592
SITE 3 BC2 20 TRP B 678 PHE B 704 TYR B 706 CMO B 751
SITE 4 BC2 20 HOH B 902 HOH B 906 HOH B 934 HOH B 938
SITE 5 BC2 20 HOH B1018 HOH B1030 H4B B1760 HAR B1770
SITE 1 BC3 3 PHE B 584 HEM B 750 HAR B1770
SITE 1 BC4 14 TRP A 676 PHE A 691 HIS A 692 SER B 334
SITE 2 BC4 14 MET B 336 ARG B 596 VAL B 677 TRP B 678
SITE 3 BC4 14 HEM B 750 HOH B 906 HOH B 909 HOH B 940
SITE 4 BC4 14 HOH B 957 HOH B1145
SITE 1 BC5 14 GLN B 478 TYR B 562 PRO B 565 VAL B 567
SITE 2 BC5 14 GLY B 586 TRP B 587 TYR B 588 GLU B 592
SITE 3 BC5 14 ASP B 597 HEM B 750 CMO B 751 HOH B 907
SITE 4 BC5 14 HOH B 945 HOH B 976
SITE 1 BC6 6 GLY B 417 GLN B 420 TRP B 587 SER B 657
SITE 2 BC6 6 HOH B1039 HOH B1195
SITE 1 BC7 4 GLN B 364 ARG B 669 THR B 701 HOH B 989
SITE 1 BC8 7 SER B 477 ALA B 497 ASN B 498 ASN B 569
SITE 2 BC8 7 ASP B 709 HOH B 904 HOH B1041
SITE 1 BC9 5 TYR B 604 ASN B 605 ILE B 606 GLU B 609
SITE 2 BC9 5 HOH B1090
CRYST1 52.160 110.847 165.042 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 0.019172 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009021 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006059 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
