HEADER OXIDOREDUCTASE 22-MAR-15 4UGR
TITLE STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH
TITLE 2 N-(3-(((2S,4S)-4-((3-((C-THIOPHEN-2-YLCARBONIMIDOYL)AMINO)PHENYL)
TITLE 3 METHOXY)PYRROLIDIN-2-YL)METHOXYMETHYL)PHENYL)THIOPHENE-2-
TITLE 4 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 4UGR 1 REMARK
REVDAT 4 06-FEB-19 4UGR 1 REMARK
REVDAT 3 30-JAN-19 4UGR 1 REMARK
REVDAT 2 22-JUL-15 4UGR 1 JRNL
REVDAT 1 24-JUN-15 4UGR 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. 2.09 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) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 29061
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) : 0.162
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1470
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 37.9898 - 4.4944 0.97 2856 162 0.1623 0.1952
REMARK 3 2 4.4944 - 3.5682 0.99 2832 151 0.1410 0.1753
REMARK 3 3 3.5682 - 3.1174 0.99 2783 145 0.1683 0.2183
REMARK 3 4 3.1174 - 2.8324 0.99 2783 131 0.1731 0.2351
REMARK 3 5 2.8324 - 2.6295 0.99 2766 131 0.1691 0.2176
REMARK 3 6 2.6295 - 2.4745 0.99 2749 157 0.1581 0.2288
REMARK 3 7 2.4745 - 2.3506 0.99 2698 167 0.1592 0.2097
REMARK 3 8 2.3506 - 2.2483 0.99 2715 154 0.1638 0.2147
REMARK 3 9 2.2483 - 2.1617 0.99 2701 140 0.1677 0.2323
REMARK 3 10 2.1617 - 2.0871 0.98 2708 132 0.1727 0.2313
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.14
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 : 0.010 3141
REMARK 3 ANGLE : 1.390 4272
REMARK 3 CHIRALITY : 0.082 438
REMARK 3 PLANARITY : 0.005 546
REMARK 3 DIHEDRAL : 14.663 1173
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 5.7044 19.6763 22.7520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0168 T22: 0.0324
REMARK 3 T33: -0.0155 T12: -0.0094
REMARK 3 T13: 0.0162 T23: -0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.8901 L22: 1.9702
REMARK 3 L33: 0.9742 L12: 0.2106
REMARK 3 L13: 0.1777 L23: -0.3454
REMARK 3 S TENSOR
REMARK 3 S11: -0.0827 S12: 0.1281 S13: 0.0440
REMARK 3 S21: -0.2369 S22: 0.0797 S23: -0.0326
REMARK 3 S31: -0.1136 S32: 0.0413 S33: 0.0094
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 4UGR 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_1290063326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-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 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29082
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
REMARK 200 RESOLUTION RANGE LOW (A) : 37.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.23000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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 DATASET AT 0.996. CC ONE HALF FOR
REMARK 200 HIGH RESOLUTION SHELL AT 0.960
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.34
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 40.17000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.61000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.17000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.61000
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: 7190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.3 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 A2340 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 ASN A 103 18.98 57.60
REMARK 500 GLU A 117 -76.64 -91.29
REMARK 500 LYS A 118 51.10 -115.96
REMARK 500 ALA A 233 70.25 -159.95
REMARK 500 ARG A 247 -67.57 -130.32
REMARK 500 ARG A 254 -127.77 -116.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2080 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A2123 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A2128 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A2130 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A2136 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH A2368 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A2369 DISTANCE = 6.26 ANGSTROMS
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 97.5
REMARK 620 3 HEM A 901 NB 93.9 85.9
REMARK 620 4 HEM A 901 NC 95.6 166.3 89.2
REMARK 620 5 HEM A 901 ND 101.1 90.0 164.9 91.4
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 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 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6E5 A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 905
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: 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: 4UGX RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH N-(3-((ETHYL(2-(3-FLUOROPHENYL)ETHYL) AMINO)METHYL)PHENYL)
REMARK 900 THIOPHENE-2-CARBOXIMIDAMIDE
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
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E25A, E26A, E316A INTRODUCED
DBREF 4UGR A 1 363 UNP O34453 NOSO_BACSU 1 363
SEQADV 4UGR ALA A 25 UNP O34453 GLU 25 ENGINEERED MUTATION
SEQADV 4UGR ALA A 26 UNP O34453 GLU 26 ENGINEERED MUTATION
SEQADV 4UGR 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 A 903 1
HET 6E5 A 904 38
HET GOL A 905 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM CL CHLORIDE ION
HETNAM 6E5 N-[3-({[(3S,5S)-5-{[(3-{[(Z)-IMINO(THIOPHEN-2-YL)
HETNAM 2 6E5 METHYL]AMINO}BENZYL)OXY]METHYL}PYRROLIDIN-3-
HETNAM 3 6E5 YL]OXY}METHYL)PHENYL]THIOPHENE-2-CARBOXIMIDAMIDE
HETNAM GOL GLYCEROL
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 6E5 C29 H31 N5 O2 S2
FORMUL 6 GOL C3 H8 O3
FORMUL 7 HOH *369(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 ILE A 265 1 9
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 2.49
CISPEP 1 LYS A 352 PRO A 353 0 -1.76
SITE 1 AC1 17 TRP A 60 ARG A 65 CYS A 66 PHE A 235
SITE 2 AC1 17 ASN A 236 TRP A 238 GLU A 243 TRP A 329
SITE 3 AC1 17 TYR A 355 TYR A 357 H4B A 902 6E5 A 904
SITE 4 AC1 17 HOH A2068 HOH A2246 HOH A2363 HOH A2364
SITE 5 AC1 17 HOH A2365
SITE 1 AC2 12 ARG A 247 TRP A 327 THR A 328 TRP A 329
SITE 2 AC2 12 PHE A 342 HIS A 343 ARG A 344 HEM A 901
SITE 3 AC2 12 HOH A2073 HOH A2335 HOH A2338 HOH A2364
SITE 1 AC3 4 GLN A 129 ARG A 132 TYR A 239 ASN A 248
SITE 1 AC4 16 ILE A 125 TRP A 126 HIS A 128 ALA A 147
SITE 2 AC4 16 PRO A 216 ILE A 218 ASP A 220 PHE A 235
SITE 3 AC4 16 ASN A 236 GLY A 237 TRP A 238 GLU A 243
SITE 4 AC4 16 GLN A 358 LYS A 360 HEM A 901 HOH A2044
SITE 1 AC5 9 GLY A 159 TRP A 160 ARG A 161 TRP A 238
SITE 2 AC5 9 SER A 298 ILE A 299 GLN A 308 HOH A2174
SITE 3 AC5 9 HOH A2306
CRYST1 80.340 95.220 63.000 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 0.012447 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015873 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
