HEADER OXIDOREDUCTASE 22-MAR-15 4UGX
TITLE STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH
TITLE 2 N-(3-((ETHYL(2-(3-FLUOROPHENYL)ETHYL)AMINO)METHYL)PHENYL)THIOPHENE-2-
TITLE 3 CARBOXIMIDAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE OXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NOSOXY-LIKE PROTEIN, NITRIC OXIDE SYNTHASE;
COMPND 5 EC: 1.14.13.165;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 ATCC: 23857;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS OXIDOREDUCTASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.HOLDEN,T.L.POULOS
REVDAT 5 10-JAN-24 4UGX 1 REMARK
REVDAT 4 06-FEB-19 4UGX 1 REMARK
REVDAT 3 30-JAN-19 4UGX 1 REMARK
REVDAT 2 22-JUL-15 4UGX 1 JRNL
REVDAT 1 24-JUN-15 4UGX 0
JRNL AUTH J.K.HOLDEN,D.DEJAM,M.C.LEWIS,H.HUANG,S.KANG,Q.JING,F.XUE,
JRNL AUTH 2 R.B.SILVERMAN,T.L.POULOS
JRNL TITL INHIBITOR BOUND CRYSTAL STRUCTURES OF BACTERIAL NITRIC OXIDE
JRNL TITL 2 SYNTHASE.
JRNL REF BIOCHEMISTRY V. 54 4075 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 26062720
JRNL DOI 10.1021/ACS.BIOCHEM.5B00431
REMARK 2
REMARK 2 RESOLUTION. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 40897
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2111
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 37.8833 - 4.5848 1.00 2795 151 0.1564 0.1790
REMARK 3 2 4.5848 - 3.6400 1.00 2655 148 0.1306 0.1565
REMARK 3 3 3.6400 - 3.1802 1.00 2639 135 0.1487 0.1668
REMARK 3 4 3.1802 - 2.8895 1.00 2636 125 0.1545 0.2045
REMARK 3 5 2.8895 - 2.6825 1.00 2605 133 0.1538 0.2319
REMARK 3 6 2.6825 - 2.5243 1.00 2596 123 0.1553 0.1842
REMARK 3 7 2.5243 - 2.3979 0.99 2557 164 0.1553 0.2118
REMARK 3 8 2.3979 - 2.2936 0.99 2540 159 0.1636 0.2086
REMARK 3 9 2.2936 - 2.2053 0.99 2572 158 0.1693 0.2182
REMARK 3 10 2.2053 - 2.1292 0.99 2549 114 0.1821 0.1993
REMARK 3 11 2.1292 - 2.0626 0.99 2557 129 0.2070 0.2659
REMARK 3 12 2.0626 - 2.0037 0.99 2565 119 0.2087 0.2329
REMARK 3 13 2.0037 - 1.9509 0.99 2530 144 0.2281 0.2388
REMARK 3 14 1.9509 - 1.9033 0.99 2506 158 0.2639 0.3434
REMARK 3 15 1.9033 - 1.8601 0.98 2484 151 0.3029 0.3317
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.38
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 : 0.012 3136
REMARK 3 ANGLE : 1.498 4263
REMARK 3 CHIRALITY : 0.090 438
REMARK 3 PLANARITY : 0.006 545
REMARK 3 DIHEDRAL : 14.477 1166
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6864 19.7103 22.8147
REMARK 3 T TENSOR
REMARK 3 T11: 0.2160 T22: 0.2083
REMARK 3 T33: 0.2239 T12: -0.0199
REMARK 3 T13: 0.0168 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 0.8751 L22: 1.5764
REMARK 3 L33: 1.0642 L12: 0.2079
REMARK 3 L13: 0.1476 L23: -0.2123
REMARK 3 S TENSOR
REMARK 3 S11: -0.0655 S12: 0.1290 S13: 0.0837
REMARK 3 S21: -0.2103 S22: 0.0733 S23: -0.0705
REMARK 3 S31: -0.1387 S32: 0.0768 S33: -0.0055
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 4UGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40955
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 37.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 1.14000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 4D3T
REMARK 200
REMARK 200 REMARK: CC ONE HALF FOR FULL DATA SET AT 0.997. CC ONE HALF FOR
REMARK 200 HIGH RESOLUTION SHELL AT 0.545
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 60 MM BIS-TRIS METHANE, 40 MM CITRIC
REMARK 280 ACID, 20% PEG3350, 1.9% 1-PROPANOL, PH 7.6, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.29650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.46350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.29650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.46350
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: 7460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2242 LIES ON A SPECIAL POSITION.
