HEADER OXIDOREDUCTASE 23-OCT-14 4D3T
TITLE STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH
TITLE 2 N-{3-[(1S)-2-(3-{(Z)-[AMINO(THIOPHEN-2-YL)METHYLIDENE]AMINO}PHENOXY)-
TITLE 3 1-HYDROXYETHYL]PHENYL}THIOPHENE-2-CARBOXIMIDAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE OXYGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NOSOXY-LIKE PROTEIN;
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 SUBSP. SUBTILIS STR. 168;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 ATCC: 23857;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28A
KEYWDS OXIDOREDUCTASE, INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.HOLDEN,T.L.POULOS
REVDAT 5 20-DEC-23 4D3T 1 REMARK
REVDAT 4 06-FEB-19 4D3T 1 REMARK
REVDAT 3 30-JAN-19 4D3T 1 REMARK
REVDAT 2 04-FEB-15 4D3T 1 JRNL
REVDAT 1 14-JAN-15 4D3T 0
JRNL AUTH J.K.HOLDEN,S.KANG,S.A.HOLLINGSWORTH,H.LI,N.LIM,S.CHEN,
JRNL AUTH 2 H.HUANG,F.XUE,W.TANG,R.B.SILVERMAN,T.L.POULOS
JRNL TITL STRUCTURE-BASED DESIGN OF BACTERIAL NITRIC OXIDE SYNTHASE
JRNL TITL 2 INHIBITORS.
JRNL REF J.MED.CHEM. V. 58 994 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 25522110
JRNL DOI 10.1021/JM501723P
REMARK 2
REMARK 2 RESOLUTION. 1.55 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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 68910
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3514
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 37.0355 - 4.5296 0.98 2829 158 0.1607 0.1876
REMARK 3 2 4.5296 - 3.5962 0.96 2655 143 0.1463 0.1658
REMARK 3 3 3.5962 - 3.1419 0.98 2677 137 0.1678 0.1840
REMARK 3 4 3.1419 - 2.8548 0.99 2676 131 0.1695 0.1911
REMARK 3 5 2.8548 - 2.6502 0.97 2642 120 0.1727 0.2088
REMARK 3 6 2.6502 - 2.4940 0.98 2626 142 0.1607 0.1850
REMARK 3 7 2.4940 - 2.3691 0.98 2599 172 0.1676 0.1941
REMARK 3 8 2.3691 - 2.2660 0.98 2625 153 0.1662 0.1990
REMARK 3 9 2.2660 - 2.1788 0.97 2576 139 0.1889 0.1740
REMARK 3 10 2.1788 - 2.1036 0.97 2596 131 0.1858 0.1981
REMARK 3 11 2.1036 - 2.0378 0.97 2630 126 0.1973 0.2256
REMARK 3 12 2.0378 - 1.9796 0.98 2620 135 0.1772 0.2005
REMARK 3 13 1.9796 - 1.9275 0.99 2614 148 0.1954 0.2289
REMARK 3 14 1.9275 - 1.8805 0.98 2592 139 0.2381 0.2874
REMARK 3 15 1.8805 - 1.8377 0.99 2592 166 0.2094 0.2514
REMARK 3 16 1.8377 - 1.7986 0.99 2605 145 0.2094 0.2160
REMARK 3 17 1.7986 - 1.7626 0.99 2629 141 0.2400 0.2494
REMARK 3 18 1.7626 - 1.7294 0.98 2613 120 0.2394 0.3001
REMARK 3 19 1.7294 - 1.6985 0.98 2564 141 0.2506 0.2584
REMARK 3 20 1.6985 - 1.6697 0.99 2660 136 0.2641 0.2690
REMARK 3 21 1.6697 - 1.6428 0.99 2606 126 0.2922 0.2973
REMARK 3 22 1.6428 - 1.6175 0.99 2620 143 0.3099 0.3056
REMARK 3 23 1.6175 - 1.5937 0.99 2634 133 0.3255 0.3525
REMARK 3 24 1.5937 - 1.5712 0.97 2535 157 0.3636 0.3550
REMARK 3 25 1.5712 - 1.5500 0.90 2381 132 0.4074 0.3737
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.57
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 : 0.006 3133
REMARK 3 ANGLE : 1.247 4248
REMARK 3 CHIRALITY : 0.070 437
REMARK 3 PLANARITY : 0.004 543
REMARK 3 DIHEDRAL : 13.766 1161
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): 5.7958 19.5079 23.0066
