HEADER OXIDOREDUCTASE 21-NOV-08 3FC5
TITLE G586S MUTANT NNOSOXY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: OXYGENASE DOMAIN, RESIDUES 297-718;
COMPND 5 SYNONYM: NNOS, BNOS, NOS TYPE I, NEURONAL NOS, N-NOS, CONSTITUTIVE
COMPND 6 NOS, NC-NOS;
COMPND 7 EC: 1.14.13.39;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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 OR BNOS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCRNNR
KEYWDS NNOS, OXYGENASE, G586S, ARGININE, ALTERNATIVE SPLICING, CALMODULIN-
KEYWDS 2 BINDING, CELL MEMBRANE, CELL PROJECTION, FAD, FMN, HEME, IRON,
KEYWDS 3 MEMBRANE, METAL-BINDING, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BRUCKMANN,C.G.MOWAT
REVDAT 3 01-NOV-23 3FC5 1 REMARK
REVDAT 2 10-NOV-21 3FC5 1 REMARK SEQADV LINK
REVDAT 1 03-NOV-09 3FC5 0
JRNL AUTH D.PAPALE,C.BRUCKMANN,C.S.MILES,C.G.MOWAT,S.DAFF
JRNL TITL OXYGEN ACTIVATION IN NEURONAL NO SYNTHASE: STABILISATION OF
JRNL TITL 2 A NOVEL INTERMEDIATE IN THE G586S MUTANT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.59 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 27789
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 34.2688 - 6.2297 0.94 2039 158 0.1923 0.2318
REMARK 3 2 6.2297 - 4.9495 0.96 1984 154 0.1778 0.2032
REMARK 3 3 4.9495 - 4.3252 0.98 1954 152 0.1512 0.2087
REMARK 3 4 4.3252 - 3.9304 0.98 1966 152 0.1700 0.2360
REMARK 3 5 3.9304 - 3.6490 0.98 1972 153 0.1680 0.2143
REMARK 3 6 3.6490 - 3.4341 0.99 1954 151 0.1839 0.2316
REMARK 3 7 3.4341 - 3.2622 0.99 1980 153 0.2021 0.2720
REMARK 3 8 3.2622 - 3.1203 0.99 1961 154 0.2108 0.2744
REMARK 3 9 3.1203 - 3.0003 0.98 1933 149 0.2293 0.3288
REMARK 3 10 3.0003 - 2.8968 0.98 1900 148 0.2349 0.3266
REMARK 3 11 2.8968 - 2.8063 0.90 1780 138 0.2274 0.2841
REMARK 3 12 2.8063 - 2.7261 0.85 1642 127 0.2449 0.3510
REMARK 3 13 2.7261 - 2.6543 0.74 1455 113 0.2411 0.3339
REMARK 3 14 2.6543 - 2.5896 0.66 1269 98 0.2472 0.3226
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 : 52.05
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 29.77400
REMARK 3 B22 (A**2) : -4.14300
REMARK 3 B33 (A**2) : -25.63100
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 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 : 06.000 NULL
REMARK 3 ANGLE : 32.000 NULL
REMARK 3 CHIRALITY : 86.000 NULL
REMARK 3 PLANARITY : 06.000 NULL
REMARK 3 DIHEDRAL : 29.000 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 299:338 OR RESSEQ
REMARK 3 350:716 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 299:338 OR RESSEQ
REMARK 3 350:716 )
REMARK 3 ATOM PAIRS NUMBER : 3315
REMARK 3 RMSD : 0.051
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-08.
REMARK 100 THE DEPOSITION ID IS D_1000050407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8-6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9737
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27819
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
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) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.790
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1OM4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM NA-MES BUFFER (PH 5.8-6.0),
REMARK 280 200MM AMMONIUM ACETATE, 25MM L-ARGININE, 35MICROM SODIUM DODECYL
REMARK 280 SULFATE(SDS), 5MM GLUTATHIONE, 2% ISOPROPANOL, 22-24% (W/V) PEG
REMARK 280 3350 , VAPOR DIFFUSION, TEMPERATURE 291K
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 25.81150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.33550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.13800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.33550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.81150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.13800
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: 9400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 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 VAL A 348
REMARK 465 ARG A 349
REMARK 465 LYS A 717
REMARK 465 GLY A 718
REMARK 465 CYS B 297
REMARK 465 PRO B 298
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 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 A 410 NE - CZ - NH1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 410 NE - CZ - NH2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 514 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG A 514 NE - CZ - NH1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 514 NE - CZ - NH2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 547 NE - CZ - NH1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 547 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 410 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 410 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 514 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 514 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG B 547 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG B 547 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 THR A 321 -58.81 -129.49
REMARK 500 LYS A 370 40.51 70.98
REMARK 500 ALA A 412 90.58 -68.33
REMARK 500 THR A 466 -82.01 -121.03