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 MET A 1
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 GLU A 117 -76.67 -107.29
REMARK 500 ALA A 233 69.20 -157.70
REMARK 500 ARG A 247 -67.08 -128.44
REMARK 500 ARG A 254 -123.46 -117.53
REMARK 500 SER A 335 51.12 35.64
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 HEM A 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 66 SG
REMARK 620 2 HEM A 901 NA 98.2
REMARK 620 3 HEM A 901 NB 93.8 86.1
REMARK 620 4 HEM A 901 NC 97.5 164.0 90.2
REMARK 620 5 HEM A 901 ND 101.3 89.3 164.7 90.3
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H4B A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1366
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5H4 A 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4UG5 RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-(2-(5-(2-(2-AMINO-6-METHYLPYRIDIN- 4-YL)ETHYL)PYRIDIN-3-YL)
REMARK 900 ETHYL)-4-METHYLPYRIDIN-2- AMINE
REMARK 900 RELATED ID: 4UG6 RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-(PYRIDINE-3,5-DIYLDIETHANE-2,1- DIYL)BIS(4-METHYLPYRIDIN-
REMARK 900 2-AMINE)
REMARK 900 RELATED ID: 4UG7 RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 3,5-BIS(2-(6-AMINO-4-METHYLPYRIDIN- 2-YL)ETHYL)BENZONITRILE
REMARK 900 RELATED ID: 4UG8 RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-(5-((3R,4R)-4-((6-AZANYL-4-METHYL -PYRIDIN-2-YL)METHYL)
REMARK 900 PYRROLIDIN-3-YL)OXYPENTYL)-4- METHYL-PYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UG9 RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-((4-(3-AMINOPROPYL)BENZENE-1,3- DIYL)DIETHANE-2,1-DIYL)
REMARK 900 BIS(4-METHYLPYRIDIN-2-AMINE)
REMARK 900 RELATED ID: 4UGA RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-((3-(((2-(3-FLUOROPHENYL)ETHYL)AMINO )METHYL)PHENOXY)METHYL)-
REMARK 900 4-METHYLPYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UGB RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-(((5-(((2-(3-FLUOROPHENYL)ETHYL)AMINO )METHYL)PYRIDIN-3-YL)
REMARK 900 OXY)METHYL)-4-METHYLPYRIDIN-2- AMINE
REMARK 900 RELATED ID: 4UGC RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-(((2S)-3-AMINOPROPANE-1,2-DIYL) BIS(OXYMETHANEDIYL))BIS(4-
REMARK 900 METHYLPYRIDIN-2-AMINE)
REMARK 900 RELATED ID: 4UGD RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-((((2S)-1-AMINO-4-((6-AMINO-4- METHYLPYRIDIN-2-YL)METHOXY)
REMARK 900 BUTAN-2-YL)OXY)METHYL)-4 -METHYLPYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UGE RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 4-METHYL-6-((3-(PIPERIDIN-4-YLMETHOXY) PHENOXY)METHYL)PYRIDIN-
REMARK 900 2-AMINE
REMARK 900 RELATED ID: 4UGF RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-((((3S, 5R)-5-(((6-AMINO-4- METHYLPYRIDIN-2-YL)METHOXY)
REMARK 900 METHYL)PYRROLIDIN-3-YL)OXY )METHYL)-4-METHYLPYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UGG RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH (R)-6-(2-AMINO-2-(3-(2-(6-AMINO-4 -METHYLPYRIDIN-2-YL)ETHYL)