REMARK 3 T TENSOR
REMARK 3 T11: 0.2477 T22: 0.2087
REMARK 3 T33: 0.2961 T12: -0.0225
REMARK 3 T13: 0.0291 T23: -0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.8413 L22: 1.7011
REMARK 3 L33: 1.0101 L12: 0.2760
REMARK 3 L13: 0.1830 L23: -0.2899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0769 S12: 0.1328 S13: 0.0685
REMARK 3 S21: -0.2657 S22: 0.0816 S23: -0.0867
REMARK 3 S31: -0.1256 S32: 0.0934 S33: -0.0010
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 4D3T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1290062085.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69172
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 37.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
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 4LWA
REMARK 200
REMARK 200 REMARK: CC ONE HALF FOR FULL DATA SET AT 0.999 CC ONE HALF FOR
REMARK 200 HIGH RESOLUTION SHELL AT 0.601 RMERGE FOR HIGH RESOLUTION SHELL
REMARK 200 AT 2.151
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
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 40.21050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.45750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.21050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.45750
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: 9180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.6 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 A2283 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 -67.46 -95.12
REMARK 500 SER A 138 132.22 -170.11
REMARK 500 ALA A 233 70.29 -158.52
REMARK 500 ARG A 247 -68.79 -132.29
REMARK 500 ARG A 254 -126.23 -116.71
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 98.6
REMARK 620 3 HEM A 901 NB 94.5 86.7
REMARK 620 4 HEM A 901 NC 95.3 165.6 88.4
REMARK 620 5 HEM A 901 ND 101.5 89.9 164.0 91.1
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 CL A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFQ A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 909
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 910
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 913
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D3I RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-((5-(AMINOMETHYL)-1,3-PHENYLENE) BIS(ETHANE-2,1-DIYL))
REMARK 900 BIS(4-METHYLPYRIDIN-2-AMINE)
REMARK 900 RELATED ID: 4D3J RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-(2,2'-(5-AMINO-1,3-PHENYLENE) BIS(ETHANE-2,1-DIYL))BIS(4-
REMARK 900 METHYLPYRIDIN-2-AMINE)
REMARK 900 RELATED ID: 4D3K RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6,6'-((5-(3-AMINOPROPYL)-1,3- PHENYLENE)BIS(ETHANE-2,1-DIYL))
REMARK 900 BIS(4-METHYLPYRIDIN-2 -AMINE)
REMARK 900 RELATED ID: 4D3M 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-(2-(4-METHYL-6-
REMARK 900 (METHYLAMINO)PYRIDIN-2-YL) ETHYL)BENZONITRILE
REMARK 900 RELATED ID: 4D3N 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-((2-(PYRIDIN-2-YL)
REMARK 900 ETHYL)AMINO)BENZONITRILE
REMARK 900 RELATED ID: 4D3O RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX
REMARK 900 WITH 6-(3-(2-(1H-PYRROLO(2,3-B)PYRIDIN- 6-YL)ETHYL)-5-(AMINOMETHYL)