REMARK 500 ARG A 514 72.69 55.43
REMARK 500 PHE A 517 56.01 -149.85
REMARK 500 CYS A 582 52.57 -154.65
REMARK 500 SER A 586 -132.39 -153.67
REMARK 500 ARG A 603 -130.64 -109.61
REMARK 500 ASP A 617 98.97 -68.77
REMARK 500 CYS A 672 101.13 -166.76
REMARK 500 THR B 321 -57.63 -129.56
REMARK 500 ARG B 349 -150.27 -105.11
REMARK 500 LYS B 370 40.15 72.48
REMARK 500 ALA B 412 90.62 -68.66
REMARK 500 ARG B 418 -7.05 -59.64
REMARK 500 THR B 466 -83.48 -121.53
REMARK 500 ARG B 514 70.36 56.00
REMARK 500 PHE B 517 56.12 -148.00
REMARK 500 CYS B 582 48.90 -153.53
REMARK 500 SER B 586 -133.03 -155.06
REMARK 500 ARG B 603 -129.52 -108.66
REMARK 500 ASP B 617 99.34 -68.96
REMARK 500 CYS B 672 98.61 -164.00
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 104.5
REMARK 620 3 CYS B 326 SG 115.5 108.6
REMARK 620 4 CYS B 331 SG 109.4 106.3 111.8
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 107.8
REMARK 620 3 HEM A 750 NB 99.2 88.8
REMARK 620 4 HEM A 750 NC 88.4 163.8 87.9
REMARK 620 5 HEM A 750 ND 99.7 85.7 161.1 92.4
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 101.7
REMARK 620 3 HEM B 750 NB 97.4 91.6
REMARK 620 4 HEM B 750 NC 85.8 172.6 87.4
REMARK 620 5 HEM B 750 ND 94.3 88.2 168.0 91.3
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 ZN A 900
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 ARG A 770
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B B 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ARG B 771
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OM4 RELATED DB: PDB
REMARK 900 WILD-TYPE
DBREF 3FC5 A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 3FC5 B 297 718 UNP P29476 NOS1_RAT 297 718
SEQADV 3FC5 SER A 586 UNP P29476 GLY 586 ENGINEERED MUTATION
SEQADV 3FC5 SER B 586 UNP P29476 GLY 586 ENGINEERED MUTATION
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 SER 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 SER 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 ZN A 900 1
HET H4B A 760 17
HET ARG A 770 12
HET H4B B 761 17
HET HEM B 750 43
HET ARG B 771 12
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM ZN ZINC ION
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM ARG ARGININE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 ZN ZN 2+
FORMUL 5 H4B 2(C9 H15 N5 O3)
FORMUL 6 ARG 2(C6 H15 N4 O2 1+)
FORMUL 10 HOH *196(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 TRP A 553 GLY A 558 5 6
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 THR A 688 5 5
HELIX 19 19 ASP A 709 HIS A 714 1 6
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 GLN B 508 1 11
HELIX 28 28 PRO B 537 VAL B 541 5 5
HELIX 29 29 PHE B 554 GLY B 558 5 5
HELIX 30 30 MET B 589 VAL B 595 1 7
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 THR B 688 5 5
HELIX 38 38 ASP B 709 HIS B 714 1 6
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 GLU A 705 N LEU A 571
SHEET 1 G 2 LYS B 302 LYS B 304 0
SHEET 2 G 2 VAL B 311 THR B 313 -1 O LEU B 312 N VAL B 303
SHEET 1 H 3 GLN B 425 ASP B 428 0
SHEET 2 H 3 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 H 3 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
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 PHE B 534 N LEU B 522
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 GLU B 705 N LEU B 571
LINK SG CYS A 326 ZN ZN A 900 1555 1555 2.39
LINK SG CYS A 331 ZN ZN A 900 1555 1555 2.32
LINK SG CYS A 415 FE HEM A 750 1555 1555 2.38
LINK ZN ZN A 900 SG CYS B 326 1555 1555 2.36
LINK ZN ZN A 900 SG CYS B 331 1555 1555 2.30
LINK SG CYS B 415 FE HEM B 750 1555 1555 2.54
CISPEP 1 THR A 701 PRO A 702 0 -2.90
CISPEP 2 THR B 701 PRO B 702 0 -0.76
SITE 1 AC1 16 HOH A 19 HOH A 102 HOH A 119 TRP A 409
SITE 2 AC1 16 CYS A 415 GLY A 417 SER A 457 PHE A 584
SITE 3 AC1 16 SER A 586 TRP A 587 GLU A 592 TRP A 678
SITE 4 AC1 16 PHE A 704 TYR A 706 H4B A 760 ARG A 770
SITE 1 AC2 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC3 15 HOH A 3 HOH A 19 HOH A 125 HOH A 134
SITE 2 AC3 15 SER A 334 MET A 336 ARG A 596 VAL A 677
SITE 3 AC3 15 TRP A 678 HEM A 750 TRP B 676 PHE B 691
SITE 4 AC3 15 HIS B 692 GLN B 693 GLU B 694
SITE 1 AC4 10 HOH A 157 GLN A 478 TYR A 562 PRO A 565
SITE 2 AC4 10 SER A 586 TRP A 587 TYR A 588 GLU A 592
SITE 3 AC4 10 ASP A 597 HEM A 750
SITE 1 AC5 16 TRP A 676 PHE A 691 HIS A 692 GLN A 693
SITE 2 AC5 16 GLU A 694 HOH B 9 HOH B 32 HOH B 37
SITE 3 AC5 16 HOH B 117 HOH B 156 SER B 334 MET B 336
SITE 4 AC5 16 ARG B 596 VAL B 677 TRP B 678 HEM B 750
SITE 1 AC6 19 HOH B 9 HOH B 95 HOH B 113 HOH B 130
SITE 2 AC6 19 HOH B 177 TRP B 409 ARG B 414 CYS B 415
SITE 3 AC6 19 GLY B 417 SER B 457 PHE B 584 SER B 586
SITE 4 AC6 19 TRP B 587 GLU B 592 TRP B 678 PHE B 704
SITE 5 AC6 19 TYR B 706 H4B B 761 ARG B 771
SITE 1 AC7 11 HOH B 57 HOH B 58 HOH B 193 GLN B 478
SITE 2 AC7 11 TYR B 562 SER B 586 TRP B 587 TYR B 588
SITE 3 AC7 11 GLU B 592 ASP B 597 HEM B 750
CRYST1 51.623 110.276 164.671 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 0.019371 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009068 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