REMARK 900 PHENYL)ETHYL)-4-METHYLPYRIDIN -2-AMINE
REMARK 900 RELATED ID: 4UGH RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N1-(3-(2-(6-AMINO-4-METHYLPYRIDIN-2- YL)ETHYL)PHENYL)-N1,N2-
REMARK 900 DIMETHYLETHANE-1,2-DIAMINE
REMARK 900 RELATED ID: 4UGI RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N1-(6-(2-(6-AMINO-4-METHYLPYRIDIN-2- YL)ETHYL)PYRIDIN-2-YL)-N1,
REMARK 900 N2-DIMETHYLETHANE-1,2- DIAMINE
REMARK 900 RELATED ID: 4UGJ RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 3-(2-(6-AMINO-4-METHYLPYRIDIN-2-YL) ETHYL)-5-(METHYL(2-
REMARK 900 (METHYLAMINO)ETHYL)AMINO)BENZONITRILE
REMARK 900 RELATED ID: 4UGK RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-(2-(5-(2-(DIMETHYLAMINO)ETHYL)PYRIDIN -3-YL)ETHYL)-4-
REMARK 900 METHYLPYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UGL RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N1-(3-(2-(6-AMINO-4-METHYLPYRIDIN-2- YL)ETHYL)-5-FLUOROPHENYL)-
REMARK 900 N1-CYCLOPROPYL-N2-METHYLETHANE -1,2-DIAMINE
REMARK 900 RELATED ID: 4UGM RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N,N'-(ETHANE-1,2-DIYLDIBENZENE-3,1- DIYL)DITHIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGN RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH (S)-N-(3-(((PYRROLIDIN-2-YLMETHYL)AMINO )METHYL)PHENYL)
REMARK 900 THIOPHENE-2-CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGO RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N-(4-(2-(ETHYL(3-(((E)-IMINO(THIOPHEN -2-YL)METHYL)AMINO)
REMARK 900 BENZYL)AMINO)ETHYL)PHENYL) THIOPHENE-2-CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGP RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N',N'-(((2R)-3-AMINOPROPANE-1,2-DIYL )
REMARK 900 BIS(OXYMETHANEDIYLBENZENE-3,1-DIYL))DITHIOPHENE-2- CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGQ RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N,N''-(((2S)-3-AMINOPROPANE-1,2-DIYL )
REMARK 900 BIS(OXYMETHANEDIYLBENZENE-3,1-DIYL))DITHIOPHENE-2- CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGR RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N-(3-(((2S,4S)-4-((3-((C-THIOPHEN-2 -YLCARBONIMIDOYL)AMINO)
REMARK 900 PHENYL)METHOXY)PYRROLIDIN-2-YL) METHOXYMETHYL)PHENYL)THIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGS RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N,N'-(ETHANE-1,2-DIYLBIS(OXYBENZENE-3 ,1-DIYL))DITHIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGT RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N-(3-((PYRROLIDIN-3-YLOXY)METHYL)PHENYL )THIOPHENE-2-
REMARK 900 CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGU RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N'-(4-(((2S,4R)-4-(3-((C-THIOPHEN-2 -YLCARBONIMIDOYL)AMINO)
REMARK 900 PHENOXY)PYRROLIDIN-2-YL)METHOXY) PHENYL)THIOPHENE-2-CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4UGV RELATED DB: PDB