REMARK 900 PHENETHYL)-4-METHYLPYRIDIN- 2-AMINE
REMARK 900 RELATED ID: 4D3U RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE H128S IN
REMARK 900 COMPLEX WITH (S)-N-(3-(1-HYDROXY-2-(3-( THIOPHENE-2-CARBOXIMIDAMIDO)
REMARK 900 PHENOXY)ETHYL)PHENYL)THIOPHENE -2-CARBOXIMIDAMIDE
REMARK 900 RELATED ID: 4D3V RELATED DB: PDB
REMARK 900 STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE I218V IN
REMARK 900 COMPLEX WITH (S)-N-(3-(1-HYDROXY-2-(3-( THIOPHENE-2-CARBOXIMIDAMIDO)
REMARK 900 PHENOXY)ETHYL)PHENYL)THIOPHENE -2-CARBOXIMIDAMIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MUTATIONS E25A, E26A, AND E316A INTRODUCED
DBREF 4D3T A 1 363 UNP O34453 NOSO_BACSU 1 363
SEQADV 4D3T ALA A 25 UNP O34453 GLU 25 ENGINEERED MUTATION
SEQADV 4D3T ALA A 26 UNP O34453 GLU 26 ENGINEERED MUTATION
SEQADV 4D3T 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 CL A 903 1
HET RFQ A 904 32
HET GOL A 905 6
HET GOL A 906 6
HET POL A 907 4
HET POL A 908 4
HET GOL A 909 6
HET GOL A 910 6
HET GOL A 913 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CL CHLORIDE ION
HETNAM RFQ N-{3-[(1S)-2-(3-{(Z)-[AMINO(THIOPHEN-2-YL)
HETNAM 2 RFQ METHYLIDENE]AMINO}PHENOXY)-1-
HETNAM 3 RFQ HYDROXYETHYL]PHENYL}THIOPHENE-2-CARBOXIMIDAMIDE
HETNAM GOL GLYCEROL
HETNAM POL N-PROPANOL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN POL 1-PROPONOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CL CL 1-
FORMUL 4 RFQ C24 H21 N4 O2 S2
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 7 POL 2(C3 H8 O)
FORMUL 12 HOH *309(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 GLY A 320 1 20
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 THR A 339 ARG A 344 5 6
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 -1.84
SITE 1 AC1 17 TRP A 60 SER A 63 ARG A 65 CYS A 66
SITE 2 AC1 17 PHE A 235 ASN A 236 TRP A 238 GLU A 243
SITE 3 AC1 17 TRP A 329 TYR A 355 TYR A 357 RFQ A 904
SITE 4 AC1 17 GOL A 906 POL A 907 HOH A2300 HOH A2301
SITE 5 AC1 17 HOH A2302
SITE 1 AC2 4 GLN A 129 TYR A 239 ASN A 248 POL A 907
SITE 1 AC3 18 HIS A 128 PRO A 216 ILE A 218 PHE A 235
SITE 2 AC3 18 ASN A 236 GLY A 237 TRP A 238 GLU A 243
SITE 3 AC3 18 ARG A 247 TRP A 327 THR A 328 TRP A 329
SITE 4 AC3 18 PHE A 342 HEM A 901 POL A 907 HOH A2114
SITE 5 AC3 18 HOH A2300 HOH A2303
SITE 1 AC4 10 GLU A 156 TRP A 160 ARG A 161 TRP A 238
SITE 2 AC4 10 SER A 298 ILE A 299 HOH A2140 HOH A2142
SITE 3 AC4 10 HOH A2256 HOH A2305
SITE 1 AC5 6 MET A 221 TYR A 355 PHE A 356 TYR A 357
SITE 2 AC5 6 HEM A 901 HOH A2306
SITE 1 AC6 7 GLU A 243 ARG A 247 ASN A 248 HEM A 901
SITE 2 AC6 7 CL A 903 RFQ A 904 HOH A2302
SITE 1 AC7 3 GLY A 144 ASP A 166 LYS A 257
SITE 1 AC8 6 VAL A 183 TRP A 184 ASP A 270 ASN A 272
SITE 2 AC8 6 HOH A2160 HOH A2235
SITE 1 AC9 8 TRP A 327 THR A 328 ARG A 344 SER A 345
SITE 2 AC9 8 HOH A2040 HOH A2041 HOH A2293 HOH A2308
SITE 1 BC1 5 TYR A 136 SER A 138 GLU A 141 ILE A 143
SITE 2 BC1 5 ARG A 164
CRYST1 80.421 94.915 62.859 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 0.012435 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015909 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
