HEADER OXIDOREDUCTASE 23-OCT-14 4D3O
TITLE STRUCTURE OF BACILLUS SUBTILIS NITRIC OXIDE SYNTHASE IN COMPLEX WITH
TITLE 2 6-(3-(2-(1H-PYRROLO(2,3-B)PYRIDIN-6-YL)ETHYL)-5-(AMINOMETHYL)
TITLE 3 PHENETHYL)-4-METHYLPYRIDIN-2-AMINE
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 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 4D3O 1 REMARK
REVDAT 4 06-FEB-19 4D3O 1 REMARK
REVDAT 3 30-JAN-19 4D3O 1 REMARK
REVDAT 2 04-FEB-15 4D3O 1 JRNL
REVDAT 1 14-JAN-15 4D3O 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. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 36318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1852
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 46.7407 - 4.4664 0.98 2853 160 0.1693 0.2031
REMARK 3 2 4.4664 - 3.5455 0.98 2758 148 0.1376 0.1735
REMARK 3 3 3.5455 - 3.0974 0.99 2738 141 0.1518 0.1894
REMARK 3 4 3.0974 - 2.8143 0.98 2707 127 0.1529 0.1831
REMARK 3 5 2.8143 - 2.6126 0.97 2676 123 0.1612 0.2245
REMARK 3 6 2.6126 - 2.4586 0.96 2617 149 0.1653 0.1973
REMARK 3 7 2.4586 - 2.3354 0.96 2593 162 0.1716 0.2263
REMARK 3 8 2.3354 - 2.2338 0.95 2575 149 0.1765 0.2297
REMARK 3 9 2.2338 - 2.1478 0.95 2579 136 0.1881 0.2279
REMARK 3 10 2.1478 - 2.0737 0.97 2641 139 0.1851 0.2106
REMARK 3 11 2.0737 - 2.0088 0.97 2641 125 0.1990 0.2423
REMARK 3 12 2.0088 - 1.9514 0.97 2574 133 0.2097 0.2376
REMARK 3 13 1.9514 - 1.9000 0.93 2514 160 0.2452 0.3337
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.960
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.18
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 : 0.007 3120
REMARK 3 ANGLE : 1.270 4243
REMARK 3 CHIRALITY : 0.074 435
REMARK 3 PLANARITY : 0.004 542
REMARK 3 DIHEDRAL : 13.977 1160
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): 5.6999 19.4395 23.0168
REMARK 3 T TENSOR
REMARK 3 T11: 0.1309 T22: 0.1220
REMARK 3 T33: 0.1118 T12: -0.0109
REMARK 3 T13: 0.0018 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 1.1226 L22: 1.5904
REMARK 3 L33: 1.1212 L12: 0.2112
REMARK 3 L13: 0.1396 L23: -0.3039
REMARK 3 S TENSOR
REMARK 3 S11: -0.0609 S12: 0.1362 S13: 0.0712
REMARK 3 S21: -0.2189 S22: 0.0606 S23: -0.0110
REMARK 3 S31: -0.0809 S32: 0.0598 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 4D3O 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_1290062084.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-14
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 : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999978
REMARK 200 MONOCHROMATOR : SI(111)
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 : 37512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 49.210
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
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 DATASET AT 0.991 CC ONE HALF FOR HIGH
REMARK 200 RESOLUTION SHELL AT 0.868
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
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 39.92650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.72650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.92650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.72650
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: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.9 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 A2302 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 363 CA C O CB CG CD OE1
REMARK 470 GLU A 363 OE2
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 -75.73 -107.07
REMARK 500 LYS A 118 37.30 -94.63
REMARK 500 ALA A 233 71.51 -154.43
REMARK 500 ARG A 247 -65.98 -126.88
REMARK 500 ARG A 254 -125.69 -119.96
REMARK 500 ASN A 348 31.86 -88.09
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 A2095 DISTANCE = 6.05 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 96.8
REMARK 620 3 HEM A 901 NB 91.1 87.2
REMARK 620 4 HEM A 901 NC 93.9 168.7 89.0
REMARK 620 5 HEM A 901 ND 102.3 89.7 166.5 91.5
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 S97 A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POL 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 GOL A 907
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
DBREF 4D3O A 1 363 UNP O34453 NOSO_BACSU 1 363
SEQADV 4D3O ALA A 25 UNP O34453 GLU 25 ENGINEERED MUTATION
SEQADV 4D3O ALA A 26 UNP O34453 GLU 26 ENGINEERED MUTATION
SEQADV 4D3O 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 S97 A 904 29
HET POL A 905 4
HET GOL A 906 6
HET GOL A 907 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM CL CHLORIDE ION
HETNAM S97 6-(2-{3-(AMINOMETHYL)-5-[2-(1H-PYRROLO[2,3-B]PYRIDIN-6-
HETNAM 2 S97 YL)ETHYL]PHENYL}ETHYL)-4-METHYLPYRIDIN-2-AMINE
HETNAM POL N-PROPANOL
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN POL 1-PROPONOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 HEM C34 H32 FE N4 O4
FORMUL 3 CL CL 1-
FORMUL 4 S97 C24 H27 N5
FORMUL 5 POL C3 H8 O
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 HOH *322(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 GLU A 157 1 10
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 GLN A 295 1 21
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 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 2.48
CISPEP 1 LYS A 352 PRO A 353 0 0.14
SITE 1 AC1 17 TRP A 60 ARG A 65 CYS A 66 ILE A 67
SITE 2 AC1 17 PHE A 235 ASN A 236 GLY A 237 TRP A 238
SITE 3 AC1 17 GLU A 243 TRP A 329 TYR A 355 TYR A 357
SITE 4 AC1 17 S97 A 904 HOH A2043 HOH A2051 HOH A2319
SITE 5 AC1 17 HOH A2320
SITE 1 AC2 4 GLN A 129 TYR A 239 ASN A 248 POL A 905
SITE 1 AC3 14 HIS A 128 ILE A 218 PHE A 235 GLY A 237
SITE 2 AC3 14 TRP A 238 GLU A 243 ARG A 247 THR A 328
SITE 3 AC3 14 TRP A 329 PHE A 342 TYR A 357 HEM A 901
SITE 4 AC3 14 POL A 905 HOH A2321
SITE 1 AC4 5 GLU A 243 ARG A 247 ASN A 248 CL A 903
SITE 2 AC4 5 S97 A 904
SITE 1 AC5 10 GLU A 156 TRP A 160 ARG A 161 TRP A 238
SITE 2 AC5 10 SER A 298 ILE A 299 HOH A2150 HOH A2153
SITE 3 AC5 10 HOH A2270 HOH A2322
SITE 1 AC6 8 ARG A 142 GLY A 144 ASP A 166 TYR A 255
SITE 2 AC6 8 LYS A 257 HOH A2134 HOH A2229 HOH A2234
CRYST1 79.853 93.453 62.483 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 0.012523 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016004 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