REMARK 900 STRUCTURE OF Y357F BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN
REMARK 900 COMPLEX WITH ARGININE AND 5,6,7,8- TETRAHYDROBIOPTERIN
REMARK 900 RELATED ID: 4UGW RELATED DB: PDB
REMARK 900 STRUCTURE OF Y357F BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN
REMARK 900 COMPLEX WITH 6-(5-((3R,4R)-4-((6- AZANYL-4-METHYL-PYRIDIN-2-YL)
REMARK 900 METHYL)PYRROLIDIN-3-YL )OXYPENTYL)-4-METHYL-PYRIDIN-2-AMINE
REMARK 900 RELATED ID: 4UGY RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N1-(5-(2-(6-AMINO-4-METHYLPYRIDIN-2- YL)ETHYL)PYRIDIN-3-YL)-N1,
REMARK 900 N2-DIMETHYLETHANE-1,2- DIAMINE
DBREF 4UGX A 1 363 UNP O34453 NOSO_BACSU 1 363
SEQADV 4UGX ALA A 25 UNP O34453 GLU 25 ENGINEERED MUTATION
SEQADV 4UGX ALA A 26 UNP O34453 GLU 26 ENGINEERED MUTATION
SEQADV 4UGX ALA A 316 UNP O34453 GLU 316 ENGINEERED MUTATION
SEQRES 1 A 363 MET GLU GLU LYS GLU ILE LEU TRP ASN GLU ALA LYS ALA
SEQRES 2 A 363 PHE ILE ALA ALA CYS TYR GLN GLU LEU GLY LYS ALA ALA
SEQRES 3 A 363 GLU VAL LYS ASP ARG LEU ALA ASP ILE LYS SER GLU ILE
SEQRES 4 A 363 ASP LEU THR GLY SER TYR VAL HIS THR LYS GLU GLU LEU
SEQRES 5 A 363 GLU HIS GLY ALA LYS MET ALA TRP ARG ASN SER ASN ARG
SEQRES 6 A 363 CYS ILE GLY ARG LEU PHE TRP ASN SER LEU ASN VAL ILE
SEQRES 7 A 363 ASP ARG ARG ASP VAL ARG THR LYS GLU GLU VAL ARG ASP
SEQRES 8 A 363 ALA LEU PHE HIS HIS ILE GLU THR ALA THR ASN ASN GLY
SEQRES 9 A 363 LYS ILE ARG PRO THR ILE THR ILE PHE PRO PRO GLU GLU
SEQRES 10 A 363 LYS GLY GLU LYS GLN VAL GLU ILE TRP ASN HIS GLN LEU
SEQRES 11 A 363 ILE ARG TYR ALA GLY TYR GLU SER ASP GLY GLU ARG ILE
SEQRES 12 A 363 GLY ASP PRO ALA SER CYS SER LEU THR ALA ALA CYS GLU
SEQRES 13 A 363 GLU LEU GLY TRP ARG GLY GLU ARG THR ASP PHE ASP LEU
SEQRES 14 A 363 LEU PRO LEU ILE PHE ARG MET LYS GLY ASP GLU GLN PRO
SEQRES 15 A 363 VAL TRP TYR GLU LEU PRO ARG SER LEU VAL ILE GLU VAL
SEQRES 16 A 363 PRO ILE THR HIS PRO ASP ILE GLU ALA PHE SER ASP LEU
SEQRES 17 A 363 GLU LEU LYS TRP TYR GLY VAL PRO ILE ILE SER ASP MET
SEQRES 18 A 363 LYS LEU GLU VAL GLY GLY ILE HIS TYR ASN ALA ALA PRO
SEQRES 19 A 363 PHE ASN GLY TRP TYR MET GLY THR GLU ILE GLY ALA ARG
SEQRES 20 A 363 ASN LEU ALA ASP GLU LYS ARG TYR ASP LYS LEU LYS LYS
SEQRES 21 A 363 VAL ALA SER VAL ILE GLY ILE ALA ALA ASP TYR ASN THR
SEQRES 22 A 363 ASP LEU TRP LYS ASP GLN ALA LEU VAL GLU LEU ASN LYS
SEQRES 23 A 363 ALA VAL LEU HIS SER TYR LYS LYS GLN GLY VAL SER ILE
SEQRES 24 A 363 VAL ASP HIS HIS THR ALA ALA SER GLN PHE LYS ARG PHE
SEQRES 25 A 363 GLU GLU GLN ALA GLU GLU ALA GLY ARG LYS LEU THR GLY
SEQRES 26 A 363 ASP TRP THR TRP LEU ILE PRO PRO ILE SER PRO ALA ALA
SEQRES 27 A 363 THR HIS ILE PHE HIS ARG SER TYR ASP ASN SER ILE VAL
SEQRES 28 A 363 LYS PRO ASN TYR PHE TYR GLN ASP LYS PRO TYR GLU
HET HEM A 901 43
HET H4B A 902 17
HET CL A1364 1
HET GOL A1365 6
HET GOL A1366 6
HET 5H4 A 803 27
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM 5H4 N-[3-({ETHYL[2-(3-FLUOROPHENYL)ETHYL]AMINO}METHYL)
HETNAM 2 5H4 PHENYL]THIOPHENE-2-CARBOXIMIDAMIDE
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 H4B C9 H15 N5 O3
FORMUL 4 CL CL 1-
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 5H4 C22 H24 F N3 S
FORMUL 8 HOH *263(H2 O)
HELIX 1 1 GLU A 2 LEU A 22 1 21
HELIX 2 2 LYS A 24 ALA A 26 5 3
HELIX 3 3 GLU A 27 GLY A 43 1 17
HELIX 4 4 THR A 48 ASN A 62 1 15
HELIX 5 5 GLY A 68 LEU A 75 5 8
HELIX 6 6 THR A 85 ASN A 102 1 18
HELIX 7 7 ASN A 103 LYS A 105 5 3
HELIX 8 8 SER A 148 LEU A 158 1 11
HELIX 9 9 PRO A 188 VAL A 192 5 5
HELIX 10 10 ILE A 202 GLU A 209 5 8
HELIX 11 11 GLY A 241 ALA A 246 1 6
HELIX 12 12 LYS A 257 GLY A 266 1 10
HELIX 13 13 TYR A 271 ASP A 274 5 4
HELIX 14 14 LEU A 275 GLY A 296 1 22
HELIX 15 15 ASP A 301 ALA A 319 1 19
HELIX 16 16 ASP A 326 ILE A 331 1 6
HELIX 17 17 SER A 335 THR A 339 5 5
HELIX 18 18 HIS A 340 ARG A 344 5 5
SHEET 1 AA 4 ASN A 76 ASP A 79 0
SHEET 2 AA 4 THR A 109 ILE A 112 1 O ILE A 110 N ILE A 78
SHEET 3 AA 4 PHE A 235 ASN A 236 -1 O ASN A 236 N THR A 109
SHEET 4 AA 4 ILE A 217 ILE A 218 -1 O ILE A 218 N PHE A 235
SHEET 1 AB 3 VAL A 123 ILE A 125 0
SHEET 2 AB 3 LEU A 172 MET A 176 -1 O ARG A 175 N GLU A 124
SHEET 3 AB 3 VAL A 183 TYR A 185 -1 O VAL A 183 N PHE A 174
SHEET 1 AC 2 GLY A 135 SER A 138 0
SHEET 2 AC 2 GLU A 141 GLY A 144 -1 O GLU A 141 N SER A 138
SHEET 1 AD 2 GLU A 194 PRO A 196 0
SHEET 2 AD 2 LYS A 211 TYR A 213 -1 O TRP A 212 N VAL A 195
SHEET 1 AE 3 ILE A 228 TYR A 230 0
SHEET 2 AE 3 LYS A 222 VAL A 225 -1 O LEU A 223 N TYR A 230
SHEET 3 AE 3 ASN A 354 PHE A 356 -1 O ASN A 354 N GLU A 224
SHEET 1 AF 2 TYR A 239 MET A 240 0
SHEET 2 AF 2 ILE A 299 VAL A 300 1 N VAL A 300 O TYR A 239
LINK SG CYS A 66 FE HEM A 901 1555 1555 2.45
CISPEP 1 LYS A 352 PRO A 353 0 0.00
SITE 1 AC1 19 TRP A 60 SER A 63 ARG A 65 CYS A 66
SITE 2 AC1 19 PHE A 235 ASN A 236 GLY A 237 TRP A 238
SITE 3 AC1 19 GLU A 243 TRP A 329 TYR A 355 TYR A 357
SITE 4 AC1 19 5H4 A 803 H4B A 902 GOL A1365 HOH A2034
SITE 5 AC1 19 HOH A2159 HOH A2260 HOH A2261
SITE 1 AC2 13 ARG A 247 TRP A 327 THR A 328 TRP A 329
SITE 2 AC2 13 PHE A 342 HIS A 343 ARG A 344 HEM A 901
SITE 3 AC2 13 HOH A2172 HOH A2173 HOH A2240 HOH A2261
SITE 4 AC2 13 HOH A2262
SITE 1 AC3 3 GLN A 129 TYR A 239 ASN A 248
SITE 1 AC4 6 MET A 221 PHE A 356 TYR A 357 HEM A 901
SITE 2 AC4 6 HOH A2032 HOH A2263
SITE 1 AC5 6 GLY A 159 ARG A 161 TRP A 238 SER A 298
SITE 2 AC5 6 ILE A 299 GLN A 308
SITE 1 AC6 13 HIS A 128 ARG A 132 PRO A 216 ILE A 218
SITE 2 AC6 13 PHE A 235 ASN A 236 GLY A 237 TRP A 238
SITE 3 AC6 13 GLU A 243 TYR A 357 HEM A 901 HOH A2085
SITE 4 AC6 13 HOH A2255
CRYST1 80.593 94.927 62.847 90.00 90.00 90.00 P 21 21 2 4
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 0.012408 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015912 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
